Regulation of collagen synthesis by ascorbic acid.

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.

authors

Murad S,Grove D,Lindberg KA,Reynolds G,Sivarajah A,Pinnell SR

doi

10.1073/pnas.78.5.2879

subject

Has Abstract

pub_date

1981-05-01 00:00:00

pages

2879-82

issue

5

eissn

0027-8424

issn

1091-6490

journal_volume

78

pub_type

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