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Published 11 November 2002. doi:10.1083/jcb.200205026
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© The Rockefeller University Press, 0021-9525/2002/11/509 $5.00
The Journal of Cell Biology, Volume 159, Number 3, 509-521

Article

ECM regulates MT1-MMP localization with ß1 or {alpha}vß3 integrins at distinct cell compartments modulating its internalization and activity on human endothelial cells



Beatriz G. Gálvez, Salomón Matías-Román, María Yáñez-Mó, Francisco Sánchez-Madrid and Alicia G. Arroyo

Departamento de Inmunología, Hospital de la Princesa, 28006 Madrid, Spain

Address correspondence to Alicia G. Arroyo, Departamento de Inmunología, Hospital de la Princesa, C/Diego de León, 62, 28006 Madrid, Spain. Tel.: 34-91-520-2334. Fax: 34-91-520-2374. E-mail: agarciaa{at}hlpr.insalud.es

Regulation of membrane-type 1 matrix metalloproteinase (MT1-MMP) by different extracellular matrices (ECMs) on human endothelial cells (ECs) has been investigated. First, MT1-MMP is found at the intercellular contacts of confluent ECs grown on ß1 integrin–dependent matrix such as type 1 collagen (COL I), fibronectin (FN), or fibrinogen (FG), but not on gelatin (GEL) or vitronectin (VN). The novel localization of MT1-MMP at cell–cell contacts is assessed by confocal videomicroscopy of MT1-MMP-GFP–transfected ECs. Moreover, MT1-MMP colocalizes with ß1 integrins at the intercellular contacts, whereas it is preferentially found with {alpha}vß3 integrin at motility-associated structures on migrating ECs. In addition, clustered integrins recruit MT1-MMP and neutralizing anti-ß1 or anti-{alpha}v integrin mAb displace MT1-MMP from its specific sites, pointing to a biochemical association that is finally demonstrated by coimmunoprecipitation assays. On the other hand, COL I, FN, or FG up-regulate cell surface MT1-MMP on confluent ECs by an impairment of its internalization, whereas expression and internalization are not modified on GEL or VN. In addition, MT1-MMP activity is diminished in confluent ECs on COL I, FN, or FG. Finally, MT1-MMP participates and cooperates with ß1 and {alpha}vß3 integrins in the migration of ECs on different ECM. These data show a novel mechanism by which ECM regulates MT1-MMP association with ß1 or {alpha}vß3 integrins at distinct cellular compartments, thus modulating its internalization, activity, and function on human ECs.

Key Words: MMP; adhesion; endocytosis; angiogenesis; extracellular matrix


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