Seprase complexes in cellular invasiveness

被引：100

作者：

Chen, WT ^{[1
]}

Kelly, T

机构：

[1] SUNY Stony Brook, Dept Med, Div Neoplast Dis, Stony Brook, NY 11794 USA

[2] Arkansas Canc Res Ctr, Dept Pathol, Little Rock, AR 72205 USA

来源：

CANCER AND METASTASIS REVIEWS | 2003年 / 22卷 / 2-3期

关键词：

seprase; FAP alpha; DPP4; invasion; angiogenesis; metastasis; wound healing;

D O I：

10.1023/A:1023055600919

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

A group of type II integral serine proteases, including dipeptidyl peptidase IV (DPP4/CD26), seprase/fibroblast activation protein alpha (FAPalpha) and related type II transmembrane prolyl serine peptidases, exert their mechanisms of action on the cell surface. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. Localization of the protease complexes at cell surface protrusions, called invadopodia, may have a prominent role in processing soluble factors (including chemokines and neuropeptide Y) and in degrading locally extracellular matrix components, that are essential to the cell migration and matrix invasion occurring during tumor invasion, angiogenesis and metastasis.

引用

页码：259 / 269

页数：11

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