Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5

被引：993

作者：

Giannelli, G

FalkMarzillier, J

Schiraldi, O

StetlerStevenson, WG

Quaranta, V

机构：

[1] SCRIPPS RES INST, DEPT CELL BIOL, LA JOLLA, CA 92037 USA

[2] UNIV BARI, INST MED CLIN 2, I-70124 BARI, ITALY

[3] NCI, PATHOL LAB, BETHESDA, MD 20892 USA

来源：

SCIENCE | 1997年 / 277卷 / 5323期

关键词：

D O I：

10.1126/science.277.5323.225

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Structural changes in the extracellular matrix are necessary for cell migration during tissue remodeling and tumor invasion. Specific cleavage of laminin-5 (Ln-5) by matrix metalloprotease-2 (MMP2) was shown to induce migration of breast epithelial cells. MMP2 cleaved the Ln-5 gamma 2 subunit at residue 587, exposing a putative cryptic promigratory site on Ln-5 that triggers cell motility. This altered form of Ln-5 is found in tumors and in tissues undergoing remodeling, but not in quiescent tissues. Cleavage of Ln-5 by MMP2 and the resulting activation of the Ln-5 cryptic site may provide new targets for modulation of tumor cell invasion and tissue remodeling.

引用

页码：225 / 228

页数：4

共 32 条

[1] IDENTIFICATION OF THE ARG-GLY-ASP SEQUENCE IN LAMININ-A CHAIN AS A LATENT CELL-BINDING SITE BEING EXPOSED IN FRAGMENT P1 [J].