Murakami A, Konomi H, Itokazu N, Arima M, Sakuragawa N, Nakajima A, Tanaka M, Tajima S, Hayashi T, Kino J
Division of Mental Retardation and Birth Defect Research, National Center of Neurology and Psychiatry, Tokyo.
J Biochem. 1989 Sep;106(3):490-4. doi: 10.1093/oxfordjournals.jbchem.a122879.
Production of an unusual collagenous protein was observed in culture of dermal fibroblasts from four patients with Marfan syndrome. The apparent molecular weight of the protein was about 185 kDa after reduction with 2-mercaptoethanol and 175 kDa after limited pepsin treatment. The 185 kDa protein was susceptible to the bacterial collagenase but resistant to the animal collagenase. Immunoprecipitation revealed the specific interaction of the pepsin-treated 175 kDa collagenous protein with monoclonal and polyclonal antibodies to human type IV collagen. From the patterns of CNBr peptide mapping the 185 kDa band was identified as alpha 1 (IV) chain. Type IV collagen in the skin is generally considered to be of non-fibroblastic origin. However, in "diseased" condition, dermal fibroblasts might produce type IV collagen. The clinical manifestation in relation to production of type IV collagen by cultured skin fibroblasts from Marfan patients is discussed.
在对四名马凡综合征患者的真皮成纤维细胞进行培养时，观察到一种异常胶原蛋白质的产生。用2-巯基乙醇还原后，该蛋白质的表观分子量约为185 kDa，经有限的胃蛋白酶处理后为175 kDa。185 kDa的蛋白质对细菌胶原酶敏感，但对动物胶原酶有抗性。免疫沉淀显示，经胃蛋白酶处理的175 kDa胶原蛋白质与抗人IV型胶原的单克隆和多克隆抗体有特异性相互作用。从溴化氰肽图谱模式来看，185 kDa条带被鉴定为α1(IV)链。皮肤中的IV型胶原通常被认为是非成纤维细胞来源的。然而，在“患病”状态下，真皮成纤维细胞可能会产生IV型胶原。本文讨论了马凡综合征患者培养的皮肤成纤维细胞产生IV型胶原与临床表现的关系。
