Nutrient chapter

Agmatine Sulfate

Sulfate salt of agmatine; PubChem CID 2794990, 1:1 composition, molecular formula C5H16N4O4S and molecular weight 228.27 g/mol. Salt mass is not free-agmatine mass. Not an established essential nutrient.

59 recorded mechanisms · 5 availability situations · 5 preserved sources. Draft and verified records are labeled separately.

Read recorded mechanisms Open recursive mind map

The mechanisms

What the sources say this nutrient does, one relationship at a time. Plain wording comes first; the technical statement follows.

Human OCT1 expression increased concentration-dependent agmatine transport in HEK293 cells, with Km 18.73 ± 4.86 mM.
Human organic cation transporter 1 / OCT1 / SLC22A1 → Agmatine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human transporter expressed in HEK293 cells; radiolabeled agmatine.
limitations
An in vitro Km is not a target blood concentration or oral bioavailability estimate.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A transporter can admit the molecule, but its affinity matters.
primary_references
OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
transport_effect
raises Expression increased concentration-dependent agmatine transport into HEK293 cells.
transport_pool
the expressing cell Expression increased concentration-dependent agmatine transport into HEK293 cells.
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 20–26
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transporter expressed in HEK293 cells; radiolabeled agmatine. · source_derived_draft · unverified_draft
## agmatine-sulfate-oct1 A transporter can admit the molecule, but its affinity matters. Human OCT1 expression increased concentration-dependent agmatine transport in HEK293 cells, with Km 18.73 ± 4.86 mM. Model: Human transporter expressed in HEK293 cells; radiolabeled agmatine. Limitations: An in vitro Km is not a target blood concentration or oral bioavailability estimate. Evidence access: Primary abstract OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
Complete structured claim and evidence
Human OCT2 mediated pH- and concentration-dependent agmatine transport, with Km 1.84 ± 0.38 mM.
Human organic cation transporter 2 / OCT2 / SLC22A2 → Agmatine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Matched human transporter expression systems.
limitations
Protein expression and assay conditions affect comparison with actual kidney clearance.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Another organic-cation transporter handles agmatine more avidly in this assay.
primary_references
OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
transport_effect
raises pH- and concentration-dependent agmatine transport into the expressing cell.
transport_pool
the expressing cell pH- and concentration-dependent agmatine transport into the expressing cell.
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 28–34
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Matched human transporter expression systems. · source_derived_draft · unverified_draft
## agmatine-sulfate-oct2 Another organic-cation transporter handles agmatine more avidly in this assay. Human OCT2 mediated pH- and concentration-dependent agmatine transport, with Km 1.84 ± 0.38 mM. Model: Matched human transporter expression systems. Limitations: Protein expression and assay conditions affect comparison with actual kidney clearance. Evidence access: Primary abstract OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
Complete structured claim and evidence
Human MATE1 expression increased saturable agmatine accumulation, with Km 240 ± 31 micromolar.
Human multidrug and toxin extrusion protein 1 / MATE1 / SLC47A1 → Agmatine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human MATE1 in HEK293 cells.
limitations
Accumulation direction in the assay is not identical to net secretion across an intact kidney.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A transporter associated with renal secretion recognizes agmatine.
primary_references
OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
transport_effect
raises Expression increased saturable agmatine accumulation in the cell.
transport_pool
the expressing cell Expression increased saturable agmatine accumulation in the cell.
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 36–42
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human MATE1 in HEK293 cells. · source_derived_draft · unverified_draft
## agmatine-sulfate-mate1 A transporter associated with renal secretion recognizes agmatine. Human MATE1 expression increased saturable agmatine accumulation, with Km 240 ± 31 micromolar. Model: Human MATE1 in HEK293 cells. Limitations: Accumulation direction in the assay is not identical to net secretion across an intact kidney. Evidence access: Primary abstract OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
Complete structured claim and evidence
An inward proton gradient trans-stimulated efflux of intracellular agmatine from MATE1-expressing cells.
Inward proton gradient in the human MATE1 agmatine assay → Human MATE1-dependent agmatine efflux source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human MATE1 expression; radiotracer efflux experiment.
limitations
This does not prescribe changing systemic pH.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
The gradient helps determine transport direction.
primary_references
OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 44–50
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human MATE1 expression; radiotracer efflux experiment. · source_derived_draft · unverified_draft
## agmatine-sulfate-mate1-proton The gradient helps determine transport direction. An inward proton gradient trans-stimulated efflux of intracellular agmatine from MATE1-expressing cells. Model: Human MATE1 expression; radiotracer efflux experiment. Limitations: This does not prescribe changing systemic pH. Evidence access: Primary abstract OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
Complete structured claim and evidence
Polyamines inhibited MATE1-mediated agmatine transport, whereas L-arginine did not inhibit it in the tested system.
Polyamine competitor pool in the human MATE1 agmatine assay → Human MATE1-mediated agmatine transport source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human MATE1-expressing HEK293 cells.
limitations
The primary abstract groups the polyamine competitors; no individual potency rank is assigned.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A shared precursor is not necessarily a transport competitor.
primary_references
OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 52–58
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human MATE1-expressing HEK293 cells. · source_derived_draft · unverified_draft
## agmatine-sulfate-polyamine-competition A shared precursor is not necessarily a transport competitor. Polyamines inhibited MATE1-mediated agmatine transport, whereas L-arginine did not inhibit it in the tested system. Model: Human MATE1-expressing HEK293 cells. Limitations: The primary abstract groups the polyamine competitors; no individual potency rank is assigned. Evidence access: Primary abstract OCT2 and MATE1 provide bidirectional agmatine transport. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21128598/ · DOI 10.1021/mp100180a
Complete structured claim and evidence
Transformed mouse NIH/3T3 cells took up agmatine through an energy- and membrane-potential-dependent saturable system with apparent Km 2.5 micromolar.
Mouse transformed NIH/3T3 polyamine transport system → Agmatine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Mouse transformed fibroblast transport experiments.
limitations
The molecular transporter gene was not identified; this system is not automatically OCT2 or MATE1.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Different cells can have much higher-affinity uptake than a single recombinant transporter.
primary_references
Polyamine transport system mediates agmatine transport in mammalian cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11401856/ · DOI 10.1152/ajpcell.2001.281.1.C329
transport_effect
raises Cells took up agmatine through an energy- and membrane-potential-dependent saturable system.
transport_pool
the expressing cell Cells took up agmatine through an energy- and membrane-potential-dependent saturable system.
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 60–66
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse transformed fibroblast transport experiments. · source_derived_draft · unverified_draft
## agmatine-sulfate-polyamine-carrier Different cells can have much higher-affinity uptake than a single recombinant transporter. Transformed mouse NIH/3T3 cells took up agmatine through an energy- and membrane-potential-dependent saturable system with apparent Km 2.5 micromolar. Model: Mouse transformed fibroblast transport experiments. Limitations: The molecular transporter gene was not identified; this system is not automatically OCT2 or MATE1. Evidence access: Primary abstract Polyamine transport system mediates agmatine transport in mammalian cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11401856/ · DOI 10.1152/ajpcell.2001.281.1.C329
Complete structured claim and evidence
Agmatine uptake was abrogated in a polyamine-transport-deficient human carcinoma cell line.
Human carcinoma polyamine-transport-deficient experimental cell line → Human carcinoma-cell agmatine uptake source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_access
Primary abstract
experimental_model
Human transport-deficient carcinoma cells compared with transport-capable cells.
limitations
Not an inherited human deficiency syndrome or proof of nutrient depletion.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
An extracellular supply cannot compensate for absent entry in this model.
primary_references
Polyamine transport system mediates agmatine transport in mammalian cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11401856/ · DOI 10.1152/ajpcell.2001.281.1.C329
trigger_kind
machinery_impairment Imported condition classification; unverified.
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 68–74
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transport-deficient carcinoma cells compared with transport-capable cells. · source_derived_draft · unverified_draft
## agmatine-sulfate-carrier-loss An extracellular supply cannot compensate for absent entry in this model. Agmatine uptake was abrogated in a polyamine-transport-deficient human carcinoma cell line. Model: Human transport-deficient carcinoma cells compared with transport-capable cells. Limitations: Not an inherited human deficiency syndrome or proof of nutrient depletion. Evidence access: Primary abstract Polyamine transport system mediates agmatine transport in mammalian cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11401856/ · DOI 10.1152/ajpcell.2001.281.1.C329
Complete structured claim and evidence
Rat hepatocytes exhibited high-affinity agmatine uptake with Km 0.03 mM; the system also transported putrescine but not arginine, spermidine or spermine.
Rat hepatocyte high-affinity agmatine uptake → Agmatine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Primary rat hepatocyte cultures and radiolabeled substrate.
limitations
Different selectivity from other polyamine uptake systems is a context difference, not a universal contradiction.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Competition depends on which cell and transport route is being studied.
primary_references
Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
transport_effect
raises Hepatocytes showed high-affinity agmatine uptake with a Km of 0.03 mM.
transport_pool
the hepatocyte interior Hepatocytes showed high-affinity agmatine uptake with a Km of 0.03 mM.
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 76–82
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Primary rat hepatocyte cultures and radiolabeled substrate. · source_derived_draft · unverified_draft
## agmatine-sulfate-rat-liver-uptake Competition depends on which cell and transport route is being studied. Rat hepatocytes exhibited high-affinity agmatine uptake with Km 0.03 mM; the system also transported putrescine but not arginine, spermidine or spermine. Model: Primary rat hepatocyte cultures and radiolabeled substrate. Limitations: Different selectivity from other polyamine uptake systems is a context difference, not a universal contradiction. Evidence access: Primary abstract Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
Complete structured claim and evidence
Difluoromethylornithine-induced polyamine depletion increased agmatine uptake in cultured rat hepatocytes.
Difluoromethylornithine / eflornithine → Agmatine uptake in polyamine-depleted rat hepatocytes source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_access
Primary abstract
experimental_model
Pharmacological ODC inhibition in rat hepatocyte culture.
limitations
This is experimentally induced cellular polyamine depletion, not ordinary dietary agmatine deficiency.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A depleted downstream pool can change entry of another compound.
primary_references
Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
trigger_kind
machinery_impairment Imported condition classification; unverified.
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 84–90
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Pharmacological ODC inhibition in rat hepatocyte culture. · source_derived_draft · unverified_draft
## agmatine-sulfate-depleted-polyamines A depleted downstream pool can change entry of another compound. Difluoromethylornithine-induced polyamine depletion increased agmatine uptake in cultured rat hepatocytes. Model: Pharmacological ODC inhibition in rat hepatocyte culture. Limitations: This is experimentally induced cellular polyamine depletion, not ordinary dietary agmatine deficiency. Evidence access: Primary abstract Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
Complete structured claim and evidence
About 50% of taken-up radiolabeled agmatine was recovered as 4-guanidinobutyrate in the rat hepatocyte experiment.
Agmatine → 4-Guanidinobutyrate source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat hepatocyte culture; HPLC and mass spectrometry.
limitations
The percentage is specific to this experiment and is not a human whole-body metabolic fraction.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Oxidation can redirect the molecule away from the polyamine route.
primary_references
Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 92–98
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat hepatocyte culture; HPLC and mass spectrometry. · source_derived_draft · unverified_draft
## agmatine-sulfate-rat-gba Oxidation can redirect the molecule away from the polyamine route. About 50% of taken-up radiolabeled agmatine was recovered as 4-guanidinobutyrate in the rat hepatocyte experiment. Model: Rat hepatocyte culture; HPLC and mass spectrometry. Limitations: The percentage is specific to this experiment and is not a human whole-body metabolic fraction. Evidence access: Primary abstract Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
Complete structured claim and evidence
About 10% of taken-up agmatine label entered the polyamine pool in rat hepatocyte cultures.
Agmatine → Rat hepatocyte agmatine-derived labeled polyamine pool source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Primary rat hepatocytes with radiotracer.
limitations
The abstract reports a polyamine pool, not a putrescine-only percentage or purified human AGMAT reaction.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Agmatine can feed polyamine metabolism in a defined preparation.
primary_references
Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 100–106
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Primary rat hepatocytes with radiotracer. · source_derived_draft · unverified_draft
## agmatine-sulfate-rat-polyamine-production Agmatine can feed polyamine metabolism in a defined preparation. About 10% of taken-up agmatine label entered the polyamine pool in rat hepatocyte cultures. Model: Primary rat hepatocytes with radiotracer. Limitations: The abstract reports a polyamine pool, not a putrescine-only percentage or purified human AGMAT reaction. Evidence access: Primary abstract Transport and metabolism of agmatine in rat hepatocyte cultures. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11179960/ · DOI 10.1046/j.1432-1327.2001.01955.x
Complete structured claim and evidence
Adding diamine oxidase or inhibiting aldehyde dehydrogenase increased agmatine-associated suppression of inducible NO generation; aldehyde removal or trapping attenuated it.
4-Guanidinobutyraldehyde / agmatine aldehyde → Agmatine-associated inducible NO suppression in cytokine-stimulated cultures source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cytokine-stimulated cell preparations; enzyme additions, inhibitors and aldehyde trapping.
limitations
The accessed abstract does not fully specify each cell species, dose or enzyme isoform. It supports aldehyde involvement rather than a direct binding target.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
How a compound is metabolized can change its signaling effect.
primary_references
Suppression of inducible nitric oxide generation by agmatine aldehyde: beneficial effects in sepsis. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11473357/ · DOI 10.1002/jcp.1119
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 108–114
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cytokine-stimulated cell preparations; enzyme additions, inhibitors and aldehyde trapping. · source_derived_draft · unverified_draft
## agmatine-sulfate-aldehyde-no How a compound is metabolized can change its signaling effect. Adding diamine oxidase or inhibiting aldehyde dehydrogenase increased agmatine-associated suppression of inducible NO generation; aldehyde removal or trapping attenuated it. Model: Cytokine-stimulated cell preparations; enzyme additions, inhibitors and aldehyde trapping. Limitations: The accessed abstract does not fully specify each cell species, dose or enzyme isoform. It supports aldehyde involvement rather than a direct binding target. Evidence access: Primary abstract Suppression of inducible nitric oxide generation by agmatine aldehyde: beneficial effects in sepsis. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11473357/ · DOI 10.1002/jcp.1119
Complete structured claim and evidence
Purified recombinant human AGMAT variants R105 and G105 showed no detected agmatine hydrolysis at 10 mM substrate in the 2022 assay.
Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase → Agmatine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text; Figures 1 and 2
experimental_model
Human proteins expressed in E. coli; urea assay, detection limit about 0.02 nmol/s/mg.
limitations
This assay result revises the proposed substrate assignment; it does not prove that humans cannot metabolize agmatine by other routes.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A gene name does not guarantee the biochemical reaction usually drawn beside it.
primary_references
Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 116–122
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human proteins expressed in E. coli; urea assay, detection limit about 0.02 nmol/s/mg. · source_derived_draft · unverified_draft
## agmatine-sulfate-agmat-reannotation A gene name does not guarantee the biochemical reaction usually drawn beside it. Purified recombinant human AGMAT variants R105 and G105 showed no detected agmatine hydrolysis at 10 mM substrate in the 2022 assay. Model: Human proteins expressed in E. coli; urea assay, detection limit about 0.02 nmol/s/mg. Limitations: This assay result revises the proposed substrate assignment; it does not prove that humans cannot metabolize agmatine by other routes. Evidence access: Primary full text; Figures 1 and 2 Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Complete structured claim and evidence
Both purified human AGMAT variants hydrolyzed guanidinobutyrate, supporting a guanidino-acid hydrolase function.
Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase → 4-Guanidinobutyrate source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text; Figures 2 and 3
experimental_model
Purified recombinant human R105 and G105 variants.
limitations
Measured Km values for the tested guanidino acids exceeded 50 mM; physiological substrate flux remains unresolved.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
The same protein was active when supplied a different substrate.
primary_references
Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 124–130
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified recombinant human R105 and G105 variants. · source_derived_draft · unverified_draft
## agmatine-sulfate-agmat-gba The same protein was active when supplied a different substrate. Both purified human AGMAT variants hydrolyzed guanidinobutyrate, supporting a guanidino-acid hydrolase function. Model: Purified recombinant human R105 and G105 variants. Limitations: Measured Km values for the tested guanidino acids exceeded 50 mM; physiological substrate flux remains unresolved. Evidence access: Primary full text; Figures 2 and 3 Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Complete structured claim and evidence
Human AGMAT R105 hydrolyzed taurocyamine more efficiently than guanidinobutyrate in the tested concentration range; R105 and G105 differed in substrate preferences.
Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase → Taurocyamine / guanidinotaurine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text; Figures 2 and 3
experimental_model
Purified human variants; 10 mM substrate comparison and concentration series.
limitations
This does not establish a clinically meaningful taurine deficit or a supplementation response.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A variant can alter which related metabolic pool is processed.
primary_references
Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 132–138
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human variants; 10 mM substrate comparison and concentration series. · source_derived_draft · unverified_draft
## agmatine-sulfate-agmat-taurocyamine A variant can alter which related metabolic pool is processed. Human AGMAT R105 hydrolyzed taurocyamine more efficiently than guanidinobutyrate in the tested concentration range; R105 and G105 differed in substrate preferences. Model: Purified human variants; 10 mM substrate comparison and concentration series. Limitations: This does not establish a clinically meaningful taurine deficit or a supplementation response. Evidence access: Primary full text; Figures 2 and 3 Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Complete structured claim and evidence
Expressing human AGMAT R105 in medium supplemented with 0.5 mM manganese increased its subsequent taurocyamine-hydrolysis activity approximately fourfold.
Mn2+ → Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text; Figure 3B
experimental_model
Recombinant human enzyme produced in bacterial expression culture.
limitations
This is not evidence that manganese supplements activate human agmatine breakdown; agmatine was not an accepted substrate.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Metal handling during enzyme production affects measured activity.
primary_references
Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 140–146
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzyme produced in bacterial expression culture. · source_derived_draft · unverified_draft
## agmatine-sulfate-agmat-manganese Metal handling during enzyme production affects measured activity. Expressing human AGMAT R105 in medium supplemented with 0.5 mM manganese increased its subsequent taurocyamine-hydrolysis activity approximately fourfold. Model: Recombinant human enzyme produced in bacterial expression culture. Limitations: This is not evidence that manganese supplements activate human agmatine breakdown; agmatine was not an accepted substrate. Evidence access: Primary full text; Figure 3B Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Complete structured claim and evidence
Recombinant rat-brain agmatinase-like protein catalyzed agmatine hydrolysis; its central 210-residue construct retained activity with reduced kcat.
Rat brain agmatinase-like protein / ALP experimental preparation → Agmatine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat ALP recombinant constructs and enzyme kinetics.
limitations
ALP is not interchangeable with the AGMAT gene product; no human oral exposure outcome is shown.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A distinct protein preparation can perform the reaction missing from purified human AGMAT.
primary_references
Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32531922/ · DOI 10.3390/ijms21114132
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 148–154
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat ALP recombinant constructs and enzyme kinetics. · source_derived_draft · unverified_draft
## agmatine-sulfate-rat-alp-reaction A distinct protein preparation can perform the reaction missing from purified human AGMAT. Recombinant rat-brain agmatinase-like protein catalyzed agmatine hydrolysis; its central 210-residue construct retained activity with reduced kcat. Model: Rat ALP recombinant constructs and enzyme kinetics. Limitations: ALP is not interchangeable with the AGMAT gene product; no human oral exposure outcome is shown. Evidence access: Primary abstract Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32531922/ · DOI 10.3390/ijms21114132
Complete structured claim and evidence
Rat ALP catalytic activity required manganese; D217A and specified multi-residue substitutions abolished measured agmatinase activity.
Mn2+ → Rat brain agmatinase-like protein / ALP experimental preparation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_access
Primary abstract
experimental_model
Recombinant rat protein, manganese activation and mutagenesis.
limitations
Mutations support residue importance but do not by themselves prove every proposed metal-coordination geometry.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
The metal-dependent catalytic machinery is a separate requirement from substrate supply.
primary_references
Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32531922/ · DOI 10.3390/ijms21114132
trigger_kind
machinery_impairment Imported condition classification; unverified.
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 156–162
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant rat protein, manganese activation and mutagenesis. · source_derived_draft · unverified_draft
## agmatine-sulfate-rat-alp-metal The metal-dependent catalytic machinery is a separate requirement from substrate supply. Rat ALP catalytic activity required manganese; D217A and specified multi-residue substitutions abolished measured agmatinase activity. Model: Recombinant rat protein, manganese activation and mutagenesis. Limitations: Mutations support residue importance but do not by themselves prove every proposed metal-coordination geometry. Evidence access: Primary abstract Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32531922/ · DOI 10.3390/ijms21114132
Complete structured claim and evidence
Human AGMAT expression supported growth of polyamine-biosynthesis-deficient yeast in the presence of agmatine despite absent directly measured in vitro agmatinase activity.
Human AGMAT, guanidino acid hydrolase candidate / historically annotated agmatinase → Yeast polyamine-deficient growth rescue by human AGMAT expression source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Saccharomyces cerevisiae TRY104Δspe1 complementation plus enzyme assays.
limitations
Indirect yeast rescue is retained as reported; it is not sufficient to override later direct human substrate-specificity experiments.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Growth complementation and direct enzyme catalysis answer different questions.
primary_references
Mammalian agmatinases constitute unusual members in the family of Mn2+-dependent ureahydrolases. · 2017 · https://pubmed.ncbi.nlm.nih.gov/27846445/ · DOI 10.1016/j.jinorgbio.2016.11.015
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 164–170
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Saccharomyces cerevisiae TRY104Δspe1 complementation plus enzyme assays. · source_derived_draft · unverified_draft
## agmatine-sulfate-yeast-rescue Growth complementation and direct enzyme catalysis answer different questions. Human AGMAT expression supported growth of polyamine-biosynthesis-deficient yeast in the presence of agmatine despite absent directly measured in vitro agmatinase activity. Model: Saccharomyces cerevisiae TRY104Δspe1 complementation plus enzyme assays. Limitations: Indirect yeast rescue is retained as reported; it is not sufficient to override later direct human substrate-specificity experiments. Evidence access: Primary abstract Mammalian agmatinases constitute unusual members in the family of Mn2+-dependent ureahydrolases. · 2017 · https://pubmed.ncbi.nlm.nih.gov/27846445/ · DOI 10.1016/j.jinorgbio.2016.11.015
Complete structured claim and evidence
Human ODC paralogue/AZIN2 had no intrinsic arginine-decarboxylase activity in the reported experiments.
Human antizyme inhibitor 2 / AZIN2 → Putative human AZIN2 arginine-decarboxylase activity source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human protein biochemical and cell studies.
limitations
This rejects that assignment, not every possible source of mammalian agmatine.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Do not assign a human agmatine-synthesis reaction to AZIN2 just because older names suggest it.
primary_references
Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase. · 2008 · https://pubmed.ncbi.nlm.nih.gov/17900240/ · DOI 10.1042/BJ20071004
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 172–178
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human protein biochemical and cell studies. · source_derived_draft · unverified_draft
## agmatine-sulfate-azin2-identity Do not assign a human agmatine-synthesis reaction to AZIN2 just because older names suggest it. Human ODC paralogue/AZIN2 had no intrinsic arginine-decarboxylase activity in the reported experiments. Model: Human protein biochemical and cell studies. Limitations: This rejects that assignment, not every possible source of mammalian agmatine. Evidence access: Primary abstract Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase. · 2008 · https://pubmed.ncbi.nlm.nih.gov/17900240/ · DOI 10.1042/BJ20071004
Complete structured claim and evidence
Human AZIN2 bound antizymes and counteracted AZ1-dependent suppression and degradation of ODC.
Human antizyme inhibitor 2 / AZIN2 → Human ornithine decarboxylase antizyme 1 / OAZ1 source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Yeast two-hybrid, binding, ODC activity and degradation assays.
limitations
Binding and functional inhibition were studied; no oral supplement response is inferred.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A regulatory protein can change polyamine supply without synthesizing agmatine itself.
primary_references
Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase. · 2008 · https://pubmed.ncbi.nlm.nih.gov/17900240/ · DOI 10.1042/BJ20071004
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 180–186
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Yeast two-hybrid, binding, ODC activity and degradation assays. · source_derived_draft · unverified_draft
## agmatine-sulfate-azin2-regulation A regulatory protein can change polyamine supply without synthesizing agmatine itself. Human AZIN2 bound antizymes and counteracted AZ1-dependent suppression and degradation of ODC. Model: Yeast two-hybrid, binding, ODC activity and degradation assays. Limitations: Binding and functional inhibition were studied; no oral supplement response is inferred. Evidence access: Primary abstract Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase. · 2008 · https://pubmed.ncbi.nlm.nih.gov/17900240/ · DOI 10.1042/BJ20071004
Complete structured claim and evidence
Purified human GATM transferred an amidino group from arginine to taurine, producing taurocyamine in vitro.
Human glycine amidinotransferase AGAT / GATM → Taurocyamine / guanidinotaurine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text; Figure 4B
experimental_model
Recombinant human GATM substrate comparison.
limitations
Taurine is a secondary substrate in this assay; tissue flux and clinically important depletion were not established.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Creatine-synthesis machinery also accepts a taurine-related side reaction.
primary_references
Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 188–194
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human GATM substrate comparison. · source_derived_draft · unverified_draft
## agmatine-sulfate-gatm-taurine Creatine-synthesis machinery also accepts a taurine-related side reaction. Purified human GATM transferred an amidino group from arginine to taurine, producing taurocyamine in vitro. Model: Recombinant human GATM substrate comparison. Limitations: Taurine is a secondary substrate in this assay; tissue flux and clinically important depletion were not established. Evidence access: Primary full text; Figure 4B Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Complete structured claim and evidence
Human GATM used GABA as an amidino acceptor to form guanidinobutyrate in vitro.
Human glycine amidinotransferase AGAT / GATM → 4-Guanidinobutyrate source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text; Figure 4B
experimental_model
Purified human GATM.
limitations
Presence of this route does not prove a change in brain inhibitory neurotransmission after agmatine supplementation.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
The same guanidino metabolite has another possible source besides agmatine oxidation.
primary_references
Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 196–202
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human GATM. · source_derived_draft · unverified_draft
## agmatine-sulfate-gatm-gaba The same guanidino metabolite has another possible source besides agmatine oxidation. Human GATM used GABA as an amidino acceptor to form guanidinobutyrate in vitro. Model: Purified human GATM. Limitations: Presence of this route does not prove a change in brain inhibitory neurotransmission after agmatine supplementation. Evidence access: Primary full text; Figure 4B Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Complete structured claim and evidence
Human GATM transferred the amidino group of arginine to beta-alanine, producing guanidinopropionate.
Human glycine amidinotransferase AGAT / GATM → 3-Guanidinopropionate source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text; Figure 4B
experimental_model
Recombinant human enzyme assay.
limitations
No competition magnitude with glycine or taurine in a living person was established.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Beta-alanine connects to the guanidino-acid network through a distinct reaction.
primary_references
Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 204–210
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzyme assay. · source_derived_draft · unverified_draft
## agmatine-sulfate-gatm-beta-alanine Beta-alanine connects to the guanidino-acid network through a distinct reaction. Human GATM transferred the amidino group of arginine to beta-alanine, producing guanidinopropionate. Model: Recombinant human enzyme assay. Limitations: No competition magnitude with glycine or taurine in a living person was established. Evidence access: Primary full text; Figure 4B Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Complete structured claim and evidence
Four purified human creatine-kinase isoforms phosphorylated creatine but not taurocyamine, guanidinobutyrate or guanidinopropionate at 10 mM test substrate.
Human CKB, CKM, CKMT1 and CKMT2 substrate panel → Taurocyamine / guanidinotaurine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text; Figure 4A
experimental_model
Human recombinant kinases; radiolabeled ATP and TLC; annelid taurocyamine kinase positive control.
limitations
The experimental result does not exclude every reaction at other conditions, but does not support replacing creatine.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Related guanidino compounds are not automatically interchangeable energy buffers.
primary_references
Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 212–218
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant kinases; radiolabeled ATP and TLC; annelid taurocyamine kinase positive control. · source_derived_draft · unverified_draft
## agmatine-sulfate-creatine-specificity Related guanidino compounds are not automatically interchangeable energy buffers. Four purified human creatine-kinase isoforms phosphorylated creatine but not taurocyamine, guanidinobutyrate or guanidinopropionate at 10 mM test substrate. Model: Human recombinant kinases; radiolabeled ATP and TLC; annelid taurocyamine kinase positive control. Limitations: The experimental result does not exclude every reaction at other conditions, but does not support replacing creatine. Evidence access: Primary full text; Figure 4A Guanidino acid hydrolysis by the human enzyme annotated as agmatinase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36543883/ · DOI 10.1038/s41598-022-26655-4
Complete structured claim and evidence
Agmatine competitively inhibited the brain-derived NOS I preparation with approximate Ki 660 micromolar and was not an NO precursor.
Agmatine → Brain-derived NOS I in the 1996 agmatine assay, species unverified source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
NOS activity measured by nitrite or citrulline production; species not specified in accessed abstract.
limitations
Isolated-preparation potency does not quantify inhibition after an oral sulfate dose.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
An arginine-related compound can inhibit the enzyme rather than supply its product.
primary_references
Inhibition of mammalian nitric oxide synthases by agmatine, an endogenous polyamine formed by decarboxylation of arginine. · 1996 · https://pubmed.ncbi.nlm.nih.gov/8645212/ · DOI 10.1042/bj3160247
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 220–226
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · NOS activity measured by nitrite or citrulline production; species not specified in accessed abstract. · source_derived_draft · unverified_draft
## agmatine-sulfate-nos1-inhibition An arginine-related compound can inhibit the enzyme rather than supply its product. Agmatine competitively inhibited the brain-derived NOS I preparation with approximate Ki 660 micromolar and was not an NO precursor. Model: NOS activity measured by nitrite or citrulline production; species not specified in accessed abstract. Limitations: Isolated-preparation potency does not quantify inhibition after an oral sulfate dose. Evidence access: Primary abstract Inhibition of mammalian nitric oxide synthases by agmatine, an endogenous polyamine formed by decarboxylation of arginine. · 1996 · https://pubmed.ncbi.nlm.nih.gov/8645212/ · DOI 10.1042/bj3160247
Complete structured claim and evidence
Agmatine competitively inhibited macrophage-derived NOS II with approximate Ki 220 micromolar.
Agmatine → Macrophage-derived NOS II in the 1996 agmatine assay, species unverified source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Macrophage NOS preparation; enzymatic activity assay.
limitations
This is not a universal inflammatory-cell response or a human concentration target.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
NOS isoforms showed different assay sensitivities.
primary_references
Inhibition of mammalian nitric oxide synthases by agmatine, an endogenous polyamine formed by decarboxylation of arginine. · 1996 · https://pubmed.ncbi.nlm.nih.gov/8645212/ · DOI 10.1042/bj3160247
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 228–234
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Macrophage NOS preparation; enzymatic activity assay. · source_derived_draft · unverified_draft
## agmatine-sulfate-nos2-inhibition NOS isoforms showed different assay sensitivities. Agmatine competitively inhibited macrophage-derived NOS II with approximate Ki 220 micromolar. Model: Macrophage NOS preparation; enzymatic activity assay. Limitations: This is not a universal inflammatory-cell response or a human concentration target. Evidence access: Primary abstract Inhibition of mammalian nitric oxide synthases by agmatine, an endogenous polyamine formed by decarboxylation of arginine. · 1996 · https://pubmed.ncbi.nlm.nih.gov/8645212/ · DOI 10.1042/bj3160247
Complete structured claim and evidence
Agmatine competitively inhibited endothelial-derived NOS III only at a much higher approximate Ki of 7.5 mM in the isoform comparison.
Agmatine → Endothelial-derived NOS III in the 1996 agmatine assay, species unverified source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Endothelial NOS enzyme preparation.
limitations
This enzyme result is distinct from upstream signaling in intact endothelial cells.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Direct inhibition of one isoform can require a very different concentration.
primary_references
Inhibition of mammalian nitric oxide synthases by agmatine, an endogenous polyamine formed by decarboxylation of arginine. · 1996 · https://pubmed.ncbi.nlm.nih.gov/8645212/ · DOI 10.1042/bj3160247
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 236–242
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Endothelial NOS enzyme preparation. · source_derived_draft · unverified_draft
## agmatine-sulfate-nos3-inhibition Direct inhibition of one isoform can require a very different concentration. Agmatine competitively inhibited endothelial-derived NOS III only at a much higher approximate Ki of 7.5 mM in the isoform comparison. Model: Endothelial NOS enzyme preparation. Limitations: This enzyme result is distinct from upstream signaling in intact endothelial cells. Evidence access: Primary abstract Inhibition of mammalian nitric oxide synthases by agmatine, an endogenous polyamine formed by decarboxylation of arginine. · 1996 · https://pubmed.ncbi.nlm.nih.gov/8645212/ · DOI 10.1042/bj3160247
Complete structured claim and evidence
Agmatine induced cytosolic calcium transients in bovine pulmonary artery endothelial cells; repeated exposure downregulated the response.
Agmatine → Bovine pulmonary-endothelial cytosolic calcium transients source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cultured bovine pulmonary artery endothelial cells.
limitations
Dose was not available in the accessed abstract; no dietary calcium-depletion claim is made.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
The compound can change the activating signal upstream of an enzyme.
primary_references
Agmatine activation of nitric oxide synthase in endothelial cells. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9010916/
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 244–250
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cultured bovine pulmonary artery endothelial cells. · source_derived_draft · unverified_draft
## agmatine-sulfate-endothelial-calcium The compound can change the activating signal upstream of an enzyme. Agmatine induced cytosolic calcium transients in bovine pulmonary artery endothelial cells; repeated exposure downregulated the response. Model: Cultured bovine pulmonary artery endothelial cells. Limitations: Dose was not available in the accessed abstract; no dietary calcium-depletion claim is made. Evidence access: Primary abstract Agmatine activation of nitric oxide synthase in endothelial cells. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9010916/
Complete structured claim and evidence
Agmatine increased nitrite production about threefold in bovine endothelial cells; idazoxan inhibited the effect whereas yohimbine did not.
Agmatine → Bovine pulmonary-endothelial nitrite output source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Bovine endothelial culture; pharmacological antagonist comparison.
limitations
The imidazoline-associated mechanism is pharmacologically inferred; a specific receptor gene was not established.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
An intact-cell signaling effect can differ from direct enzyme inhibition.
primary_references
Agmatine activation of nitric oxide synthase in endothelial cells. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9010916/
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 252–258
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Bovine endothelial culture; pharmacological antagonist comparison. · source_derived_draft · unverified_draft
## agmatine-sulfate-endothelial-no An intact-cell signaling effect can differ from direct enzyme inhibition. Agmatine increased nitrite production about threefold in bovine endothelial cells; idazoxan inhibited the effect whereas yohimbine did not. Model: Bovine endothelial culture; pharmacological antagonist comparison. Limitations: The imidazoline-associated mechanism is pharmacologically inferred; a specific receptor gene was not established. Evidence access: Primary abstract Agmatine activation of nitric oxide synthase in endothelial cells. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9010916/
Complete structured claim and evidence
Extracellular agmatine blocked NMDA currents in rat hippocampal neurons in a voltage- and concentration-dependent manner; estimated pore-site Kd was 952 micromolar at 0 mV.
Agmatine → Rat NMDA-type glutamate receptors, subunits unresolved source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cultured rat hippocampal neurons; whole-cell patch clamp.
limitations
The inferred pore site is not a solved binding structure or measured oral human brain exposure.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Its glutamate-receptor effect depends on electrical conditions and concentration.
primary_references
Agmatine selectively blocks the N-methyl-D-aspartate subclass of glutamate receptor channels in rat hippocampal neurons. · 1999 · https://pubmed.ncbi.nlm.nih.gov/9918557/
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 260–266
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cultured rat hippocampal neurons; whole-cell patch clamp. · source_derived_draft · unverified_draft
## agmatine-sulfate-nmda-block Its glutamate-receptor effect depends on electrical conditions and concentration. Extracellular agmatine blocked NMDA currents in rat hippocampal neurons in a voltage- and concentration-dependent manner; estimated pore-site Kd was 952 micromolar at 0 mV. Model: Cultured rat hippocampal neurons; whole-cell patch clamp. Limitations: The inferred pore site is not a solved binding structure or measured oral human brain exposure. Evidence access: Primary abstract Agmatine selectively blocks the N-methyl-D-aspartate subclass of glutamate receptor channels in rat hippocampal neurons. · 1999 · https://pubmed.ncbi.nlm.nih.gov/9918557/
Complete structured claim and evidence
Spermine still potentiated NMDA current in the presence of agmatine, supporting distinct interaction sites for the two compounds.
Spermine → Rat NMDA-type glutamate receptors, subunits unresolved source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat hippocampal-neuron electrophysiology.
limitations
This is a cellular interaction, not evidence that co-supplementation is beneficial.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Two connected polyamine-related molecules can push the same channel in different directions.
primary_references
Agmatine selectively blocks the N-methyl-D-aspartate subclass of glutamate receptor channels in rat hippocampal neurons. · 1999 · https://pubmed.ncbi.nlm.nih.gov/9918557/
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 268–274
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat hippocampal-neuron electrophysiology. · source_derived_draft · unverified_draft
## agmatine-sulfate-spermine-nmda Two connected polyamine-related molecules can push the same channel in different directions. Spermine still potentiated NMDA current in the presence of agmatine, supporting distinct interaction sites for the two compounds. Model: Rat hippocampal-neuron electrophysiology. Limitations: This is a cellular interaction, not evidence that co-supplementation is beneficial. Evidence access: Primary abstract Agmatine selectively blocks the N-methyl-D-aspartate subclass of glutamate receptor channels in rat hippocampal neurons. · 1999 · https://pubmed.ncbi.nlm.nih.gov/9918557/
Complete structured claim and evidence
Putrescine had little NMDA-blocking effect compared with agmatine or arcaine in the same experiments.
Putrescine → Rat NMDA-type glutamate receptors, subunits unresolved source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat neuron comparison of guanidine-containing and diamine compounds.
limitations
The result supports structural specificity; it does not measure metabolic conversion during recording.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Converting agmatine to a related amine can change channel activity.
primary_references
Agmatine selectively blocks the N-methyl-D-aspartate subclass of glutamate receptor channels in rat hippocampal neurons. · 1999 · https://pubmed.ncbi.nlm.nih.gov/9918557/
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat neuron comparison of guanidine-containing and diamine compounds. · source_derived_draft · unverified_draft
## agmatine-sulfate-putrescine-nmda Converting agmatine to a related amine can change channel activity. Putrescine had little NMDA-blocking effect compared with agmatine or arcaine in the same experiments. Model: Rat neuron comparison of guanidine-containing and diamine compounds. Limitations: The result supports structural specificity; it does not measure metabolic conversion during recording. Evidence access: Primary abstract Agmatine selectively blocks the N-methyl-D-aspartate subclass of glutamate receptor channels in rat hippocampal neurons. · 1999 · https://pubmed.ncbi.nlm.nih.gov/9918557/
Complete structured claim and evidence
Agmatine bound human platelet I1 sites with high- and low-affinity components and preferential affinity for the high-affinity I1 component over tested alpha-2 subtypes.
Agmatine → Human platelet imidazoline I1 binding sites source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human platelet membrane radioligand competition.
limitations
Binding alone does not establish agonist efficacy, receptor sequence or clinical blood-pressure effects.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A pharmacological binding site is recorded without inventing its molecular identity.
primary_references
Comparison of the properties of agmatine and endogenous clonidine-displacing substance at imidazoline and alpha-2 adrenergic receptors. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7853171/
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human platelet membrane radioligand competition. · source_derived_draft · unverified_draft
## agmatine-sulfate-human-i1-binding A pharmacological binding site is recorded without inventing its molecular identity. Agmatine bound human platelet I1 sites with high- and low-affinity components and preferential affinity for the high-affinity I1 component over tested alpha-2 subtypes. Model: Human platelet membrane radioligand competition. Limitations: Binding alone does not establish agonist efficacy, receptor sequence or clinical blood-pressure effects. Evidence access: Primary abstract Comparison of the properties of agmatine and endogenous clonidine-displacing substance at imidazoline and alpha-2 adrenergic receptors. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7853171/
Complete structured claim and evidence
Agmatine competed at human alpha-2A adrenergic receptors expressed in transfected cells in the 1995 receptor-panel study.
Agmatine → Human alpha-2A adrenergic receptor / ADRA2A source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human receptor expression and radioligand competition.
limitations
The study establishes binding in its assay, not that agmatine reproduces every action of clonidine or norepinephrine.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
An adrenergic receptor is another distinct interaction node.
primary_references
Comparison of the properties of agmatine and endogenous clonidine-displacing substance at imidazoline and alpha-2 adrenergic receptors. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7853171/
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human receptor expression and radioligand competition. · source_derived_draft · unverified_draft
## agmatine-sulfate-alpha2a-binding An adrenergic receptor is another distinct interaction node. Agmatine competed at human alpha-2A adrenergic receptors expressed in transfected cells in the 1995 receptor-panel study. Model: Human receptor expression and radioligand competition. Limitations: The study establishes binding in its assay, not that agmatine reproduces every action of clonidine or norepinephrine. Evidence access: Primary abstract Comparison of the properties of agmatine and endogenous clonidine-displacing substance at imidazoline and alpha-2 adrenergic receptors. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7853171/
Complete structured claim and evidence
Agmatine competed at human alpha-2B adrenergic receptors expressed in transfected cells in the 1995 receptor-panel study.
Agmatine → Human alpha-2B adrenergic receptor / ADRA2B source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human receptor expression and radioligand competition.
limitations
The study establishes binding in its assay, not that agmatine reproduces every action of clonidine or norepinephrine.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
An adrenergic receptor is another distinct interaction node.
primary_references
Comparison of the properties of agmatine and endogenous clonidine-displacing substance at imidazoline and alpha-2 adrenergic receptors. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7853171/
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human receptor expression and radioligand competition. · source_derived_draft · unverified_draft
## agmatine-sulfate-alpha2b-binding An adrenergic receptor is another distinct interaction node. Agmatine competed at human alpha-2B adrenergic receptors expressed in transfected cells in the 1995 receptor-panel study. Model: Human receptor expression and radioligand competition. Limitations: The study establishes binding in its assay, not that agmatine reproduces every action of clonidine or norepinephrine. Evidence access: Primary abstract Comparison of the properties of agmatine and endogenous clonidine-displacing substance at imidazoline and alpha-2 adrenergic receptors. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7853171/
Complete structured claim and evidence
Agmatine competed at human alpha-2C adrenergic receptors expressed in transfected cells in the 1995 receptor-panel study.
Agmatine → Human alpha-2C adrenergic receptor / ADRA2C source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human receptor expression and radioligand competition.
limitations
The study establishes binding in its assay, not that agmatine reproduces every action of clonidine or norepinephrine.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
An adrenergic receptor is another distinct interaction node.
primary_references
Comparison of the properties of agmatine and endogenous clonidine-displacing substance at imidazoline and alpha-2 adrenergic receptors. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7853171/
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human receptor expression and radioligand competition. · source_derived_draft · unverified_draft
## agmatine-sulfate-alpha2c-binding An adrenergic receptor is another distinct interaction node. Agmatine competed at human alpha-2C adrenergic receptors expressed in transfected cells in the 1995 receptor-panel study. Model: Human receptor expression and radioligand competition. Limitations: The study establishes binding in its assay, not that agmatine reproduces every action of clonidine or norepinephrine. Evidence access: Primary abstract Comparison of the properties of agmatine and endogenous clonidine-displacing substance at imidazoline and alpha-2 adrenergic receptors. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7853171/
Complete structured claim and evidence
Agmatine and endogenous bovine hypothalamic clonidine-displacing material had different affinity rankings across the tested receptor panel.
Agmatine → Bovine hypothalamic clonidine-displacing-substance binding profile source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human and bovine receptor preparations with purified compound and endogenous extract.
limitations
This qualifies the identity of the extract; it does not negate agmatine binding.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
An extract containing an active compound can have additional active constituents.
primary_references
Comparison of the properties of agmatine and endogenous clonidine-displacing substance at imidazoline and alpha-2 adrenergic receptors. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7853171/
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 316–322
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human and bovine receptor preparations with purified compound and endogenous extract. · source_derived_draft · unverified_draft
## agmatine-sulfate-cds-specificity An extract containing an active compound can have additional active constituents. Agmatine and endogenous bovine hypothalamic clonidine-displacing material had different affinity rankings across the tested receptor panel. Model: Human and bovine receptor preparations with purified compound and endogenous extract. Limitations: This qualifies the identity of the extract; it does not negate agmatine binding. Evidence access: Primary abstract Comparison of the properties of agmatine and endogenous clonidine-displacing substance at imidazoline and alpha-2 adrenergic receptors. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7853171/
Complete structured claim and evidence
Agmatine at 1 mM reduced DMPP-induced chick retinal depolarization by approximately 70% without preventing neuronal bungarotoxin binding.
Agmatine → Chick retinal nicotinic depolarization source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Intact chick retina and retinal-homogenate binding assays.
limitations
Millimolar exposure; exact human receptor subunits or oral effects are not established.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Nicotinic function was blocked without competing at that toxin-binding site.
primary_references
Agmatine acts as an antagonist of neuronal nicotinic receptors. · 1990 · https://pubmed.ncbi.nlm.nih.gov/2331571/ · DOI 10.1111/j.1476-5381.1990.tb14680.x
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Intact chick retina and retinal-homogenate binding assays. · source_derived_draft · unverified_draft
## agmatine-sulfate-nicotinic-chick Nicotinic function was blocked without competing at that toxin-binding site. Agmatine at 1 mM reduced DMPP-induced chick retinal depolarization by approximately 70% without preventing neuronal bungarotoxin binding. Model: Intact chick retina and retinal-homogenate binding assays. Limitations: Millimolar exposure; exact human receptor subunits or oral effects are not established. Evidence access: Primary abstract Agmatine acts as an antagonist of neuronal nicotinic receptors. · 1990 · https://pubmed.ncbi.nlm.nih.gov/2331571/ · DOI 10.1111/j.1476-5381.1990.tb14680.x
Complete structured claim and evidence
Agmatine at 10 micromolar substantially blocked DMPP depolarization and synaptic transmission in rat superior cervical ganglion.
Agmatine → Rat superior cervical ganglion nicotinic transmission source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat isolated ganglion experiments.
limitations
Different tissue sensitivities are not interchangeable dose estimates.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A second tissue showed nicotinic inhibition at a different exposure.
primary_references
Agmatine acts as an antagonist of neuronal nicotinic receptors. · 1990 · https://pubmed.ncbi.nlm.nih.gov/2331571/ · DOI 10.1111/j.1476-5381.1990.tb14680.x
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat isolated ganglion experiments. · source_derived_draft · unverified_draft
## agmatine-sulfate-nicotinic-rat A second tissue showed nicotinic inhibition at a different exposure. Agmatine at 10 micromolar substantially blocked DMPP depolarization and synaptic transmission in rat superior cervical ganglion. Model: Rat isolated ganglion experiments. Limitations: Different tissue sensitivities are not interchangeable dose estimates. Evidence access: Primary abstract Agmatine acts as an antagonist of neuronal nicotinic receptors. · 1990 · https://pubmed.ncbi.nlm.nih.gov/2331571/ · DOI 10.1111/j.1476-5381.1990.tb14680.x
Complete structured claim and evidence
Agmatine promoted an antizyme-mRNA frameshift producing full-length antizyme; anti-antizyme antibody or antizyme inhibitor suppressed associated inhibitory activity.
Agmatine → Agmatine-dependent antizyme translational frameshift in the 1998 experiments source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cell and translation assays; exact construct and cell species not resolved in accessed abstract.
limitations
This is not assigned to a human isoform without checking the complete preparation.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
It can influence production of a regulator of polyamine metabolism.
primary_references
Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9624108/ · DOI 10.1074/jbc.273.25.15313
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell and translation assays; exact construct and cell species not resolved in accessed abstract. · source_derived_draft · unverified_draft
## agmatine-sulfate-antizyme-frameshift It can influence production of a regulator of polyamine metabolism. Agmatine promoted an antizyme-mRNA frameshift producing full-length antizyme; anti-antizyme antibody or antizyme inhibitor suppressed associated inhibitory activity. Model: Cell and translation assays; exact construct and cell species not resolved in accessed abstract. Limitations: This is not assigned to a human isoform without checking the complete preparation. Evidence access: Primary abstract Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9624108/ · DOI 10.1074/jbc.273.25.15313
Complete structured claim and evidence
Agmatine lowered intracellular polyamines and suppressed transformed-cell proliferation; polyamine supplementation reversed growth suppression.
Polyamine supplementation pool in the 1998 agmatine experiments → Agmatine-associated growth suppression in the 1998 transformed-cell model source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Transformed-cell supplementation experiment.
limitations
The accessed abstract reports polyamine supplementation as a group, not a spermidine-only rescue or cancer therapy.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Restoring a downstream pool changed the cellular outcome.
primary_references
Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9624108/ · DOI 10.1074/jbc.273.25.15313
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Transformed-cell supplementation experiment. · source_derived_draft · unverified_draft
## agmatine-sulfate-polyamine-rescue Restoring a downstream pool changed the cellular outcome. Agmatine lowered intracellular polyamines and suppressed transformed-cell proliferation; polyamine supplementation reversed growth suppression. Model: Transformed-cell supplementation experiment. Limitations: The accessed abstract reports polyamine supplementation as a group, not a spermidine-only rescue or cancer therapy. Evidence access: Primary abstract Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9624108/ · DOI 10.1074/jbc.273.25.15313
Complete structured claim and evidence
Agmatine reduced ODC activity before antizyme rose; proteasome inhibition did not prevent the ODC effect in rat pulmonary endothelial cells.
Agmatine → Rat pulmonary-endothelial ODC activity source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat pulmonary artery endothelial culture; timing and proteasome interventions.
limitations
The mechanism was not resolved; this is a limit on generalizing the antizyme-only model.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Antizyme induction did not explain every observed effect in this preparation.
primary_references
Regulation of ornithine decarboxylase activity and polyamine transport by agmatine in rat pulmonary artery endothelial cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11160620/
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 356–362
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat pulmonary artery endothelial culture; timing and proteasome interventions. · source_derived_draft · unverified_draft
## agmatine-sulfate-rat-odc-timing Antizyme induction did not explain every observed effect in this preparation. Agmatine reduced ODC activity before antizyme rose; proteasome inhibition did not prevent the ODC effect in rat pulmonary endothelial cells. Model: Rat pulmonary artery endothelial culture; timing and proteasome interventions. Limitations: The mechanism was not resolved; this is a limit on generalizing the antizyme-only model. Evidence access: Primary abstract Regulation of ornithine decarboxylase activity and polyamine transport by agmatine in rat pulmonary artery endothelial cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11160620/
Complete structured claim and evidence
Agmatine present in culture medium competitively inhibited radiolabeled polyamine uptake, increasing apparent Km.
Agmatine → Rat pulmonary-endothelial polyamine uptake source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat pulmonary endothelial transport kinetics.
limitations
No universal human polyamine depletion magnitude or clinical supplement interaction is established.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Immediate transport competition can coexist with slower regulation of protein expression.
primary_references
Regulation of ornithine decarboxylase activity and polyamine transport by agmatine in rat pulmonary artery endothelial cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11160620/
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 364–370
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat pulmonary endothelial transport kinetics. · source_derived_draft · unverified_draft
## agmatine-sulfate-rat-polyamine-competition Immediate transport competition can coexist with slower regulation of protein expression. Agmatine present in culture medium competitively inhibited radiolabeled polyamine uptake, increasing apparent Km. Model: Rat pulmonary endothelial transport kinetics. Limitations: No universal human polyamine depletion magnitude or clinical supplement interaction is established. Evidence access: Primary abstract Regulation of ornithine decarboxylase activity and polyamine transport by agmatine in rat pulmonary artery endothelial cells. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11160620/
Complete structured claim and evidence
Agmatine entered rat liver mitochondrial matrix through membrane-potential-dependent transport; putrescine, arginine, ornithine and lysine did not inhibit uptake.
Rat liver mitochondrial membrane potential → Rat liver mitochondrial agmatine uptake source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Isolated rat liver mitochondria; force-flux and inhibitor analysis.
limitations
The proposed transporter was not genetically identified; no single universal agmatine carrier is asserted.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Mitochondrial entry has different requirements from plasma-membrane entry.
primary_references
Agmatine is transported into liver mitochondria by a specific electrophoretic mechanism. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16509824/ · DOI 10.1042/BJ20060003
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Isolated rat liver mitochondria; force-flux and inhibitor analysis. · source_derived_draft · unverified_draft
## agmatine-sulfate-liver-mito-transport Mitochondrial entry has different requirements from plasma-membrane entry. Agmatine entered rat liver mitochondrial matrix through membrane-potential-dependent transport; putrescine, arginine, ornithine and lysine did not inhibit uptake. Model: Isolated rat liver mitochondria; force-flux and inhibitor analysis. Limitations: The proposed transporter was not genetically identified; no single universal agmatine carrier is asserted. Evidence access: Primary abstract Agmatine is transported into liver mitochondria by a specific electrophoretic mechanism. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16509824/ · DOI 10.1042/BJ20060003
Complete structured claim and evidence
Putrescine and idazoxan inhibited rat brain mitochondrial agmatine uptake despite being ineffective in the compared liver mitochondrial preparation.
Putrescine → Rat brain mitochondrial agmatine uptake source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Isolated rat brain versus liver mitochondria.
limitations
A pharmacological pattern does not establish a particular I2 receptor protein as the transporter.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Compartment and organ identity change which interactions occur.
primary_references
Agmatine transport in brain mitochondria: a different mechanism from that in liver mitochondria. · 2010 · https://pubmed.ncbi.nlm.nih.gov/19997762/ · DOI 10.1007/s00726-009-0401-1
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 380–386
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Isolated rat brain versus liver mitochondria. · source_derived_draft · unverified_draft
## agmatine-sulfate-brain-mito-transport Compartment and organ identity change which interactions occur. Putrescine and idazoxan inhibited rat brain mitochondrial agmatine uptake despite being ineffective in the compared liver mitochondrial preparation. Model: Isolated rat brain versus liver mitochondria. Limitations: A pharmacological pattern does not establish a particular I2 receptor protein as the transporter. Evidence access: Primary abstract Agmatine transport in brain mitochondria: a different mechanism from that in liver mitochondria. · 2010 · https://pubmed.ncbi.nlm.nih.gov/19997762/ · DOI 10.1007/s00726-009-0401-1
Complete structured claim and evidence
Agmatine induced permeability transition at lower tested concentrations but inhibited calcium/phosphate-associated swelling at higher concentrations in isolated rat liver mitochondria.
Agmatine → Rat liver mitochondrial permeability during agmatine exposure source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Isolated rat liver mitochondria; swelling and protein-release assays.
limitations
Numerical concentration ranges are not provided in the accessed abstract; no human protective threshold is inferred.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A compound can change direction across concentrations and assay endpoints.
primary_references
Involvement of the biogenic active amine agmatine in mitochondrial membrane permeabilization and release of pro-apoptotic factors. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31654209/ · DOI 10.1007/s00726-019-02791-6
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Isolated rat liver mitochondria; swelling and protein-release assays. · source_derived_draft · unverified_draft
## agmatine-sulfate-mitochondrial-state A compound can change direction across concentrations and assay endpoints. Agmatine induced permeability transition at lower tested concentrations but inhibited calcium/phosphate-associated swelling at higher concentrations in isolated rat liver mitochondria. Model: Isolated rat liver mitochondria; swelling and protein-release assays. Limitations: Numerical concentration ranges are not provided in the accessed abstract; no human protective threshold is inferred. Evidence access: Primary abstract Involvement of the biogenic active amine agmatine in mitochondrial membrane permeabilization and release of pro-apoptotic factors. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31654209/ · DOI 10.1007/s00726-019-02791-6
Complete structured claim and evidence
At conditions inhibiting swelling, agmatine still enhanced cytochrome-c and Smac/DIABLO release while preventing AIF release.
Agmatine → Rat liver mitochondrial cytochrome-c release during agmatine exposure source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Same isolated rat mitochondrial study with inhibitor probes.
limitations
Outer-membrane permeabilization was proposed; it is not a demonstrated beneficial effect of supplementation.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Less swelling did not mean that every cell-death-related endpoint was prevented.
primary_references
Involvement of the biogenic active amine agmatine in mitochondrial membrane permeabilization and release of pro-apoptotic factors. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31654209/ · DOI 10.1007/s00726-019-02791-6
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 396–402
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Same isolated rat mitochondrial study with inhibitor probes. · source_derived_draft · unverified_draft
## agmatine-sulfate-mitochondrial-release Less swelling did not mean that every cell-death-related endpoint was prevented. At conditions inhibiting swelling, agmatine still enhanced cytochrome-c and Smac/DIABLO release while preventing AIF release. Model: Same isolated rat mitochondrial study with inhibitor probes. Limitations: Outer-membrane permeabilization was proposed; it is not a demonstrated beneficial effect of supplementation. Evidence access: Primary abstract Involvement of the biogenic active amine agmatine in mitochondrial membrane permeabilization and release of pro-apoptotic factors. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31654209/ · DOI 10.1007/s00726-019-02791-6
Complete structured claim and evidence
Deleting E. coli speB increased the worm acs-2 reporter response; deleting additional agmatine-production genes abolished that increase.
Escherichia coli agmatinase / SpeB → C. elegans acs-2 reporter response to bacterial agmatine source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_access
Primary full text; Figure 4 and Figure S5
experimental_model
E. coli OP50 mutants feeding C. elegans.
limitations
This is a worm–bacterium experiment, not human gene manipulation or demonstrated clinical synergy.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Bacterial production and disposal influence a host metabolic signal.
primary_references
Host-Microbe-Drug-Nutrient Screen Identifies Bacterial Effectors of Metformin Therapy. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31474368/ · DOI 10.1016/j.cell.2019.08.003
trigger_kind
machinery_impairment Imported condition classification; unverified.
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · E. coli OP50 mutants feeding C. elegans. · source_derived_draft · unverified_draft
## agmatine-sulfate-bacterial-speb Bacterial production and disposal influence a host metabolic signal. Deleting E. coli speB increased the worm acs-2 reporter response; deleting additional agmatine-production genes abolished that increase. Model: E. coli OP50 mutants feeding C. elegans. Limitations: This is a worm–bacterium experiment, not human gene manipulation or demonstrated clinical synergy. Evidence access: Primary full text; Figure 4 and Figure S5 Host-Microbe-Drug-Nutrient Screen Identifies Bacterial Effectors of Metformin Therapy. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31474368/ · DOI 10.1016/j.cell.2019.08.003
Complete structured claim and evidence
Metformin no longer extended C. elegans lifespan when worms ate E. coli lacking both agmatine-production genes adiA and speA.
Metformin → E. coli agmatine production in the metformin worm-lifespan model source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_access
Primary full text; Figure 4I
experimental_model
Worm lifespan with defined E. coli deletion mutants.
limitations
No human lifespan extension or agmatine-sulfate/metformin combination efficacy is established.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A drug response depended on the microbes in a specific experimental system.
primary_references
Host-Microbe-Drug-Nutrient Screen Identifies Bacterial Effectors of Metformin Therapy. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31474368/ · DOI 10.1016/j.cell.2019.08.003
trigger_kind
machinery_impairment Imported condition classification; unverified.
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 412–418
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Worm lifespan with defined E. coli deletion mutants. · source_derived_draft · unverified_draft
## agmatine-sulfate-bacterial-metformin A drug response depended on the microbes in a specific experimental system. Metformin no longer extended C. elegans lifespan when worms ate E. coli lacking both agmatine-production genes adiA and speA. Model: Worm lifespan with defined E. coli deletion mutants. Limitations: No human lifespan extension or agmatine-sulfate/metformin combination efficacy is established. Evidence access: Primary full text; Figure 4I Host-Microbe-Drug-Nutrient Screen Identifies Bacterial Effectors of Metformin Therapy. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31474368/ · DOI 10.1016/j.cell.2019.08.003
Complete structured claim and evidence
Microbial-community models predicted higher agmatine-production capacity in metformin-treated cohorts, including longitudinal treatment data.
Metformin → Modeled human microbial agmatine-production capacity source_derived_draftungraded
Experimental context and source evidence
availability_state
biomarker_context Imported condition classification; unverified.
evidence_access
Primary full text; Figure 5
experimental_model
Human microbiome composition and diet-constrained metabolic modeling.
limitations
Not a direct measurement of plasma agmatine or proof that agmatine causes metformin benefits in humans.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
The human evidence here concerns a modeled capacity rather than a measured causal mediator.
primary_references
Host-Microbe-Drug-Nutrient Screen Identifies Bacterial Effectors of Metformin Therapy. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31474368/ · DOI 10.1016/j.cell.2019.08.003
trigger_kind
biomarker_context Imported condition classification; unverified.
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 420–426
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human microbiome composition and diet-constrained metabolic modeling. · source_derived_draft · unverified_draft
## agmatine-sulfate-microbiome-prediction The human evidence here concerns a modeled capacity rather than a measured causal mediator. Microbial-community models predicted higher agmatine-production capacity in metformin-treated cohorts, including longitudinal treatment data. Model: Human microbiome composition and diet-constrained metabolic modeling. Limitations: Not a direct measurement of plasma agmatine or proof that agmatine causes metformin benefits in humans. Evidence access: Primary full text; Figure 5 Host-Microbe-Drug-Nutrient Screen Identifies Bacterial Effectors of Metformin Therapy. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31474368/ · DOI 10.1016/j.cell.2019.08.003
Complete structured claim and evidence
L-arginine at 600 mg/kg intraperitoneally attenuated agmatine-associated antinociception in the mouse acetic-acid test.
L-Arginine → Mouse agmatine-associated antinociception source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Mouse chemical-pain assays; high-dose injected arginine.
limitations
This does not prove that normal dietary arginine negates an oral agmatine supplement or identify one exclusive target.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
A precursor-related nutrient changed the response in a pharmacological animal experiment.
primary_references
Mechanisms involved in the antinociception caused by agmatine in mice. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15857629/ · DOI 10.1016/j.neuropharm.2005.01.012
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 428–434
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse chemical-pain assays; high-dose injected arginine. · source_derived_draft · unverified_draft
## agmatine-sulfate-arginine-pain-interaction A precursor-related nutrient changed the response in a pharmacological animal experiment. L-arginine at 600 mg/kg intraperitoneally attenuated agmatine-associated antinociception in the mouse acetic-acid test. Model: Mouse chemical-pain assays; high-dose injected arginine. Limitations: This does not prove that normal dietary arginine negates an oral agmatine supplement or identify one exclusive target. Evidence access: Primary abstract Mechanisms involved in the antinociception caused by agmatine in mice. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15857629/ · DOI 10.1016/j.neuropharm.2005.01.012
Complete structured claim and evidence
A randomized trial of 2.670 g/day oral agmatine sulfate for 14 days reported greater pain and quality-of-life improvements than placebo; 51 and 48 were randomized, but 31 and 30 were analyzed.
Agmatine Sulfate → Human radiculopathy outcomes after agmatine sulfate source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Lumbar disc-associated radiculopathy; double-blind placebo-controlled trial after dose escalation.
limitations
Short exposure and reduced analyzed sample limit inference; molecular mediation and general chronic-pain efficacy were not established.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
There is limited human outcome evidence, with substantial attrition to consider.
primary_references
Safety and Efficacy of Dietary Agmatine Sulfate in Lumbar Disc-associated Radiculopathy. An Open-label, Dose-escalating Study Followed by a Randomized, Double-blind, Placebo-controlled Trial. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20447305/ · DOI 10.1111/j.1526-4637.2010.00808.x
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 436–442
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Lumbar disc-associated radiculopathy; double-blind placebo-controlled trial after dose escalation. · source_derived_draft · unverified_draft
## agmatine-sulfate-oral-clinical There is limited human outcome evidence, with substantial attrition to consider. A randomized trial of 2.670 g/day oral agmatine sulfate for 14 days reported greater pain and quality-of-life improvements than placebo; 51 and 48 were randomized, but 31 and 30 were analyzed. Model: Lumbar disc-associated radiculopathy; double-blind placebo-controlled trial after dose escalation. Limitations: Short exposure and reduced analyzed sample limit inference; molecular mediation and general chronic-pain efficacy were not established. Evidence access: Primary abstract Safety and Efficacy of Dietary Agmatine Sulfate in Lumbar Disc-associated Radiculopathy. An Open-label, Dose-escalating Study Followed by a Randomized, Double-blind, Placebo-controlled Trial. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20447305/ · DOI 10.1111/j.1526-4637.2010.00808.x
Complete structured claim and evidence
Three participants in the highest dose-escalation cohort reported diarrhea and mild nausea that resolved after stopping agmatine sulfate.
Agmatine Sulfate → Human agmatine-sulfate gastrointestinal tolerability source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Open-label regimens from 1.335 to 3.560 g/day for 10–21 days preceding the randomized trial.
limitations
The source does not establish a safe maximum for all users or identify sulfate as the cause of the symptoms.
nutrient_topic
Agmatine Sulfate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Agmatine Sulfate
plain_language
Tolerability at one dose and duration cannot establish universal long-term safety.
primary_references
Safety and Efficacy of Dietary Agmatine Sulfate in Lumbar Disc-associated Radiculopathy. An Open-label, Dose-escalating Study Followed by a Randomized, Double-blind, Placebo-controlled Trial. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20447305/ · DOI 10.1111/j.1526-4637.2010.00808.x
Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20) · lines 444–450
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Open-label regimens from 1.335 to 3.560 g/day for 10–21 days preceding the randomized trial. · source_derived_draft · unverified_draft
## agmatine-sulfate-oral-tolerability Tolerability at one dose and duration cannot establish universal long-term safety. Three participants in the highest dose-escalation cohort reported diarrhea and mild nausea that resolved after stopping agmatine sulfate. Model: Open-label regimens from 1.335 to 3.560 g/day for 10–21 days preceding the randomized trial. Limitations: The source does not establish a safe maximum for all users or identify sulfate as the cause of the symptoms. Evidence access: Primary abstract Safety and Efficacy of Dietary Agmatine Sulfate in Lumbar Disc-associated Radiculopathy. An Open-label, Dose-escalating Study Followed by a Randomized, Double-blind, Placebo-controlled Trial. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20447305/ · DOI 10.1111/j.1526-4637.2010.00808.x
Complete structured claim and evidence
Arginine-derived tracer also appeared in agmatine, without suppression by the arginase inhibitor.
L-Arginine → Agmatine source_derived_draftungraded
Experimental context and source evidence
evidence_access
Full-text results, Figures 2 and 6, Europe PMC PMC5075284; primary abstract.
experimental_model
Primary human activated T cells; isotope tracing and functional assays.
limitations
The responsible enzyme was not established here; no universal human arginine-decarboxylase assignment.
nutrient_topic
L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
plain_language
A separate metabolic branch remained detectable.
primary_references
L-Arginine Modulates T Cell Metabolism and Enhances Survival and Anti-tumor Activity. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27745970/ · DOI 10.1016/j.cell.2016.09.031
L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 230–236
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Primary human activated T cells; isotope tracing and functional assays. · source_derived_draft · unverified_draft
## arg-tcell-agmatine A separate metabolic branch remained detectable. Arginine-derived tracer also appeared in agmatine, without suppression by the arginase inhibitor. Model: Primary human activated T cells; isotope tracing and functional assays. Limitations: The responsible enzyme was not established here; no universal human arginine-decarboxylase assignment. Evidence access: Full-text results, Figures 2 and 6, Europe PMC PMC5075284; primary abstract. L-Arginine Modulates T Cell Metabolism and Enhances Survival and Anti-tumor Activity. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27745970/ · DOI 10.1016/j.cell.2016.09.031
Complete structured claim and evidence
AGAT catalyzes transfer of an amidino group from arginine to glycine, forming guanidinoacetate and ornithine.
Human glycine amidinotransferase AGAT / GATM → Guanidinoacetate source_derived_draftungraded
Experimental context and source evidence
evidence_span
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experimental_model
Human AGAT crystal structures and inactive-mutant substrate complex
exposure
Native, ornithine-bound and inactive mutant structures
limitations
Structures support an amidino-transfer mechanism; substrate availability in a person and effects of amino-acid supplementation were not measured.
nutrient_topic
Creatine research collection; topical membership is not evidence of a direct dietary effect. · Creatine
organism
Recombinant human enzyme
plain_language
The first synthesis step joins material from arginine and glycine to make the precursor of creatine.
primary_references
[creatine-p9218780] Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. (1997). https://pubmed.ncbi.nlm.nih.gov/9218780/ DOI: 10.1093/emboj/16.12.3373
tissue_or_cell_type
Purified protein
Creatine: synthesis, transport, phosphocreatine energetics and nutrient interactions (2026-09-17) · lines 177–188
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human AGAT crystal structures and inactive-mutant substrate complex · source_derived_draft · unverified_draft
### creatine-agat-reaction AGAT catalyzes transfer of an amidino group from arginine to glycine, forming guanidinoacetate and ornithine. Condition category: normal nutrient_topic: Creatine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The first synthesis step joins material from arginine and glycine to make the precursor of creatine. organism: Recombinant human enzyme tissue_or_cell_type: Purified protein experimental_model: Human AGAT crystal structures and inactive-mutant substrate complex limitations: Structures support an amidino-transfer mechanism; substrate availability in a person and effects of amino-acid supplementation were not measured. exposure: Native, ornithine-bound and inactive mutant structures evidence_span: {"source_cache": "artifacts/creatine-research/9218780.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "407baedc2f982a5abb9d14a01e8ac9dc331d60115acc716604c1e6003aa12c1b", "start_char": 0, "end_char": 1112, "text_sha256": "407baedc2f982a5abb9d14a01e8ac9dc331d60115acc716604c1e6003aa12c1b"} [creatine-p9218780] Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. (1997). https://pubmed.ncbi.nlm.nih.gov/9218780/ DOI: 10.1093/emboj/16.12.3373
Complete structured claim and evidence
Ornithine binding to human AGAT induced movement of a flexible loop and neighboring helix at the active-site region.
L-Ornithine → Human glycine amidinotransferase AGAT / GATM source_derived_draftungraded
Experimental context and source evidence
evidence_span
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experimental_model
Human AGAT crystal structures and inactive-mutant substrate complex
exposure
Native, ornithine-bound and inactive mutant structures
limitations
Structures support an amidino-transfer mechanism; substrate availability in a person and effects of amino-acid supplementation were not measured.
nutrient_topic
Creatine research collection; topical membership is not evidence of a direct dietary effect. · Creatine
organism
Recombinant human enzyme
plain_language
A product of the first step can bind back to the enzyme and change its working shape.
primary_references
[creatine-p9218780] Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. (1997). https://pubmed.ncbi.nlm.nih.gov/9218780/ DOI: 10.1093/emboj/16.12.3373
tissue_or_cell_type
Purified protein
Creatine: synthesis, transport, phosphocreatine energetics and nutrient interactions (2026-09-17) · lines 190–201
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human AGAT crystal structures and inactive-mutant substrate complex · source_derived_draft · unverified_draft
### creatine-ornithine-agat Ornithine binding to human AGAT induced movement of a flexible loop and neighboring helix at the active-site region. Condition category: normal nutrient_topic: Creatine research collection; topical membership is not evidence of a direct dietary effect. plain_language: A product of the first step can bind back to the enzyme and change its working shape. organism: Recombinant human enzyme tissue_or_cell_type: Purified protein experimental_model: Human AGAT crystal structures and inactive-mutant substrate complex limitations: Structures support an amidino-transfer mechanism; substrate availability in a person and effects of amino-acid supplementation were not measured. exposure: Native, ornithine-bound and inactive mutant structures evidence_span: {"source_cache": "artifacts/creatine-research/9218780.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "407baedc2f982a5abb9d14a01e8ac9dc331d60115acc716604c1e6003aa12c1b", "start_char": 0, "end_char": 1112, "text_sha256": "407baedc2f982a5abb9d14a01e8ac9dc331d60115acc716604c1e6003aa12c1b"} [creatine-p9218780] Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. (1997). https://pubmed.ncbi.nlm.nih.gov/9218780/ DOI: 10.1093/emboj/16.12.3373
Complete structured claim and evidence
Human OCT2 transported berberine in transfected cells, with reported Km 4.4 micromolar.
Human organic cation transporter 2 / OCT2 / SLC22A2 → Berberine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/berberine-research/18157518.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34651ed2e9ce3c38b6042e616b5c36d932fe6f1099c627d1b5403b338eae7b2b", "start_char": 0, "end_char": 1918, "text_sha256": "34651ed2e9ce3c38b6042e616b5c36d932fe6f1099c627d1b5403b338eae7b2b"}
experimental_model
Polarized transporter-transfected MDCKII cells
exposure
Berberine transport kinetics and transporter inhibition
limitations
Engineered system, not direct evidence for human oral bioavailability or a universal transport bottleneck.
nutrient_topic
Berberine research collection; topical membership is not evidence of a direct dietary effect. · Berberine
organism
Human OCT1, OCT2 and ABCB1 in engineered canine cells
plain_language
Berberine uses a separately identified organic-cation uptake transporter.
primary_references
[berberine-p18157518] Vectorial transport of the plant alkaloid berberine by double-transfected cells expressing the human organic cation transporter 1 (OCT1, SLC22A1) and the efflux pump MDR1 P-glycoprotein (ABCB1). (2008). https://pubmed.ncbi.nlm.nih.gov/18157518/ DOI: 10.1007/s00210-007-0219-x
tissue_or_cell_type
Basolateral uptake and apical export
transport_effect
raises Berberine uptake measured in transfected cells, which stand for the tubular cell, with a reported Km of 4.4 micromolar.
transport_pool
the renal tubular cell interior Berberine uptake measured in transfected cells, which stand for the tubular cell, with a reported Km of 4.4 micromolar.
Berberine: metabolism, nutrient connections and drug interactions (2026-09-17) · lines 220–231
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Polarized transporter-transfected MDCKII cells · source_derived_draft · unverified_draft
### berberine-uptake-oct2 Human OCT2 transported berberine in transfected cells, with reported Km 4.4 micromolar. Condition category: normal nutrient_topic: Berberine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Berberine uses a separately identified organic-cation uptake transporter. organism: Human OCT1, OCT2 and ABCB1 in engineered canine cells tissue_or_cell_type: Basolateral uptake and apical export experimental_model: Polarized transporter-transfected MDCKII cells limitations: Engineered system, not direct evidence for human oral bioavailability or a universal transport bottleneck. exposure: Berberine transport kinetics and transporter inhibition evidence_span: {"source_cache": "artifacts/berberine-research/18157518.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34651ed2e9ce3c38b6042e616b5c36d932fe6f1099c627d1b5403b338eae7b2b", "start_char": 0, "end_char": 1918, "text_sha256": "34651ed2e9ce3c38b6042e616b5c36d932fe6f1099c627d1b5403b338eae7b2b"} [berberine-p18157518] Vectorial transport of the plant alkaloid berberine by double-transfected cells expressing the human organic cation transporter 1 (OCT1, SLC22A1) and the efflux pump MDR1 P-glycoprotein (ABCB1). (2008). https://pubmed.ncbi.nlm.nih.gov/18157518/ DOI: 10.1007/s00210-007-0219-x
Complete structured claim and evidence
MATE1 transported metformin in a proton-gradient-dependent manner, with a Michaelis-Menten constant of 0.78 mM.
Human multidrug and toxin extrusion protein 1 / MATE1 / SLC47A1 → Metformin source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/metformin-research/17509534.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2660dd67050133c958e8aa13cf2ac6b574bd56fcefa116d3a73c3db4a7cea44", "start_char": 0, "end_char": 1841, "text_sha256": "d2660dd67050133c958e8aa13cf2ac6b574bd56fcefa116d3a73c3db4a7cea44"}
experimental_model
MATE1 and MATE2-K cDNA transfection into HEK293 cells with kinetic analysis
exposure
Oppositely directed proton gradient; Michaelis-Menten constants for ten substrates
limitations
Millimolar affinities in a transfected system. Substrate overlap describes a shared route, not a predicted clinical interaction.
nutrient_topic
Metformin research collection; topical membership is not evidence of a direct clinical effect, and pharmacological exposure is not dietary intake. · Metformin
organism
Human transporters
plain_language
A proton-driven pump moves the drug out of the cell into urine.
primary_references
[metformin-p17509534] Substrate specificity of MATE1 and MATE2-K, human multidrug and toxin extrusions/H(+)-organic cation antiporters. (2007). https://pubmed.ncbi.nlm.nih.gov/17509534/ DOI: 10.1016/j.bcp.2007.04.010
tissue_or_cell_type
Renal brush-border membrane transport
transport_effect
depends Recorded as proton-gradient-dependent transport. MATE carriers run either way with the proton gradient, and the assay's pool and the extrusion role move opposite ways.
transport_pool
the renal tubular cell interior Recorded as proton-gradient-dependent transport. MATE carriers run either way with the proton gradient, and the assay's pool and the extrusion role move opposite ways.
Metformin: transport, molecular targets, gut mechanisms and nutrient interactions (2026-09-19) · lines 203–214
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · MATE1 and MATE2-K cDNA transfection into HEK293 cells with kinetic analysis · source_derived_draft · unverified_draft
### metformin-mate1-metformin MATE1 transported metformin in a proton-gradient-dependent manner, with a Michaelis-Menten constant of 0.78 mM. Condition category: normal nutrient_topic: Metformin research collection; topical membership is not evidence of a direct clinical effect, and pharmacological exposure is not dietary intake. plain_language: A proton-driven pump moves the drug out of the cell into urine. organism: Human transporters tissue_or_cell_type: Renal brush-border membrane transport experimental_model: MATE1 and MATE2-K cDNA transfection into HEK293 cells with kinetic analysis limitations: Millimolar affinities in a transfected system. Substrate overlap describes a shared route, not a predicted clinical interaction. exposure: Oppositely directed proton gradient; Michaelis-Menten constants for ten substrates evidence_span: {"source_cache": "artifacts/metformin-research/17509534.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2660dd67050133c958e8aa13cf2ac6b574bd56fcefa116d3a73c3db4a7cea44", "start_char": 0, "end_char": 1841, "text_sha256": "d2660dd67050133c958e8aa13cf2ac6b574bd56fcefa116d3a73c3db4a7cea44"} [metformin-p17509534] Substrate specificity of MATE1 and MATE2-K, human multidrug and toxin extrusions/H(+)-organic cation antiporters. (2007). https://pubmed.ncbi.nlm.nih.gov/17509534/ DOI: 10.1016/j.bcp.2007.04.010
Complete structured claim and evidence

Availability and dependencies

Each situation shows the normal role first, then what the sources report under a specific condition. A shortfall in the diet, a fault in the machinery, and a low blood reading are kept separate because they are not the same thing.

A missing uptake system blocks cellular access

Condition: machinery_impairment · Polyamine-transport-deficient carcinoma cells.

Normal role: Transport provides intracellular agmatine.

Recorded consequence: Agmatine uptake was lost.

Scope: Human experimental carcinoma cell line.

Depleting one metabolic pool can increase uptake of another compound

Condition: machinery_impairment · Difluoromethylornithine-induced depletion.

Normal role: Polyamine state influences transport regulation.

Recorded consequence: Greater agmatine uptake.

Scope: Rat hepatocyte culture.

Agmatine processing requires the correct catalytic machinery

Condition: machinery_impairment · Metal requirement and catalytic-residue substitutions.

Normal role: Rat ALP hydrolyzes agmatine in a manganese-dependent assay.

Recorded consequence: Loss of measured activity with specified mutants.

Scope: Rat recombinant enzyme.

Microbial genes determine a response in the worm model

Condition: machinery_impairment · Targeted bacterial gene deletions.

Normal role: Bacterial synthesis and catabolism control agmatine-related host signals.

Recorded consequence: Altered worm reporter and metformin-associated lifespan responses.

Scope: E. coli–C. elegans experiments.

Predicted microbial production is not measured tissue availability

Condition: biomarker_context · Metformin-treated human microbiome datasets.

Normal role: Microbial pathways can contribute to metabolite exposure.

Recorded consequence: Higher predicted agmatine-production capacity.

Scope: Diet-constrained microbial community models.

The sources

Every document behind this chapter is preserved word for word. Open one to read it in full with its recorded conflicts marked in place.

Agmatine Sulfate: transport, guanidino metabolism, ion channels and cross-nutrient mechanisms (2026-09-20)AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · unverified_draftRead preserved source
Berberine: metabolism, nutrient connections and drug interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Creatine: synthesis, transport, phosphocreatine energetics and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18)AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · unverified_draftRead preserved source
Metformin: transport, molecular targets, gut mechanisms and nutrient interactions (2026-09-19)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source

Recorded disagreements

Where two sources say different things, both are kept and the difference is explained. You can discuss a disagreement or propose a mechanism that might account for it.

Open questions in this collection

Questions the curators could not answer from the sources in front of them, kept here with the reason each one is still open. These are gaps in this collection, not findings or proof that no one has studied them.

Chapters are assembled from supplied drafts and curated literature summaries. Statements remain unverified against the primary studies, and the ledger is not medical advice.

Evidence, AI assistance and curation standards

Agmatine Sulfate

The mechanisms

Human OCT1 expression increased concentration-dependent agmatine transport in HEK293 cells, with Km 18.73 ± 4.86 mM.

Human OCT2 mediated pH- and concentration-dependent agmatine transport, with Km 1.84 ± 0.38 mM.

Human MATE1 expression increased saturable agmatine accumulation, with Km 240 ± 31 micromolar.

An inward proton gradient trans-stimulated efflux of intracellular agmatine from MATE1-expressing cells.

Polyamines inhibited MATE1-mediated agmatine transport, whereas L-arginine did not inhibit it in the tested system.

Transformed mouse NIH/3T3 cells took up agmatine through an energy- and membrane-potential-dependent saturable system with apparent Km 2.5 micromolar.

Agmatine uptake was abrogated in a polyamine-transport-deficient human carcinoma cell line.

Rat hepatocytes exhibited high-affinity agmatine uptake with Km 0.03 mM; the system also transported putrescine but not arginine, spermidine or spermine.

Difluoromethylornithine-induced polyamine depletion increased agmatine uptake in cultured rat hepatocytes.

About 50% of taken-up radiolabeled agmatine was recovered as 4-guanidinobutyrate in the rat hepatocyte experiment.

About 10% of taken-up agmatine label entered the polyamine pool in rat hepatocyte cultures.

Adding diamine oxidase or inhibiting aldehyde dehydrogenase increased agmatine-associated suppression of inducible NO generation; aldehyde removal or trapping attenuated it.

Purified recombinant human AGMAT variants R105 and G105 showed no detected agmatine hydrolysis at 10 mM substrate in the 2022 assay.

Both purified human AGMAT variants hydrolyzed guanidinobutyrate, supporting a guanidino-acid hydrolase function.

Human AGMAT R105 hydrolyzed taurocyamine more efficiently than guanidinobutyrate in the tested concentration range; R105 and G105 differed in substrate preferences.

Expressing human AGMAT R105 in medium supplemented with 0.5 mM manganese increased its subsequent taurocyamine-hydrolysis activity approximately fourfold.

Recombinant rat-brain agmatinase-like protein catalyzed agmatine hydrolysis; its central 210-residue construct retained activity with reduced kcat.

Rat ALP catalytic activity required manganese; D217A and specified multi-residue substitutions abolished measured agmatinase activity.

Human AGMAT expression supported growth of polyamine-biosynthesis-deficient yeast in the presence of agmatine despite absent directly measured in vitro agmatinase activity.

Human ODC paralogue/AZIN2 had no intrinsic arginine-decarboxylase activity in the reported experiments.

Human AZIN2 bound antizymes and counteracted AZ1-dependent suppression and degradation of ODC.

Purified human GATM transferred an amidino group from arginine to taurine, producing taurocyamine in vitro.

Human GATM used GABA as an amidino acceptor to form guanidinobutyrate in vitro.

Human GATM transferred the amidino group of arginine to beta-alanine, producing guanidinopropionate.

Four purified human creatine-kinase isoforms phosphorylated creatine but not taurocyamine, guanidinobutyrate or guanidinopropionate at 10 mM test substrate.

Agmatine competitively inhibited the brain-derived NOS I preparation with approximate Ki 660 micromolar and was not an NO precursor.

Agmatine competitively inhibited macrophage-derived NOS II with approximate Ki 220 micromolar.

Agmatine competitively inhibited endothelial-derived NOS III only at a much higher approximate Ki of 7.5 mM in the isoform comparison.

Agmatine induced cytosolic calcium transients in bovine pulmonary artery endothelial cells; repeated exposure downregulated the response.

Agmatine increased nitrite production about threefold in bovine endothelial cells; idazoxan inhibited the effect whereas yohimbine did not.

Extracellular agmatine blocked NMDA currents in rat hippocampal neurons in a voltage- and concentration-dependent manner; estimated pore-site Kd was 952 micromolar at 0 mV.

Spermine still potentiated NMDA current in the presence of agmatine, supporting distinct interaction sites for the two compounds.

Putrescine had little NMDA-blocking effect compared with agmatine or arcaine in the same experiments.

Agmatine bound human platelet I1 sites with high- and low-affinity components and preferential affinity for the high-affinity I1 component over tested alpha-2 subtypes.

Agmatine competed at human alpha-2A adrenergic receptors expressed in transfected cells in the 1995 receptor-panel study.

Agmatine competed at human alpha-2B adrenergic receptors expressed in transfected cells in the 1995 receptor-panel study.

Agmatine competed at human alpha-2C adrenergic receptors expressed in transfected cells in the 1995 receptor-panel study.

Agmatine and endogenous bovine hypothalamic clonidine-displacing material had different affinity rankings across the tested receptor panel.

Agmatine at 1 mM reduced DMPP-induced chick retinal depolarization by approximately 70% without preventing neuronal bungarotoxin binding.

Agmatine at 10 micromolar substantially blocked DMPP depolarization and synaptic transmission in rat superior cervical ganglion.

Agmatine promoted an antizyme-mRNA frameshift producing full-length antizyme; anti-antizyme antibody or antizyme inhibitor suppressed associated inhibitory activity.

Agmatine lowered intracellular polyamines and suppressed transformed-cell proliferation; polyamine supplementation reversed growth suppression.

Agmatine reduced ODC activity before antizyme rose; proteasome inhibition did not prevent the ODC effect in rat pulmonary endothelial cells.

Agmatine present in culture medium competitively inhibited radiolabeled polyamine uptake, increasing apparent Km.

Agmatine entered rat liver mitochondrial matrix through membrane-potential-dependent transport; putrescine, arginine, ornithine and lysine did not inhibit uptake.

Putrescine and idazoxan inhibited rat brain mitochondrial agmatine uptake despite being ineffective in the compared liver mitochondrial preparation.

Agmatine induced permeability transition at lower tested concentrations but inhibited calcium/phosphate-associated swelling at higher concentrations in isolated rat liver mitochondria.

At conditions inhibiting swelling, agmatine still enhanced cytochrome-c and Smac/DIABLO release while preventing AIF release.

Deleting E. coli speB increased the worm acs-2 reporter response; deleting additional agmatine-production genes abolished that increase.

Metformin no longer extended C. elegans lifespan when worms ate E. coli lacking both agmatine-production genes adiA and speA.

Microbial-community models predicted higher agmatine-production capacity in metformin-treated cohorts, including longitudinal treatment data.

L-arginine at 600 mg/kg intraperitoneally attenuated agmatine-associated antinociception in the mouse acetic-acid test.

A randomized trial of 2.670 g/day oral agmatine sulfate for 14 days reported greater pain and quality-of-life improvements than placebo; 51 and 48 were randomized, but 31 and 30 were analyzed.

Three participants in the highest dose-escalation cohort reported diarrhea and mild nausea that resolved after stopping agmatine sulfate.

Arginine-derived tracer also appeared in agmatine, without suppression by the arginase inhibitor.

AGAT catalyzes transfer of an amidino group from arginine to glycine, forming guanidinoacetate and ornithine.

Ornithine binding to human AGAT induced movement of a flexible loop and neighboring helix at the active-site region.

Human OCT2 transported berberine in transfected cells, with reported Km 4.4 micromolar.

MATE1 transported metformin in a proton-gradient-dependent manner, with a Michaelis-Menten constant of 0.78 mM.

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