Component

Human fibroblast collagen prolyl hydroxylase activity

Collagen prolyl hydroxylase assay in cultured skin fibroblasts, without isoform resolution.

1 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.

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 acts on it

  1. In the same human fibroblast culture study, measured collagen prolyl hydroxylase activity decreased after ascorbate treatment even while collagen synthesis increased.

    Experimental context and source evidence
    cross_nutrient
    Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing.
    experimental_model
    Cultured human skin fibroblasts
    exposure
    Prolonged ascorbate exposure versus no added ascorbate; exact culture concentration not verified in accessible abstract.
    limitations
    A cell-adaptation/activity measurement; not evidence that ascorbate directly inhibits the purified enzyme.
    nutrient_topic
    Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
    organism
    Homo sapiens
    plain_language
    More collagen production did not mean that every hydroxylase activity assay increased.
    primary_references
    [collagen1981] Regulation of collagen synthesis by ascorbic acid. (1981). https://pubmed.ncbi.nlm.nih.gov/6265920/ DOI: 10.1073/pnas.78.5.2879
    tissue_or_cell_type
    Skin fibroblasts

    Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 676–687

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cultured human skin fibroblasts · source_derived_draft · unverified_draft

    ### vc-enzyme-fibroblast-prolyl-activity In the same human fibroblast culture study, measured collagen prolyl hydroxylase activity decreased after ascorbate treatment even while collagen synthesis increased. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: More collagen production did not mean that every hydroxylase activity assay increased. organism: Homo sapiens tissue_or_cell_type: Skin fibroblasts experimental_model: Cultured human skin fibroblasts limitations: A cell-adaptation/activity measurement; not evidence that ascorbate directly inhibits the purified enzyme. cross_nutrient: Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing. exposure: Prolonged ascorbate exposure versus no added ascorbate; exact culture concentration not verified in accessible abstract. [collagen1981] Regulation of collagen synthesis by ascorbic acid. (1981). https://pubmed.ncbi.nlm.nih.gov/6265920/ DOI: 10.1073/pnas.78.5.2879
    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.

    Evidence, AI assistance and curation standards