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 γ2 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.

Keywords

LamininExtracellular matrixMMP2Matrix metalloproteinaseCell migrationCell biologyCleavage (geology)MotilityMetalloproteinaseChemistryProtein subunitCellBiologyBiochemistryDownregulation and upregulationGene

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Publication Info

Year
1997
Type
article
Volume
277
Issue
5323
Pages
225-228
Citations
1215
Access
Closed

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Cite This

Gianluigi Giannelli, Jutta Falk-Marzillier, O Schiraldi et al. (1997). Induction of Cell Migration by Matrix Metalloprotease-2 Cleavage of Laminin-5. Science , 277 (5323) , 225-228. https://doi.org/10.1126/science.277.5323.225

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DOI
10.1126/science.277.5323.225