胶原酶
基质金属蛋白酶
细胞外基质
生物
明胶酶
成纤维细胞
细胞生物学
明胶酶A
金属蛋白酶
癌细胞
MMP1型
细胞外
细胞
体外
癌症
生物化学
基因表达
酶
基因
遗传学
作者
Farideh Sabeh,Ichiro Ota,Kenn Holmbeck,Henning Birkedal‐Hansen,Paul D. Soloway,Milagros Balbı́n,Carlos López-Otı́n,Steven D. Shapiro,Masaki Inada,Stephen M. Krane,Edward Allen,Duane Chung,Stephen J. Weiss
标识
DOI:10.1083/jcb.200408028
摘要
As cancer cells traverse collagen-rich extracellular matrix (ECM) barriers and intravasate, they adopt a fibroblast-like phenotype and engage undefined proteolytic cascades that mediate invasive activity. Herein, we find that fibroblasts and cancer cells express an indistinguishable pericellular collagenolytic activity that allows them to traverse the ECM. Using fibroblasts isolated from gene-targeted mice, a matrix metalloproteinase (MMP)–dependent activity is identified that drives invasion independently of plasminogen, the gelatinase A/TIMP-2 axis, gelatinase B, collagenase-3, collagenase-2, or stromelysin-1. In contrast, deleting or suppressing expression of the membrane-tethered MMP, MT1-MMP, in fibroblasts or tumor cells results in a loss of collagenolytic and invasive activity in vitro or in vivo. Thus, MT1-MMP serves as the major cell-associated proteinase necessary to confer normal or neoplastic cells with invasive activity.
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