The translation, assembly, and release of polysome-associated type I collagen pro alpha chains

he production and assembly of type I procollagen is a complex process. Two types of individual subunit chains, translated upon different mRNAs, must be coordinately synthesized, co-translationally modified and brought together in a 2:1 ratio. The objective of this work was to examine the assembly process at the nascent polypeptide chain level. Pro ;An endoplasmic reticulum resident, collagen and gelatin-binding heat shock glycoprotein, hsp47, has been postulated to act as a chaperone protein for type I collagen. Both monoclonal and polyclonal antibodies to hsp47 were found to co-immunoprecipitate...