Assessment of Gelatinases (MMP-2 and MMP-9 by Gelatin Zymography.
Assessment of Gelatinases (MMP-2 and MMP-9 by Gelatin Zymography.
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DOI：
10.1385/1-59259-136-1:163
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发表时间：
2001-01-01
期刊：
影响因子：
--
通讯作者：
Fridman, R
中科院分区：
文献类型：
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作者：
Toth, M;Fridman, R
肿瘤细胞的侵袭和转移已经显示需要蛋白水解活性以降解细胞外基质（ECM）的组分。ECM的水解似乎促进肿瘤细胞迁移，从而促进恶性细胞的转移性播散（1）。与肿瘤转移直接相关的一组主要蛋白酶是基质金属蛋白酶（MMP），这是已知切割许多ECM蛋白的内肽酶家族（1）。MMPs是多结构域蛋白酶，在活性位点含有锌原子，并以潜在的非活性形式（酶原）产生（2）。酶活性的获得需要切割抑制性N-末端结构域（3）。因此，活性形式的产生通常伴随着分子量的降低和活性位点的暴露而发生。一旦激活，所有MMP都被一组称为金属蛋白酶组织抑制剂（TIMP）的内源性蛋白酶抑制剂特异性抑制，其结合到抑制催化活性的活性位点（4）。
The invasion and metastasis of tumor cells has been shown to require proteolytic activity in order to degrade components of the extracellular matrix (ECM). The hydrolysis of the ECM appears to facilitate tumor cell migration contributing to the metastatic dissemination of malignant cells (1). A major group of proteases that has been directly associated with tumor metastasis is the matrix metalloproteinases (MMPs), a family of endopeptidases known to cleave many ECM proteins (1). The MMPs are multidomain proteases that contain a zinc atom in the active site and are produced in a latent inactive form (zymogen) (2). Acquisition of enzymatic activity requires cleavage of the inhibitory N-terminal domain (3). Thus, generation of the active form usually occurs concomitantly with a decrease in molecular mass and exposure of the active site. Once activated, all the MMPs are specifically inhibited by a group of endogenous protease inhibitors known as the tissue inhibitors of metalloproteinases (TIMPs), which bind to the active site inhibiting catalytic activity (4).