Component

Human multidrug and toxin extrusion protein 1 / MATE1 / SLC47A1

Human multidrug and toxin extrusion protein 1 / MATE1 / SLC47A1. Species, exposure and limitations are retained in each linked claim.

6 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. 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

  2. MATE1 and MATE2-K together mediate tubular secretion of intracellular ionic compounds across the kidney brush-border membranes.

    Human multidrug and toxin extrusion protein 1 / MATE1 / SLC47A1 → MATE-mediated metformin efflux across brush-border membranes 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
    Entry and exit are separate steps handled by different proteins.
    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

    Metformin: transport, molecular targets, gut mechanisms and nutrient interactions (2026-09-19) · lines 229–240

    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-mate-detoxication MATE1 and MATE2-K together mediate tubular secretion of intracellular ionic compounds across the kidney brush-border membranes. 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: Entry and exit are separate steps handled by different proteins. 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

  3. 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

  4. The SLC47A1 rs2289669 A allele was associated with a 0.30% larger HbA1c reduction per allele during metformin treatment.

    Human multidrug and toxin extrusion protein 1 / MATE1 / SLC47A1 → Glycated hemoglobin / HbA1c concentration source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/metformin-research/19228809.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e90099f316586ff994eff67af58f075f654413a68d8605e869755e9b8c68adb3", "start_char": 0, "end_char": 1383, "text_sha256": "e90099f316586ff994eff67af58f075f654413a68d8605e869755e9b8c68adb3"}
    experimental_model
    Pharmacogenetic analysis of 116 incident metformin users in the Rotterdam Study
    exposure
    Twelve tagging SNPs in SLC47A1 against change in HbA1c
    limitations
    A preliminary association in a small sample that the authors say requires replication; no mechanism was measured.
    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
    plain_language
    How quickly the body clears the drug tracks with how much it lowers long-term glucose.
    primary_references
    [metformin-p19228809] Genetic variation in the multidrug and toxin extrusion 1 transporter protein influences the glucose-lowering effect of metformin in patients with diabetes: a preliminary study. (2009). https://pubmed.ncbi.nlm.nih.gov/19228809/ DOI: 10.2337/db08-1028
    tissue_or_cell_type
    Glycaemic response

    Metformin: transport, molecular targets, gut mechanisms and nutrient interactions (2026-09-19) · lines 372–383

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pharmacogenetic analysis of 116 incident metformin users in the Rotterdam Study · source_derived_draft · unverified_draft

    ### metformin-mate1-variant-response The SLC47A1 rs2289669 A allele was associated with a 0.30% larger HbA1c reduction per allele during metformin treatment. 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: How quickly the body clears the drug tracks with how much it lowers long-term glucose. organism: Human tissue_or_cell_type: Glycaemic response experimental_model: Pharmacogenetic analysis of 116 incident metformin users in the Rotterdam Study limitations: A preliminary association in a small sample that the authors say requires replication; no mechanism was measured. exposure: Twelve tagging SNPs in SLC47A1 against change in HbA1c evidence_span: {"source_cache": "artifacts/metformin-research/19228809.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e90099f316586ff994eff67af58f075f654413a68d8605e869755e9b8c68adb3", "start_char": 0, "end_char": 1383, "text_sha256": "e90099f316586ff994eff67af58f075f654413a68d8605e869755e9b8c68adb3"} [metformin-p19228809] Genetic variation in the multidrug and toxin extrusion 1 transporter protein influences the glucose-lowering effect of metformin in patients with diabetes: a preliminary study. (2009). https://pubmed.ncbi.nlm.nih.gov/19228809/ DOI: 10.2337/db08-1028
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. 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

  2. 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

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

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