Synthesis and processing of a type I procollagen containing shortened pro-alpha 1(I) chains by fibroblasts from a patient with osteogenesis imperfecta.
作者： C J Williams , D J Prockop
DOI: 10.1016/S0021-9258(20)81983-8
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摘要: Skin fibroblasts from a patient with lethal form of osteogenesis imprefecta were found to synthesize equal amounts normal pro-alpha 1(I) chains and which are about 10% shorter because deletion 100 amino acids in the middle alpha chain domain. The incorporated into three different kinds trimers: type I trimer length chains; Is one shortened two Iss containing 2(I) chain. As judged by resistance digestion chymotrypsin trypsin, trimers denatured at temperature least 3 degrees C lower than procollagen. Procollagen was slowly secreted cells but degraded extracellular proteinases within 6 h chase medium. results indicated that presence procollagen produces delay rate helix formation, overmodification polypeptides post-translational enzymes, decrease thermal stability trimers, increased susceptibility protein endogenous proteinases. Additionally, this synthesized III-like species unusual chromatographic properties.
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