Seiki M
Department of Cancer Cell Research, Institute of Medical Science, University of Tokyo, Japan.
APMIS. 1999 Jan;107(1):137-43. doi: 10.1111/j.1699-0463.1999.tb01536.x.
Matrix metalloproteinases (MMP) degrade components of extracellular matrix (ECM), and thereby regulate formation, remodeling and maintenance of tissue. Abnormal function of cell surface proteases associated with malignant tumors may contribute directly to the invasive and malignant nature of the cells. Among the MMP's associated with the tumor cell surface, gelatinase A is believed to be particularly important, since it degrades type IV collagen, and is activated in a tumor specific manner, correlating with tumor spread and poor prognosis. Activation of pro-gelatinase A is uniquely regulated by a cell-mediated mechanism. This study describes an in vitro model that mimics the cell-surface activation mechanism. The expression of MT-MMP could not be detected in normal epithelial cells, but can be seen in transformed epithelial carcinoma cells.
基质金属蛋白酶(MMP)可降解细胞外基质(ECM)的成分,从而调节组织的形成、重塑和维持。与恶性肿瘤相关的细胞表面蛋白酶功能异常可能直接导致细胞的侵袭性和恶性特征。在与肿瘤细胞表面相关的MMP中,明胶酶A被认为尤为重要,因为它可降解IV型胶原蛋白,并以肿瘤特异性方式被激活,这与肿瘤扩散和不良预后相关。前明胶酶A的激活由细胞介导的机制独特调控。本研究描述了一种模拟细胞表面激活机制的体外模型。在正常上皮细胞中未检测到MT-MMP的表达,但在转化的上皮癌细胞中可见。