Collagen prolyl hydroxylation in WI-38 fibroblast cultures: Action of hydralazine |
| |
Authors: | Katherine H Chen Mercedes A Paz Paul M Gallop |
| |
Institution: | (1) The Department of Biological Chemistry and Orthopaedic Surgery, Harvard Medical School and Harvard School of Dental Medicine, 300 Longwood Avenue, 02115 Boston, Massachusetts;(2) The Children's Hospital Medical Center, 300 Longwood Avenue, 02115 Boston, Massachusetts |
| |
Abstract: | Summary The action of hydralazine on collagen prolyl hydroxylation was studied in a cell culture system using WI-38 fibroblasts. The
prolyl hydroxylation level was determined by a method involving the digestion of collagen by bacterial collagenase and the
examination of specific peptides. The presence of low concentrations of hydralazine (0.2 mM) in both “young” and “old” fibroblast
cultures strongly inhibited collagen prolyl hydroxylation. The degree of inhibition was greater in serum-deficient cultures.
No significant improvement in the degree of hydroxylation was observed by increasing either ascorbate or iron levels in the
hydralazine-containing cultures in which hydroxylation was inhibited. Some of the reported side effects of hydralazine seen
in patients might be related to its inhibitory effects on mixed function oxidative (MFO) hydroxylation systems. While the
ascorbate dependence of the prolyl hydroxylase system of WI-38 decreased with the “age” of the culture, hydralazine inhibition
of hydroxylation was dramatic with cultures of all “ages”.
This work was supported by NIH grants nos. AM15671, AM1675 and HD07376, and fellowship no. HD01998. |
| |
Keywords: | collagen prolyl hydroxylation fibroblast hydralazine |
本文献已被 SpringerLink 等数据库收录! |
|