Proteases associated with invadopodia, and their role in degradation of extracellular matrix
Proteases associated with invadopodia, and their role in degradation of extracellular matrix
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DOI：
10.1159/000468616
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发表时间：
1996-01-01
期刊：
影响因子：
--
通讯作者：
Chen, WT
中科院分区：
文献类型：
--
作者：
Chen, WT
转移癌细胞利用接触并溶解基质的质膜突起（侵入伪足）侵入细胞外基质。有证据表明，膜相关蛋白酶、170-kD 明胶酶 (seprase) 和明胶酶 A 对侵袭伪足发挥作用机制。还讨论了其他金属和丝氨酸类型的膜蛋白酶，包括膜型基质金属蛋白酶、meprin、二肽基肽酶 IV、成纤维细胞活化蛋白 a 和胍基苯甲酸酶在细胞表面蛋白水解中发挥的潜在作用。有人提出，在侵袭伪足上形成结构和功能连接的蛋白酶复合物使得癌细胞能够侵入细胞外基质。
Metastasizing cancer cells invade the extracellular matrix using plasma membrane protrusions (invadopodia) that contact and dissolve the matrix. Evidence suggests that membrane-associated proteases, 170-kD gelatinase (seprase) and Gelatinase A, exert their mechanisms of action on invadopodia. Potential roles that other metallo- and serine-types of membrane proteases, including membrane-type matrix metalloprotease, meprin, dipeptidyl peptidase IV, fibroblast activation protein a and guanidinobenzoatase, play in the cell surface proteolysis are also discussed. It is proposed that formation of a structurally and functionally linked protease complex on invadopodia allows the invasion of cancer cells into the extracellular matrix.