Chen J K, Green G, Weinberg C B
Department of Physiology, Chang Gung Medical College, Taiwan, Republic of China.
Exp Cell Res. 1991 Apr;193(2):297-302. doi: 10.1016/0014-4827(91)90100-9.
Conditioned media collected from arterial endothelial cells contain protein factor(s) that promotes the contraction of collagen lattices made with skin fibroblasts. Based on the lattice contraction-promoting activity, a protein with an apparent molecular weight of 22 kDa was identified. This 22-kDa protein stimulated lattice contraction in both serum-containing and serum-free media. When assayed at a 30% equivalent of the conditioned medium, the contraction-promoting activity of the purified factor was about 50 to 60% of that elicited by the unfractionated conditioned medium. Some contraction-promoting activity was also present in certain subfractions of the conditioned medium generated during the separation of the 22-kDa protein. Taken together, the results indicate that the lattice contraction-promoting activity in the endothelial cell-conditioned medium is probably aided by multiple active principles. The biochemical and biological characteristics indicated that the 22-kDa protein is not a transforming growth factor-beta-related factor nor a fibroblast growth promoter.
从动脉内皮细胞收集的条件培养基含有促进由皮肤成纤维细胞制成的胶原晶格收缩的蛋白质因子。基于促进晶格收缩的活性,鉴定出一种表观分子量为22 kDa的蛋白质。这种22 kDa的蛋白质在含血清和无血清培养基中均刺激晶格收缩。当以条件培养基的30%当量进行测定时,纯化因子的促进收缩活性约为未分级条件培养基引发活性的50%至60%。在分离22 kDa蛋白质过程中产生的条件培养基的某些亚组分中也存在一些促进收缩的活性。综合来看,结果表明内皮细胞条件培养基中促进晶格收缩的活性可能由多种活性成分辅助。生化和生物学特性表明,22 kDa的蛋白质既不是转化生长因子-β相关因子,也不是成纤维细胞生长促进剂。