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

Giannelli G, Falk-Marzillier J, Schiraldi O, Stetler-Stevenson WG, Quaranta V
Science. 1997 277 (5323): 225-8

PMID: 9211848 · DOI:10.1126/science.277.5323.225

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.

MeSH Terms (26)

Animals Breast Cell Adhesion Cell Adhesion Molecules Cell Division Cell Line Cell Movement Cell Size Collagenases Epithelial Cells Epithelium Extracellular Matrix Female Fibrinolysin Gelatinases Humans Matrix Metalloproteinase 2 Matrix Metalloproteinase 9 Metalloendopeptidases Mice Phenylalanine Protease Inhibitors Rats Recombinant Fusion Proteins Skin Neoplasms Thiophenes

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