Human glutaredoxin 1 / GLRX: molecular mechanisms & dependencies

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.

Human evidence only

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

Purified human placental glutaredoxin catalyzed GSH-dependent reduction of DHA to ascorbate.
Human glutaredoxin 1 / GLRX → Dehydroascorbic acid source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
true
experimental_model
Purified human placental glutaredoxin and bovine liver PDI; additional porcine/bovine glutaredoxins
exposure
Purified enzyme plus DHA and GSH
limitations
In vitro activity does not establish its share of total placental recycling.
nutrient_topic
Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
organism
Homo sapiens
plain_language
Glutaredoxin can use glutathione to restore reduced vitamin C.
primary_references
[wells1990] Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. (1990). https://pubmed.ncbi.nlm.nih.gov/2394726/ DOI: 10.1016/s0021-9258(18)55401-6
tissue_or_cell_type
Placental enzyme preparation
Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 351–362
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human placental glutaredoxin and bovine liver PDI; additional porcine/bovine glutaredoxins · source_derived_draft · unverified_draft
### vc-transport-human-glutaredoxin-dha Purified human placental glutaredoxin catalyzed GSH-dependent reduction of DHA to ascorbate. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glutaredoxin can use glutathione to restore reduced vitamin C. organism: Homo sapiens tissue_or_cell_type: Placental enzyme preparation experimental_model: Purified human placental glutaredoxin and bovine liver PDI; additional porcine/bovine glutaredoxins limitations: In vitro activity does not establish its share of total placental recycling. exposure: Purified enzyme plus DHA and GSH cross_nutrient: true [wells1990] Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. (1990). https://pubmed.ncbi.nlm.nih.gov/2394726/ DOI: 10.1016/s0021-9258(18)55401-6
Complete structured claim and evidence
Recombinant human glutaredoxin enhanced GAPDH S-glutathionylation under the tested GSSG conditions.
Human glutaredoxin 1 / GLRX → S-Glutathionylation of purified human GAPDH source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/glutathione-research/9642155.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72", "start_char": 0, "end_char": 1538, "text_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72"}
experimental_model
Purified GAPDH oxidation and radiolabeled disulfide assays
exposure
Hydrogen peroxide versus GSSG and glutaredoxin
limitations
This particular assay separates oxidation from glutathionylation; it does not establish one universal effect for all modified proteins.
nutrient_topic
Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
organism
Human GAPDH; human or bacterial glutaredoxin
plain_language
Reaction conditions can change the direction of a redox enzyme’s effect.
primary_references
[glutathione-p9642155] Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. (1998). https://pubmed.ncbi.nlm.nih.gov/9642155/ DOI: 10.1006/bbrc.1998.8695
tissue_or_cell_type
Cell-free enzyme system
Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 866–877
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified GAPDH oxidation and radiolabeled disulfide assays · source_derived_draft · unverified_draft
### glutathione-glrx-gapdh-tagging Recombinant human glutaredoxin enhanced GAPDH S-glutathionylation under the tested GSSG conditions. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Reaction conditions can change the direction of a redox enzyme’s effect. organism: Human GAPDH; human or bacterial glutaredoxin tissue_or_cell_type: Cell-free enzyme system experimental_model: Purified GAPDH oxidation and radiolabeled disulfide assays limitations: This particular assay separates oxidation from glutathionylation; it does not establish one universal effect for all modified proteins. exposure: Hydrogen peroxide versus GSSG and glutaredoxin evidence_span: {"source_cache": "artifacts/glutathione-research/9642155.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72", "start_char": 0, "end_char": 1538, "text_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72"} [glutathione-p9642155] Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. (1998). https://pubmed.ncbi.nlm.nih.gov/9642155/ DOI: 10.1006/bbrc.1998.8695
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.

Human glutaredoxin 1 / GLRX