THE MATRIX METALLOPROTEINASES AND THEIR INHIBITORS
THE MATRIX METALLOPROTEINASES AND THEIR INHIBITORS
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DOI：
10.1165/ajrcmb/7.2.120
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发表时间：
1992-08-01
影响因子：
6.4
通讯作者：
DOCHERTY, AJP
中科院分区：
文献类型：
--
作者：
MURPHY, G;DOCHERTY, AJP
许多降解结缔组织细胞外基质的金属蛋白酶和两种特异性金属蛋白酶组织抑制剂（TIMPs）现已被分离、鉴定和克隆。酶序列的比较已经允许域结构的描绘，并且已经进行了初步研究以评估这些域对其生化和生物学特性的贡献，包括激活、由TIMP抑制和基质结合。这些事件代表了金属蛋白酶活性的细胞外调节的主要水平，这被认为是其控制的一个重要方面。激活可能是一种细胞表面现象，涉及纤溶酶原激活剂级联或其他膜相关机制。TIMPs的抑制作用被假定为在激活中与在基质的酶降解的随后调节中一样重要。
A number of metalloproteinases that degrade the extracellular matrix of connective tissues and two specific tissue inhibitors of metalloproteinases (TIMPs) have now been isolated, characterized, and cloned. Comparison of the enzyme sequences has allowed the delineation of domain structures, and initial studies have been carried out to assess the contribution of these domains to their biochemical and biologic properties, including activation, inhibition by TIMPs, and matrix binding. Such events represent the major levels of extracellular regulation of metalloproteinase activity, which is thought to be an important aspect of their control. Activation is probably a cell surface phenomenon, involving the plasminogen activator cascade or other membrane-associated mechanisms. The inhibitory action of TIMPs is postulated to be as important in activation as in the subsequent regulation of enzyme degradation of the matrix.