Induction of Cell Migration by Matrix Metalloprotease-2 Cleavage of Laminin-5

doi:10.1126/science.277.5323.225

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Science 11 July 1997:
Vol. 277. no. 5323, pp. 225 - 228
DOI: 10.1126/science.277.5323.225

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Induction of Cell Migration by Matrix Metalloprotease-2 Cleavage of Laminin-5

Gianluigi Giannelli, Jutta Falk-Marzillier, Oronzo Schiraldi, William G. Stetler-Stevenson, Vito Quaranta ^*

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 $gamma$ 2 subunit at residue 587, exposing a putativecryptic promigratory site on Ln-5 that triggers cell motility.This altered form of Ln-5 is found in tumors and in tissues undergoingremodeling, but not in quiescent tissues. Cleavage of Ln-5 byMMP2 and the resulting activation of the Ln-5 cryptic site mayprovide new targets for modulation of tumor cell invasion andtissue remodeling.

G. Giannelli, Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA, and Institute of Clinica Medica II, Università degli Studi Bari, 70124 Bari, Italy.
J. Falk-Marzillier and V. Quaranta, Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.
O. Schiraldi, Institute of Clinica Medica II, Università degli Studi Bari, 70124 Bari, Italy.
W. G. Stetler-Stevenson, Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
^* To whom correspondence should be addressed. E-mail: quaranta{at}scripps.edu