Effect of prevention of procollagen triple-helix formation on proline 3-hydroxylation in freshly isolated chick-embryo tendon cells.
Inhibition of procollagen triple-helix formation by the addition of cis-hydroxyproline or azetidine-2-carboxylic acid increased the synthesis of 3-hydroxy[14C]proline 1.7-1.8-fold in pulse-chase experiments with freshly isolated chick-embryo tendon cells. The amount of 3-hydroxy[14C]proline, expressed as a percentage of the total 14C radioactivity in hydroxyproline, reached 8.4%. Control experiments indicated that the two analogues had no effect on the prolyl 3-hydroxylase activity of these cells. The data suggest that the time available before triple-helix formation in part regulates the extent of the 3-hydroxylation of proline in the biosynthesis of collagen in intact cells.
D000818:Animals; D001383:Azetidinecarboxylic Acid / Q000494:pharmacology*; D001385:Azetines / Q000494:pharmacology*; D002642:Chick Embryo; D006900:Hydroxylation; D006909:Hydroxyproline / Q000096:biosynthesis* / Q000494:pharmacology; D066298:In Vitro Techniques; D011347:Procollagen / Q000096:biosynthesis*; D011393:Procollagen-Proline Dioxygenase / Q000378:metabolism; D011487:Protein Conformation / Q000187:drug effects; D013710:Tendons / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*
D001385:Azetines; D011347:Procollagen; D001383:Azetidinecarboxylic Acid; D011393:Procollagen-Proline Dioxygenase; D006909:Hydroxyproline