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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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Detalles Bibliográficos
Autor principal: Pinnell, S. R.
Formato: Texto
Lenguaje:English
Publicado: Yale Journal of Biology and Medicine 1985
Materias:
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.
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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
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