INDUCTION OF CELL-MIGRATION BY MATRIX METALLOPROTEASE-2 CLEAVAGE OF LAMININ-5

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