Regulation of type I collagen synthesis. Total pro alpha 1(I) and pro alpha 2(I) mRNAs are maintained in a 2:1 ratio under varying rates of collagen synthesis.

The type I collagen molecule contains two alpha 1(I) chains and one alpha 2(I) chain. Previous investigations, using embryonic chick calvaria, have indicated that the two chains are synthesized in a 2:1 ratio which is controlled at a pretranslational level, since the cells contain twice as much translatable pro alpha 1(I) mRNA as pro alpha 2(I) mRNA. The present report describes hybridization analyses of the cellular levels of total cellular RNAs coding for the pro alpha 1(I) and pro alpha 2(I) chains, using as probes two cloned cDNAs complementary to chick pro alpha 1(I) and pro alpha 2(I) mRNA, respectively. Total cellular RNA was extracted from embryonic chick calvaria, pro alpha 1(I) and pro alpha 2(I) RNA sequences were quantified by Northern hybridization using conditions ensuring that hybridization efficiency and specific radioactivity were the same for the two probes. Similar analyses were carried out on RNA extracted from calvaria with different levels of collagen synthesis after culture in the presence or absence of ascorbic acid. The results for all samples analyzed indicate that total cellular pro alpha 1(I) and pro alpha 2(I) mRNAs are present in a 2:1 ratio which is maintained even during variations in collagen synthesis rate. There is no evidence for regulation mediated by different rates of processing of mRNA precursors, although preferential degradation of the pro alpha 2(I) gene transcript cannot be excluded. Thus, the synthesis of type I procollagen chains is presumably coordinated by transcriptional control.