Component
Collagen synthesis
Collagen synthesis. Species, exposure and limitations are retained in each linked claim.
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.
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
Collagen synthesis in ascorbate-deficient guinea pigs is decreased with only moderate effects on proline hydroxylation, proteoglycan synthesis which does not require ascorbate is also decreased, both correlate with weight loss, and the inhibition is reversed by IGF-I, the inhibitor appearing to be two IGF-binding proteins induced during deficiency and starvation.
Experimental context and source evidence
- availability_state
- nutrient_deficiency Imported condition classification; unverified.
- evidence_span
- {"source_cache": "artifacts/hbot-research/1720597.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b769da8d030351b117b7a349262e9b52d54aab00ca3a2679900cb1372006bc31", "start_char": 0, "end_char": 1015, "text_sha256": "b769da8d030351b117b7a349262e9b52d54aab00ca3a2679900cb1372006bc31"}
- experimental_model
- Ascorbate-deficient guinea pigs, fasting controls, and cells cultured in scorbutic serum
- exposure
- Vitamin C deficiency, with fasting plus ascorbate supplementation as a comparison
- limitations
- The study separates a direct hydroxylation defect from a growth-factor-mediated one, so it argues against reading scurvy as pure under-hydroxylation.
- nutrient_topic
- Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
- organism
- Guinea pig and cultured cells
- plain_language
- Scurvy lowers collagen by more than one route, and one of them is not about the hydroxylation step at all.
- primary_references
- [hbot-p1720597] Ascorbate requirement for hydroxylation and secretion of procollagen: relationship to inhibition of collagen synthesis in scurvy. (1991). https://pubmed.ncbi.nlm.nih.gov/1720597/ DOI: 10.1093/ajcn/54.6.1135s
- tissue_or_cell_type
- Connective tissue
- trigger_kind
- nutrient_deficiency Imported condition classification; unverified.
Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 920–931
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ascorbate-deficient guinea pigs, fasting controls, and cells cultured in scorbutic serum · source_derived_draft · unverified_draft
### hbot-scurvy-beyond-hydroxylation Collagen synthesis in ascorbate-deficient guinea pigs is decreased with only moderate effects on proline hydroxylation, proteoglycan synthesis which does not require ascorbate is also decreased, both correlate with weight loss, and the inhibition is reversed by IGF-I, the inhibitor appearing to be two IGF-binding proteins induced during deficiency and starvation. Condition category: nutrient_deficiency nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: Scurvy lowers collagen by more than one route, and one of them is not about the hydroxylation step at all. organism: Guinea pig and cultured cells tissue_or_cell_type: Connective tissue experimental_model: Ascorbate-deficient guinea pigs, fasting controls, and cells cultured in scorbutic serum limitations: The study separates a direct hydroxylation defect from a growth-factor-mediated one, so it argues against reading scurvy as pure under-hydroxylation. exposure: Vitamin C deficiency, with fasting plus ascorbate supplementation as a comparison evidence_span: {"source_cache": "artifacts/hbot-research/1720597.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b769da8d030351b117b7a349262e9b52d54aab00ca3a2679900cb1372006bc31", "start_char": 0, "end_char": 1015, "text_sha256": "b769da8d030351b117b7a349262e9b52d54aab00ca3a2679900cb1372006bc31"} [hbot-p1720597] Ascorbate requirement for hydroxylation and secretion of procollagen: relationship to inhibition of collagen synthesis in scurvy. (1991). https://pubmed.ncbi.nlm.nih.gov/1720597/ DOI: 10.1093/ajcn/54.6.1135s
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.