An elastinolytic enzyme detected in the culture medium of human arterial smooth muscle cells
An elastinolytic enzyme detected in the culture medium of human arterial smooth muscle cells
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DOI：
10.1006/cbir.1993.1149
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发表时间：
1993-09
影响因子：
3.9
通讯作者：
Y. Okada;S. Katsuda;Y. Okada;Isao Nakanishi
中科院分区：
文献类型：
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作者：
Y. Okada;S. Katsuda;Y. Okada;Isao Nakanishi
人动脉平滑肌细胞培养液在弹性蛋白底物凝胶上显示出68和kDa的弹性蛋白溶解活性。酶活性可被金属蛋白酶抑制剂乙二胺四乙酸抑制，但不能被丝氨酸、半胱氨酸和天冬氨酸蛋白酶的其他抑制剂抑制。培养基中的蛋白酶可被4-氨基苯基汞醋酸酯激活，并降解不溶的弹性蛋白。与其他基质金属蛋白酶(MMPs)相比，其活性与从人类风湿滑膜中提纯的MMP2相似，而MMP3和MMP9具有不同的裂解模式，而MMP1没有弹性裂解活性。免疫印迹分析表明，该68 kDa的酶为基质金属蛋白酶-2。免疫荧光研究表明，基质金属蛋白酶-2定位于平滑肌细胞的胞浆中。提示人动脉平滑肌细胞分泌的弹性蛋白水解酶为基质金属蛋白酶-2。
The culture medium of human arterial smooth muscle cells exhibits an elastinolytic activity with 68 and 64 kDa on elastin substrate gels. The enzymatic activities are inhibited by ethylenediamine tetraacetic acid, a metalloproteinase inhibitor, but not by other inhibitors of serine, cysteine and aspartic proteinases. The proteinase in the culture medium is activatable by 4‐aminophenylmercuric acetate and degrades insoluble elastin. Compared to other matrix metalloproteinases (MMP), the activity shows the similar elastinolytic pattern to that by MMP‐2 purified from human rheumatoid synovium, while MMP‐3 and MMP‐9 have different lytic patterns and MMP‐1 possesses no elastinolytic activity. An immunoblot analysis demonstrated that the 68‐kDa enzyme is MMP‐2. An immunofluorescence study illustrates that MMP‐2 is localized within the cytoplasm of the smooth muscle cells. These findings suggest that the elastinolytic enzyme secreted by human arterial smooth muscle cells is MMP‐2.