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Regulation of collagen synthesis by ascorbic acid.

Open access
Murad, S, Grove, D, Lindberg, K A, Reynolds, G, Sivarajah, A, Pinnell, S R·1981·Proceedings of the National Academy of Sciences

Abstract

After prolonged exposure to ascorbate, collagen synthesis in cultured human skin fibroblasts increased approximately 8-fold with no significant change in synthesis of noncollagen protein. This effect of ascorbate appears to be unrelated to its cofactor function in collagen hydroxylation. The collagenous protein secreted in the absence of added ascorbate was normal in hydroxylysine but was mildly deficient in hydroxyproline. In parallel experiments, lysine hydroxylase (peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase, EC 1.14.11.4) activity increased 3-fold in response to ascorbate administration whereas proline hydroxylase (prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase, EC 1.14.11.2) activity decreased considerably. These results suggest that collage polypeptide synthesis, posttranslational hydroxylations, and activities of the two hydroxylases are independently regulated by ascorbate.

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Metadata

Authors
Murad, S., Grove, D., Lindberg, K. A., Reynolds, G., Sivarajah, A., & Pinnell, S. R.
Venue
Proceedings of the National Academy of Sciences
Published
1981-05
Volume
78
Issue
5
Pages
2879-2882
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2064481190
Cited by
493
References
0
FWCI
7.77
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Regulation of collagen synthesis by ascorbic acid. https://app.cochat.ai/papers/10.1073/pnas.78.5.2879
The paper
Murad, S., Grove, D., Lindberg, K. A., Reynolds, G., Sivarajah, A., & Pinnell, S. R. (1981). Regulation of collagen synthesis by ascorbic acid. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.78.5.2879

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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