Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5
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Updated: Nov 1, 2026

Concentric Gel System to Study the Biophysical Role of Matrix Microenvironment on 3D Cell Migration
Published on: April 3, 2015
G Giannelli1, J Falk-Marzillier, O Schiraldi
1Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.
Abstract:
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 gamma2 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.
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