Expression and activity of matrix metalloproteases in human malignant mesothelioma cell lines
Expression and activity of matrix metalloproteases in human malignant mesothelioma cell lines
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DOI：
10.1002/1097-0215(200002)9999:9999
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发表时间：
2001-03-01
影响因子：
6.4
通讯作者：
Klominek, J
中科院分区：
文献类型：
--
作者：
Liu, ZW;Ivanoff, A;Klominek, J
由多种人类肿瘤细胞分泌的细胞外基质金属蛋白酶（MMPs）在肿瘤细胞的侵袭和转移中起着至关重要的作用，但其在恶性间皮瘤（MM）细胞中的表达尚未被研究。在这项研究中，我们已经调查了8个MM细胞系产生的MMPs和金属蛋白酶组织抑制剂（TIMPs）的光谱。RT-PCR检测结果显示，所有MM细胞株均表达MMP-1（间质胶原酶）、MMP-2（明胶酶A）、MMP-3（基质溶解素-I）、MMP-9（明胶酶B）和TIMP 1、2和3的mRNA，6/8例MM细胞株表达MMP-7（基质溶解素），3/8例MM细胞株表达MMP-10（基质溶解素-2）。在任何MM细胞系中均未检测到MMP-II（基质分解素-3）。此外，所有MM细胞株均分泌66 kDa的金属蛋白酶，而3/8的MM细胞株分泌46、48、51和63 kDa的金属蛋白酶，其特异性降解细胞外基质组分纤连蛋白、玻连蛋白和层粘连蛋白。我们的结果揭示了MM细胞产生的广泛的MMPs和TIMP，并表明MMPs的不同底物特异性可能在MM细胞侵袭中发挥作用。(C)2001 Wiley-Liss，Inc.
The extracellular matrix metalloproteases (MMPs) secreted by various human tumor cells play a crucial role in tumor cell invasion and metastasis, but their expression in malignant mesothelioma (MM) cells has not been examined. In this study, we have investigated the spectrum of MM Ps and tissue inhibitors of metalloproteases (TIMPs) produced by 8 MM cell lines. Using RT-PCR, we found that all investigated MM cell lines expressed genes encoding mRNA for MMP-1 (interstitial collagenase), MMP-2 (gelatinase A), MMP-3 (stromelysin-I), MMP-9 (gelatinase B) and TIMPs 1, 2 and 3, We also found that 6/8 MM cell lines expressed MMP-7 (matrilysin) and 3/8 MM cell lines expressed MMP-10 (stromelysin-2). MMP-II (stromelysin-3) was not detected in any of the MM cell lines. Production of MMP-2 and MMP-9 was confirmed using gelatin zymography, In addition, all MM cell lines secreted a 66 kDa metalloprotease, while 3/8 MM cell lines secreted 46, 48, 51 and 63 kDa metalloproteases which specifically degraded the extracellular matrix components fibronectin, vitronectin and laminin, The 66 kDa protease was identified as MMP-3 by Western blot. Our results reveal a broad spectrum of MMPs and TIMPs produced by MM cells and indicate that different substrate specificities of MMPs may play a role in MM cell invasion. (C) 2001 Wiley-Liss, Inc.