[Biosynthesis and properties of collagen forming in the cartilage of chick embryos in the presence of various proline analogs].
Effect of proline analogues on biosynthesis and properties of collagen in chick embryo cartilage was studied. Azethidine-2-carboxylic acid, 3,4-dehydroproline, cis-fluoro-proline, cis-hydroxyproline and thiazolidine-4-carboxylic acid were found to inhibit the incorporation of 14C-proline into proteins by 66-89%. Introduction of proline analogues, instead of the amino acid, into the polypeptide chains of collagen caused the impairment of the enzymatic hydroxylation of the proline residues (formation of hydroxyproline). 3,4-dehydroproline possessed the highest inhibitory effect (80%) on formation of hydroxyproline. When it was introduced into alpha-chains of protocollagen, 3,4-dehydroproline inhibited 1.5-6-fold the cleavage of the protein by bacterial collagenase.
D000818:Animals; D001383:Azetidinecarboxylic Acid / Q000494:pharmacology; D002250:Carbon Radioisotopes; D002264:Carboxylic Acids / Q000494:pharmacology; D002356:Cartilage / Q000378:metabolism*; D002642:Chick Embryo / Q000378:metabolism*; D003094:Collagen / Q000096:biosynthesis*; D006900:Hydroxylation; D006909:Hydroxyproline / Q000096:biosynthesis / Q000494:pharmacology; D007553:Isotope Labeling; D003012:Microbial Collagenase / Q000037:antagonists & inhibitors; D011347:Procollagen / Q000096:biosynthesis; D011392:Proline / Q000031:analogs & derivatives* / Q000037:antagonists & inhibitors; D013844:Thiazoles / Q000494:pharmacology
D002250:Carbon Radioisotopes; D002264:Carboxylic Acids; D011347:Procollagen; D013844:Thiazoles; D001383:Azetidinecarboxylic Acid; D003094:Collagen; D011392:Proline; D003012:Microbial Collagenase; D006909:Hydroxyproline
Biosintez i svoistva kollagena, obrazuiushchegosia v khriashchevoĭ tkani kurinykh embrionov v prisutstvii razlichnykh analogov prolina