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. 1997 Jul 11;277(5323):225-8.
doi: 10.1126/science.277.5323.225.

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

G Giannelli  1 , J Falk-Marzillier, O Schiraldi, W G Stetler-Stevenson, V Quaranta
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Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5

G Giannelli et al. Science. .

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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