Release of basic fibroblast growth factor-heparan sulfate complexes from endothelial cells by plasminogen activator-mediated proteolytic activity.
Release of basic fibroblast growth factor-heparan sulfate complexes from endothelial cells by plasminogen activator-mediated proteolytic activity.
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通过纤溶酶原激活剂介导的蛋白水解活性从内皮细胞释放碱性成纤维细胞生长因子-硫酸乙酰肝素复合物。
DOI：
10.1083/jcb.110.3.767
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发表时间：
1990
期刊：
影响因子：
--
通讯作者：
Rifkin,DB
中科院分区：
文献类型：
--
作者：
Saksela,O;Rifkin,DB
Cultured bovine capillary endothelial (BCE) cells synthesize heparan sulfate proteoglycans (HSPG), which are both secreted into the culture medium and deposited in the cell layer. The nonsoluble HSPGs can be isolated as two predominant species: a larger 800-kD HSPG, which is recovered from preparations of extracellular matrix, and a 250-kD HSPG, which is solubilized by nonionic detergent extraction of the cells. Both HSPG species bind bFGE~ 25I-bFGF bound to BCE cell cultures is readily released by either heparinase or plasmin. When released by plasmin, the growth factor is recovered from the incubation medium as a complex with the partly degraded high molecular mass HSPG. Endogenous bFGF activity is released by a proteolytic treatment of cultured BCE cells.
