Deletion of the pro-alpha 1(I) N-propeptide affects secretion of type I collagen in Chinese hamster lung cells but not in Mov-13 mouse cells.

摘要: We have introduced two mutations into a full-length human pro-alpha 1(I) cDNA that delete 114 amino acids or the entire 139 of N-propeptide domain. Wild-type and mutated versions were cultured Chinese hamster lung (CHL) cells, which do not produce endogenous type I collagen, Mov-13 mouse 2(I) chains but chains. As judged by resistance to proteases, neither mutation impaired intracellular triple helical assembly alpha homotrimers in CHL chimeric collagen comprised cells. Thus, is necessary for main domain collagen. In cells rate secretion mutant was greatly reduced as compared wild homotrimers, immunofluorescence immunoelectron microscopy, shown be accumulated large vesicular expansions rough endoplasmic reticulum. When such retransfected with encoding wild-type chains, rescued heterotrimers containing also retained vesicles. By contrast, deletion did affect from an intact appears efficient some all cell types.