PROTEASE-NEXIN - A CELLULAR-COMPONENT THAT LINKS THROMBIN AND PLASMINOGEN-ACTIVATOR AND MEDIATES THEIR BINDING TO CELLS
PROTEASE-NEXIN - A CELLULAR-COMPONENT THAT LINKS THROMBIN AND PLASMINOGEN-ACTIVATOR AND MEDIATES THEIR BINDING TO CELLS
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DOI：
10.1016/0092-8674(80)90112-9
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发表时间：
1980-01-01
期刊：
影响因子：
64.5
通讯作者：
CUNNINGHAM, DD
中科院分区：
文献类型：
--
作者：
BAKER, JB;LOW, DA;CUNNINGHAM, DD
鉴定了正常人成纤维细胞的一种组分，其与凝血酶和尿激酶（尿纤溶酶原激活剂）形成共价键，并介导这些蛋白酶的大多数特异性细胞结合。这种成分称为蛋白酶-连接蛋白（PN），与细胞表面结合并释放到培养基中。在几个方面，PN类似于抗凝血酶III（AT 3），一种血清中凝血酶的主要抑制剂：PN可能通过酯键连接凝血酶; PN不连接在其催化位点丝氨酸被阻断的凝血酶; PN具有高亲和力肝素结合位点;肝素大大加速可溶性PN和凝血酶之间的连接速率。尽管有这些相似之处，PN和AT 3是不同的;它们的大小不同，并且没有免疫交叉反应。而AT 3调节凝血酶在血清中的蛋白水解活性，PN可以调节丝氨酸蛋白酶在细胞表面和附近的活性。
A component of normal human fibroblasts which forms a covalent linkage with thrombin and urokinase (urinary plasminogen activator) and mediates most of the specific cellular binding of these proteases was identified. This component, named protease-nexin (PN), is associated with the cell surface and released into the culture medium. In several ways PN resembles antithrombin III (AT3), a prominent inhibitor of thrombin in serum: PN links thrombin, probably via an ester bond; PN does not link thrombin blocked at its catalytic site serine; PN has a high-affinity heparin-binding site; and heparin greatly accelerates the rate of linkage between soluble PN and thrombin. Despite these similarities, PN and AT3 are distinct; they differ in size and are not immunologically cross-reactive. Whereas AT3 regulates the proteolytic activity of thrombin in serum, PN may regulate the activity of serine proteases at and near the cell surface.