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Regulation of collagen biosynthesis by ascorbic acid: a review.
L-ascorbic acid is an essential cofactor for lysyl hydroxylase and prolyl hydroxylase, enzymes essential for collagen biosynthesis. In addition, L-ascorbic acid preferentially stimulates collagen synthesis in a manner which appears unrelated to the effect of L-ascorbic acid on hydroxylation reaction...
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Formato: | Texto |
Lenguaje: | English |
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Yale Journal of Biology and Medicine
1985
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2589959/ https://www.ncbi.nlm.nih.gov/pubmed/3008449 |
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author | Pinnell, S. R. |
author_facet | Pinnell, S. R. |
author_sort | Pinnell, S. R. |
collection | PubMed |
description | L-ascorbic acid is an essential cofactor for lysyl hydroxylase and prolyl hydroxylase, enzymes essential for collagen biosynthesis. In addition, L-ascorbic acid preferentially stimulates collagen synthesis in a manner which appears unrelated to the effect of L-ascorbic acid on hydroxylation reactions. This reaction is stereospecific and unrelated to intracellular degradation of collagen. The effect apparently occurs at a transcriptional or translational level, since L-ascorbic acid preferentially stimulates collagen-specific mRNA. In addition, it stimulates lysyl hydroxylase activity but inhibits prolyl hydroxylase activity in human skin fibroblasts in culture. |
format | Text |
id | pubmed-2589959 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1985 |
publisher | Yale Journal of Biology and Medicine |
record_format | MEDLINE/PubMed |
spelling | pubmed-25899592008-11-28 Regulation of collagen biosynthesis by ascorbic acid: a review. Pinnell, S. R. Yale J Biol Med Research Article L-ascorbic acid is an essential cofactor for lysyl hydroxylase and prolyl hydroxylase, enzymes essential for collagen biosynthesis. In addition, L-ascorbic acid preferentially stimulates collagen synthesis in a manner which appears unrelated to the effect of L-ascorbic acid on hydroxylation reactions. This reaction is stereospecific and unrelated to intracellular degradation of collagen. The effect apparently occurs at a transcriptional or translational level, since L-ascorbic acid preferentially stimulates collagen-specific mRNA. In addition, it stimulates lysyl hydroxylase activity but inhibits prolyl hydroxylase activity in human skin fibroblasts in culture. Yale Journal of Biology and Medicine 1985 /pmc/articles/PMC2589959/ /pubmed/3008449 Text en |
spellingShingle | Research Article Pinnell, S. R. Regulation of collagen biosynthesis by ascorbic acid: a review. |
title | Regulation of collagen biosynthesis by ascorbic acid: a review. |
title_full | Regulation of collagen biosynthesis by ascorbic acid: a review. |
title_fullStr | Regulation of collagen biosynthesis by ascorbic acid: a review. |
title_full_unstemmed | Regulation of collagen biosynthesis by ascorbic acid: a review. |
title_short | Regulation of collagen biosynthesis by ascorbic acid: a review. |
title_sort | regulation of collagen biosynthesis by ascorbic acid: a review. |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2589959/ https://www.ncbi.nlm.nih.gov/pubmed/3008449 |
work_keys_str_mv | AT pinnellsr regulationofcollagenbiosynthesisbyascorbicacidareview |