Interactions of serine proteases with cultured fibroblasts.
Interactions of serine proteases with cultured fibroblasts.
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丝氨酸蛋白酶与培养的成纤维细胞的相互作用。
DOI：
10.1002/jcb.240320405
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发表时间：
1986
影响因子：
4
通讯作者：
Campbell,CH
中科院分区：
文献类型：
--
作者：
Cunningham,DD;VanNostrand,WE;Farrell,DH;Campbell,CH
本文综述了几种丝氨酸蛋白酶，特别是尿激酶，凝血酶和弹性蛋白酶，与培养的成纤维细胞相互作用的机制。这些研究中的许多是由这些蛋白酶与细胞和细胞外基质的相互作用在许多生理和病理过程中是重要的发现所促使的。已经确定了这些蛋白酶与成纤维细胞特异性相互作用的两种主要途径。一种是游离蛋白酶的表面结合位点，它们似乎只结合一种特定的蛋白酶。尿激酶、凝血酶和弹性蛋白酶的结合位点共同具有的一个不寻常的特征是，结合的蛋白酶不能被成纤维细胞可检测地内化。丝氨酸蛋白酶与成纤维细胞相互作用的另一途径涉及称为蛋白酶连接蛋白（PN）的蛋白质。已确定三个PN。它们由成纤维细胞分泌并通过与蛋白酶催化位点丝氨酸形成共价复合物来抑制某些丝氨酸蛋白酶。然后，复合物通过复合物的PN部分结合回成纤维细胞，并被内化和降解。最近的研究表明，成纤维细胞表面和细胞外基质加速了PN-1对凝血酶的灭活，这支持了PN控制细胞表面及其附近蛋白酶活性的假设。PN与血浆蛋白酶抑制剂的不同之处在于其分子特性、在血浆中的不存在、合成位点和抑制剂：蛋白酶复合物的清除位点。
This review summarizes the mechanisms by which several serine proteases, particularly urokinase, thrombin, and elastase, interact with cultured fibroblasts. Many of these studies were prompted by findings that interactions of these proteases with cells and the extracellular matrix are important in a number of physiologic and pathologic processes. Two main pathways have been identified for specific interactions of these proteases with fibroblasts. One involves surface binding sites for the free protease that appear to bind only one particular protease. An unusual feature collectively shared by the binding sites for urokinase, thrombin, and elastase is that the bound protease is not detectably internalized by the fibroblasts. The other pathway by which serine proteases interact with fibroblasts involves proteins named protease nexins (PNs). Three PNs have been identified. They are secreted by fibroblasts and inhibit certain serine proteases by forming a covalent complex with the protease catalytic site serine. The complexes then bind back to the fibroblasts via the PN portion of the complex and are internalized and degraded. Recent studies showing that the fibroblast surface and extracellular matrix accelerate the inactivation of thrombin by PN‐1 support the hypothesis that the PNs control protease activity at and near the cell surface. The PNs differ from plasma protease inhibitors in their molecular properties, absence in plasma, site of synthesis, and site of clearance of the inhibitor:protease complexes.