Generalized inhibition of cell-free translation by the amino-terminal propeptide of chick type I procollagen.
Fragments of the amino-terminal propeptide of procollagen have been shown to inhibit the synthesis of procollagen in cultured cells and in a reticulocyte lysate cell-free system (for review see Timpl, R. and Glanville, R.W. (1981) Clin. Orth. Rel. Res. 158, 224-242). In this report, we show that the full-length amino-terminal propeptide of chick pro alpha1(I) chains inhibits the translation of chick tendon mRNA and rat brain mRNA in a reticulocyte lysate cell-free system. The synthesis of procollagen and non-collagenous proteins was equally affected. Inhibition was dose-dependent up to 10 microM. A similar pattern of inhibition was observed for the collagenase-resistant fragment, col 1(I).
D000818:Animals; D001923:Brain Chemistry; D002474:Cell-Free System; D002645:Chickens; D003094:Collagen / Q000096:biosynthesis / Q000235:genetics; D005246:Feedback; D010446:Peptide Fragments / Q000302:isolation & purification / Q000494:pharmacology*; D011347:Procollagen / Q000302:isolation & purification / Q000494:pharmacology*; D014176:Protein Biosynthesis / Q000187:drug effects*; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D013710:Tendons / Q000032:analysis
D010446:Peptide Fragments; D011347:Procollagen; D012333:RNA, Messenger; C047202:procollagen Type I N-terminal peptide; D003094:Collagen