Regulation of collagen synthesis by ascorbic acid.
作者： S. Murad , D. Grove , K. A. Lindberg , G. Reynolds , A. Sivarajah
关键词: Hydroxylation 、 Oxidoreductase 、 Procollagen-proline dioxygenase 、 Hydroxyproline 、 Hydroxylysine 、 Cofactor 、 Biochemistry 、 Biology 、 Human skin 、 Ascorbic acid
摘要: After prolonged exposure to ascorbate, collagen synthesis in cultured human skin fibroblasts increased approximately 8-fold with no significant change of noncollagen protein. This effect ascorbate appears be unrelated its cofactor function hydroxylation. The collagenous protein secreted the absence added was normal hydroxylysine but mildly deficient hydroxyproline. In parallel experiments, lysine hydroxylase (peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase, EC 1.14.11.4) activity 3-fold response administration whereas proline (prolyl-glycyl-peptide, oxidoreductase, 1.14.11.2) decreased considerably. These results suggest that collage polypeptide synthesis, posttranslational hydroxylations, and activities two hydroxylases are independently regulated by ascorbate.
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