体外培养的猴牙周膜成纤维细胞合成的胶原蛋白的性质。
Nature of collagens synthesized by monkey periodontal-ligament fibroblasts in vitro.
作者信息
Limeback H F, Sodek J, Brunette D M
出版信息
Biochem J. 1978 Jan 15;170(1):63-71. doi: 10.1042/bj1700063.
Abstract
- First subcultures of fibroblast-like cells from adult monkey periodontal ligament were incubated in the presence of 14C-labelled amino acids and produced significant amounts of type-I and type-III collagens. 2. The proportion of type-III collagen produced was calculated on the basis of the recovery of procollagens from DEAE-cellulose chromatography to be approx. 20%, and at least 10% when analysed as collagens on CM-cellulose chromatography. 3. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of the procollagens, the collagens and their CNBr peptides was used to confirm the identity of the collagen types. 4. In serum-free media extensive conversion of type-I procollagen, but not of type-III procollagen, into collagen was observed, suggesting that a specific type-I procollagen peptidase was produced. 5. The pattern of collagen synthesis was not significantly different from that obtained with fibroblasts derived from skin corium of the same animals.
摘要
- 取自成年猴牙周韧带的成纤维细胞样细胞的初代传代培养物在含有14C标记氨基酸的条件下孵育，产生了大量的I型和III型胶原蛋白。2. 根据从二乙氨基乙基纤维素色谱法中回收的前胶原计算，所产生的III型胶原蛋白的比例约为20%，当在羧甲基纤维素色谱法上作为胶原蛋白进行分析时，至少为10%。3. 对前胶原、胶原蛋白及其溴化氰肽进行十二烷基硫酸钠/聚丙烯酰胺凝胶电泳，以确认胶原蛋白类型的一致性。4. 在无血清培养基中，观察到I型前胶原大量转化为胶原蛋白，而III型前胶原未发生转化，这表明产生了一种特异性的I型前胶原肽酶。5. 胶原蛋白合成模式与取自同一动物皮肤真皮的成纤维细胞所获得的模式没有显著差异。
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