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

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...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1997-07, Vol.277 (5323), p.225-228
Hauptverfasser:	Giannelli, Gianluigi, Falk-Marzillier, Jutta, Schiraldi, Oronzo, Stetler-Stevenson, William G., Quaranta, Vito
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Basement membrane Biological and medical sciences Breast - cytology Breast - metabolism Breast cancer Breasts Cancer cells Cell Adhesion Cell Adhesion Molecules - metabolism Cell Division Cell Line Cell migration Cell motility Cell Movement Cell physiology Cell Size Cells Cellular biology Collagenases - metabolism Epithelial Cells Epithelium - metabolism Extracellular Matrix - metabolism Female Fibrinolysin - metabolism Fundamental and applied biological sciences. Psychology Gelatinases - antagonists & inhibitors Gelatinases - metabolism Humans Kalinin Laminin Logical Thinking Matrix Metalloproteinase 2 Matrix Metalloproteinase 9 Membranes Metalloendopeptidases - antagonists & inhibitors Metalloendopeptidases - metabolism Metalloenzymes Mice Migration Molecular and cellular biology Motility and taxis Phenylalanine - analogs & derivatives Phenylalanine - pharmacology Physiological aspects Protease Inhibitors - pharmacology Rats Recombinant Fusion Proteins - metabolism Renovations Skin Neoplasms - metabolism Skin Neoplasms - pathology Stromal cells Thiophenes - pharmacology Tumors
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Beschreibung
Zusammenfassung:	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.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.277.5323.225