纤溶酶
纤溶酶原激活剂
角质形成细胞
尿激酶
体内
表皮(动物学)
化学
激活剂(遗传学)
劈理(地质)
体外
生物化学
分子生物学
酶
细胞生物学
生物
受体
内分泌学
解剖
古生物学
遗传学
生物技术
断裂(地质)
作者
Koji Hashimoto,Janet H. Prystowsky,Janet Baird,Gerald S. Lazarus,Pamela J. Jensen
标识
DOI:10.1111/1523-1747.ep12462057
摘要
Urokinase-type plasminogen activator (uPA) is produced and secreted by cultured human keratinocytes as a single chain precursor. UPA in keratinocyte conditioned medium is not susceptible to inhibition with diisopropylfluorophosphate (DFP), and it has an apparent molecular weight of 55 kD under both reducing and nonreducing conditions. Cleavage of keratinocyte uPA by plasmin results in the formation of a 96 kD complex comprised of activated uPA and PA inhibitor 2. PA extracted from normal human epidermis is only partially inhibited by DFP, suggesting that precursor uPA is also present in vivo. The synthesis of uPA as a precursor with reduced enzymatic activity as well as decreased affinity for inhibitors is likely to be a mechanism by which normal epidermis regulates plasminogen activation in vivo.
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