Collagen biosynthesis by human skin fibroblasts III. The effects of ascorbic acid on procollagen production and prolyl hydroxylase activity |
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Authors: | Barbara A. Booth Jouni Uitto |
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Affiliation: | 1. Department of Dermatology, Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA;2. Division of Dermatology, Department of Medicine, Harbor-UCLA Medical Center, Torrance, CA 90509, U.S.A. |
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Abstract: | Human skin fibroblasts were cultured under conditions optimized for collagen synthesis, and the effects of ascorbic acid on procollagen production, proline hydroxylation and the activity of prolyl hydroxylase were examined in cultures. The results indicated that addition of ascorbic acid to confluent monolayer cultures of adult human skin fibroblasts markedly increased tha amount of [3H]hydroxyproline syntehsized. Ascorbic acid, however, did not increase the synthesis of 3H-labeled collagenous polypeptides assayed independently of hydroxylation of proline residues, nor did it affect the amount of prolyl hydroxylase detectable by an in vitro enzyme assay. Also long-term cultures of the cells or initiation of fibroblast cultures in the presence of ascorbic acid did not lead to an apparent selection of a cell population which might be abnormally responsive to ascorbic acid. Thus, ascorbic acid appears to have one primary action on the synthesis of procollagen by cultured human skin fibroblasts: it is necessary for synthesis of hydroxyproline, and consequently for proper triple helix formation and selection of procollagen. |
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Keywords: | Collagen synthesis Ascorbic acid Procollagen Prolyl hydroxylase (Human skin fibroblast) Hepes Tris 2-amino-2-hydroxymethyl-1,3-propanediol |
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