Okada Y, Nakanishi I
Department of Pathology, School of Medicine, Kanazawa University, Japan.
FEBS Lett. 1989 Jun 5;249(2):353-6. doi: 10.1016/0014-5793(89)80657-x.
The ability of human neutrophil elastase and cathepsin G to activate matrix metalloproteinase 3 (MMP-3 = stromelysin) and MMP-2 ('gelatinase') purified from human rheumatoid synovial fibroblasts in culture was examined. The zymogen of MMP-3 (proMMP-3) was activated to full activity with elastase and cathepsin G by limited proteolysis of the molecule into two active forms of Mr approximately 45,000 and Mr approximately 25,000. In contrast, proMMP-2 was not activated at all by these neutrophil serine proteinases, although it was degraded into small fragments. These data suggest that neutrophil elastase and cathepsin G may play an important role in the activation of proMMP-3 in vivo in various inflammatory conditions, but proMMP-2 may be activated in different ways.
研究了人中性粒细胞弹性蛋白酶和组织蛋白酶G激活从培养的人类风湿性滑膜成纤维细胞中纯化的基质金属蛋白酶3（MMP - 3 = 基质溶解素）和MMP - 2（“明胶酶”）的能力。MMP - 3的酶原（proMMP - 3）通过分子的有限蛋白水解被弹性蛋白酶和组织蛋白酶G激活至完全活性，形成两种活性形式，分子量分别约为45,000和25,000。相反，proMMP - 2虽然被这些中性粒细胞丝氨酸蛋白酶降解成小片段，但根本未被激活。这些数据表明，中性粒细胞弹性蛋白酶和组织蛋白酶G可能在各种炎症条件下的体内proMMP - 3激活中起重要作用，但proMMP - 2可能以不同方式被激活。
