Component
Cellular manganese uptake
Cellular manganese uptake
6 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What acts on it
ZIP8-specific siRNA reduced manganese uptake from the apical side of polarized mouse proximal-tubule cells.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- cross_nutrient
- true
- experimental_model
- Polarized proximal-tubule culture with separately accessible apical and basolateral compartments
- exposure
- ZIP8 siRNA versus controls during apical manganese exposure.
- limitations
- This is manganese uptake, not direct proof of zinc reabsorption by ZIP8; ZIP14 and DMT1 knockdowns also affected uptake in the paper.
- nutrient_topic
- Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
- organism
- Mus musculus
- plain_language
- A transporter known to handle zinc also helped kidney-derived cells take up manganese from their lumen-facing side.
- primary_references
- [zinc-trans-22534978] Roles of ZIP8, ZIP14, and DMT1 in transport of cadmium and manganese in mouse kidney proximal tubule cells. (2012). https://pubmed.ncbi.nlm.nih.gov/22534978/ DOI: 10.1039/c2mt20024d
- tissue_or_cell_type
- Mouse proximal-tubule epithelial cells
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 531–542
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Polarized proximal-tubule culture with separately accessible apical and basolateral compartments · source_derived_draft · unverified_draft
### zinc-trans-renal-zip8-manganese ZIP8-specific siRNA reduced manganese uptake from the apical side of polarized mouse proximal-tubule cells. Condition category: machinery_impairment nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: A transporter known to handle zinc also helped kidney-derived cells take up manganese from their lumen-facing side. organism: Mus musculus tissue_or_cell_type: Mouse proximal-tubule epithelial cells experimental_model: Polarized proximal-tubule culture with separately accessible apical and basolateral compartments limitations: This is manganese uptake, not direct proof of zinc reabsorption by ZIP8; ZIP14 and DMT1 knockdowns also affected uptake in the paper. exposure: ZIP8 siRNA versus controls during apical manganese exposure. cross_nutrient: true [zinc-trans-22534978] Roles of ZIP8, ZIP14, and DMT1 in transport of cadmium and manganese in mouse kidney proximal tubule cells. (2012). https://pubmed.ncbi.nlm.nih.gov/22534978/ DOI: 10.1039/c2mt20024d
Complete structured claim and evidenceMouse ZIP14 directly mediated 54Mn(II) uptake in RNA-injected Xenopus oocytes.
Experimental context and source evidence
- cross_nutrient
- true
- experimental_model
- RNA-injected Xenopus oocytes with radiolabeled metal uptake
- exposure
- 54Mn transport compared with uninjected controls.
- limitations
- Transport capacity is not proof that manganese supplements improve zinc transport or vice versa.
- nutrient_topic
- Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
- organism
- Mouse protein in Xenopus laevis oocytes
- plain_language
- ZIP14 could carry manganese as well as zinc in this experiment.
- primary_references
- [zinc-trans-21653899] Zip14 is a complex broad-scope metal-ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron. (2011). https://pubmed.ncbi.nlm.nih.gov/21653899/ DOI: 10.1152/ajpcell.00479.2010
- tissue_or_cell_type
- Oocyte plasma membrane
Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 492–503
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · RNA-injected Xenopus oocytes with radiolabeled metal uptake · source_derived_draft · unverified_draft
### zinc-trans-zip14-manganese-influx Mouse ZIP14 directly mediated 54Mn(II) uptake in RNA-injected Xenopus oocytes. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: ZIP14 could carry manganese as well as zinc in this experiment. organism: Mouse protein in Xenopus laevis oocytes tissue_or_cell_type: Oocyte plasma membrane experimental_model: RNA-injected Xenopus oocytes with radiolabeled metal uptake limitations: Transport capacity is not proof that manganese supplements improve zinc transport or vice versa. exposure: 54Mn transport compared with uninjected controls. cross_nutrient: true [zinc-trans-21653899] Zip14 is a complex broad-scope metal-ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron. (2011). https://pubmed.ncbi.nlm.nih.gov/21653899/ DOI: 10.1152/ajpcell.00479.2010
Complete structured claim and evidenceDMT1-specific siRNA reduced apical manganese uptake in polarized mouse proximal-tubule cells.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- cross_nutrient
- false
- experimental_model
- Transporter-specific siRNA in polarized mouse kidney proximal-tubule culture
- exposure
- DMT1 siRNA versus controls during apical manganese exposure.
- limitations
- Cell culture supports an uptake contribution; it does not quantify in vivo urinary reabsorption or rank transporter contributions.
- nutrient_topic
- Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
- organism
- Mus musculus
- plain_language
- DMT1 helped kidney-derived cells take up manganese from their lumen-facing side.
- primary_references
- [mn-trans-22534978] Roles of ZIP8, ZIP14, and DMT1 in transport of cadmium and manganese in mouse kidney proximal tubule cells. (2012). https://pubmed.ncbi.nlm.nih.gov/22534978/ DOI: 10.1039/c2mt20024d
- tissue_or_cell_type
- Proximal-tubule epithelial cells, apical membrane
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 344–355
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transporter-specific siRNA in polarized mouse kidney proximal-tubule culture · source_derived_draft · unverified_draft
### mn-trans-renal-dmt1 DMT1-specific siRNA reduced apical manganese uptake in polarized mouse proximal-tubule cells. Condition category: machinery_impairment nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: DMT1 helped kidney-derived cells take up manganese from their lumen-facing side. organism: Mus musculus tissue_or_cell_type: Proximal-tubule epithelial cells, apical membrane experimental_model: Transporter-specific siRNA in polarized mouse kidney proximal-tubule culture limitations: Cell culture supports an uptake contribution; it does not quantify in vivo urinary reabsorption or rank transporter contributions. exposure: DMT1 siRNA versus controls during apical manganese exposure. cross_nutrient: false [mn-trans-22534978] Roles of ZIP8, ZIP14, and DMT1 in transport of cadmium and manganese in mouse kidney proximal tubule cells. (2012). https://pubmed.ncbi.nlm.nih.gov/22534978/ DOI: 10.1039/c2mt20024d
Complete structured claim and evidenceZIP14-specific siRNA reduced apical manganese uptake in polarized mouse proximal-tubule cells.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- cross_nutrient
- false
- experimental_model
- Transporter-specific siRNA in polarized mouse kidney proximal-tubule culture
- exposure
- ZIP14 siRNA versus controls during apical manganese exposure.
- limitations
- Cell culture supports an uptake contribution; it does not quantify in vivo urinary reabsorption or rank transporter contributions.
- nutrient_topic
- Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
- organism
- Mus musculus
- plain_language
- ZIP14 helped kidney-derived cells take up manganese from their lumen-facing side.
- primary_references
- [mn-trans-22534978] Roles of ZIP8, ZIP14, and DMT1 in transport of cadmium and manganese in mouse kidney proximal tubule cells. (2012). https://pubmed.ncbi.nlm.nih.gov/22534978/ DOI: 10.1039/c2mt20024d
- tissue_or_cell_type
- Proximal-tubule epithelial cells, apical membrane
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 331–342
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transporter-specific siRNA in polarized mouse kidney proximal-tubule culture · source_derived_draft · unverified_draft
### mn-trans-renal-zip14 ZIP14-specific siRNA reduced apical manganese uptake in polarized mouse proximal-tubule cells. Condition category: machinery_impairment nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: ZIP14 helped kidney-derived cells take up manganese from their lumen-facing side. organism: Mus musculus tissue_or_cell_type: Proximal-tubule epithelial cells, apical membrane experimental_model: Transporter-specific siRNA in polarized mouse kidney proximal-tubule culture limitations: Cell culture supports an uptake contribution; it does not quantify in vivo urinary reabsorption or rank transporter contributions. exposure: ZIP14 siRNA versus controls during apical manganese exposure. cross_nutrient: false [mn-trans-22534978] Roles of ZIP8, ZIP14, and DMT1 in transport of cadmium and manganese in mouse kidney proximal tubule cells. (2012). https://pubmed.ncbi.nlm.nih.gov/22534978/ DOI: 10.1039/c2mt20024d
Complete structured claim and evidenceFe(II) inhibited mouse ZIP14-mediated Mn(II) uptake in Xenopus oocytes under the tested competition conditions.
Experimental context and source evidence
- cross_nutrient
- true
- experimental_model
- Mouse ZIP14 in RNA-injected Xenopus laevis oocytes
- exposure
- 2 micromolar radiolabeled Mn(II) with candidate inhibitor metal at 20 micromolar and 1 mM L-ascorbic acid; Figure 9B.
- limitations
- A tenfold molar competitor in a heterologous system is not a dietary competition threshold.
- nutrient_topic
- Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
- organism
- Mouse protein in Xenopus laevis oocytes
- plain_language
- Fe(II) competed with manganese entry through ZIP14 in this assay.
- primary_references
- [mn-trans-21653899] Zip14 is a complex broad-scope metal-ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron. (2011). https://pubmed.ncbi.nlm.nih.gov/21653899/ DOI: 10.1152/ajpcell.00479.2010
- tissue_or_cell_type
- Oocyte plasma membrane
Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 305–316
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mouse ZIP14 in RNA-injected Xenopus laevis oocytes · source_derived_draft · unverified_draft
### mn-trans-zip14-fe-inhibits-mn Fe(II) inhibited mouse ZIP14-mediated Mn(II) uptake in Xenopus oocytes under the tested competition conditions. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: Fe(II) competed with manganese entry through ZIP14 in this assay. organism: Mouse protein in Xenopus laevis oocytes tissue_or_cell_type: Oocyte plasma membrane experimental_model: Mouse ZIP14 in RNA-injected Xenopus laevis oocytes limitations: A tenfold molar competitor in a heterologous system is not a dietary competition threshold. exposure: 2 micromolar radiolabeled Mn(II) with candidate inhibitor metal at 20 micromolar and 1 mM L-ascorbic acid; Figure 9B. cross_nutrient: true [mn-trans-21653899] Zip14 is a complex broad-scope metal-ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron. (2011). https://pubmed.ncbi.nlm.nih.gov/21653899/ DOI: 10.1152/ajpcell.00479.2010
Complete structured claim and evidenceZn(II) inhibited mouse ZIP14-mediated Mn(II) uptake in Xenopus oocytes under the tested competition conditions.
Experimental context and source evidence
- cross_nutrient
- true
- experimental_model
- Mouse ZIP14 in RNA-injected Xenopus laevis oocytes
- exposure
- 2 micromolar radiolabeled Mn(II) with candidate inhibitor metal at 20 micromolar and 1 mM L-ascorbic acid; Figure 9B.
- limitations
- A tenfold molar competitor in a heterologous system is not a dietary competition threshold.
- nutrient_topic
- Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
- organism
- Mouse protein in Xenopus laevis oocytes
- plain_language
- Zn(II) competed with manganese entry through ZIP14 in this assay.
- primary_references
- [mn-trans-21653899] Zip14 is a complex broad-scope metal-ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron. (2011). https://pubmed.ncbi.nlm.nih.gov/21653899/ DOI: 10.1152/ajpcell.00479.2010
- tissue_or_cell_type
- Oocyte plasma membrane
Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 318–329
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mouse ZIP14 in RNA-injected Xenopus laevis oocytes · source_derived_draft · unverified_draft
### mn-trans-zip14-zn-inhibits-mn Zn(II) inhibited mouse ZIP14-mediated Mn(II) uptake in Xenopus oocytes under the tested competition conditions. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: Zn(II) competed with manganese entry through ZIP14 in this assay. organism: Mouse protein in Xenopus laevis oocytes tissue_or_cell_type: Oocyte plasma membrane experimental_model: Mouse ZIP14 in RNA-injected Xenopus laevis oocytes limitations: A tenfold molar competitor in a heterologous system is not a dietary competition threshold. exposure: 2 micromolar radiolabeled Mn(II) with candidate inhibitor metal at 20 micromolar and 1 mM L-ascorbic acid; Figure 9B. cross_nutrient: true [mn-trans-21653899] Zip14 is a complex broad-scope metal-ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron. (2011). https://pubmed.ncbi.nlm.nih.gov/21653899/ DOI: 10.1152/ajpcell.00479.2010
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.