Inhibition of procollagen cell-free synthesis by amino-terminal extension peptides.
Peptides prepared from the amino termini of pro alpha 1(I) and pro alpha 1(III) collagen chains inhibit the production of pro alpha 1(I) and pro alpha 2 by rat calvaria rna in a reticulocyte cell-free system. The synthesis of other proteins was not altered, suggesting a specific effect on collagen production. Various peptides from the helical region of the alpha 1(I) chain did not alter translation. These studies, taken together with earlier studies showing inhibition of collagen synthesis by cells in culture receiving the amino-terminal peptides, are consistent with a regulatory function in collagen synthesis for the amino-terminal peptides from procollagen.
D000818:Animals; D000831:Animals, Newborn; D001842:Bone and Bones / Q000378:metabolism; D002474:Cell-Free System; D007700:Kinetics; D010455:Peptides / Q000494:pharmacology*; D011347:Procollagen / Q000096:biosynthesis*; D014176:Protein Biosynthesis / Q000187:drug effects*; D012313:RNA / Q000378:metabolism; D011817:Rabbits; D051381:Rats; D012156:Reticulocytes / Q000378:metabolism; D013329:Structure-Activity Relationship
D010455:Peptides; D011347:Procollagen; D012313:RNA