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Blood, 15 May 2005, Vol. 105, No. 10, pp. 3956-3964. Prepublished online as a Blood First Edition Paper on January 21, 2005; DOI 10.1182/blood-2004-06-2382. This Article Full Text Full Text (PDF) Erratum (v107,p2586) All Versions of this Article: 2004-06-2382v1 105/10/3956    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Matías-Román, S. Articles by Arroyo, A. G. Search for Related Content PubMed PubMed Citation Articles by Matías-Román, S. Articles by Arroyo, A. G. Related Collections Immunobiology Cell Adhesion and Motility Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  IMMUNOBIOLOGY Membrane type 1–matrix metalloproteinase is involved in migration of human monocytes and is regulated through their interaction with fibronectin or endothelium Salomón Matías-Román, Beatriz G. Gálvez, Laura Genís, María Yáñez-Mó, Gonzalo de la Rosa, Paloma Sánchez-Mateos, Francisco Sánchez-Madrid, and Alicia G. Arroyo From the Centro Nacional de Investigaciones Cardiovasculares, Madrid, Spain; Departamento de Inmunología, Hospital Universitario de la Princesa, Madrid, Spain; and the Departamento de Inmunología, Hospital Universitario Gregorio Marañón, Madrid, Spain. Membrane type 1–matrix metalloproteinase (MT1-MMP) is involved in endothelial and tumor-cell migration, but its putative role in leukocyte migration has not been characterized yet. Here, we demonstrate that anti–MT1-MMP monoclonal antibody (mAb) impaired monocyte chemotactic protein-1 (MCP-1)–stimulated monocyte migration on fibronectin (FN), vascular cell adhesion molecule-1 (VCAM-1), and intercellular adhesion molecule-1 (ICAM-1). In addition, monocyte transmigration through tumor necrosis factor- (TNF-)–activated endothelium is also inhibited by anti–MT1-MMP mAb. Therefore, regulation of MT1-MMP in human peripheral blood monocytes was investigated. First, MT1-MMP clustering was observed at motility-associated membrane protrusions of MCP-1–stimulated monocytes migrating on FN, VCAM-1, or ICAM-1 and at the leading edge, together with profilin, of monocytes transmigrating through activated endothelial cells. In addition, up-regulation of MT1-MMP expression was induced in human monocytes upon attachment to FN in a manner dependent on 41 and 51 integrins. Binding of monocytes to TNF-–activated human endothelial cells as well as to VCAM-1 or ICAM-1 also resulted in an increase of MT1-MMP expression. These findings correlated with an enhancement of MT1-MMP fibrinolytic activity in monocytes bound to FN, VCAM-1, or ICAM-1. Our data show that MT1-MMP is required during human monocyte migration and endothelial transmigration and that MT1-MMP localization, expression, and activity are regulated in monocytes upon contact with FN or endothelial ligands, pointing to a key role of MT1-MMP in monocyte recruitment during inflammation. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. H. Cox, R. A. Dean, C. R. Roberts, and C. M. Overall Matrix Metalloproteinase Processing of CXCL11/I-TAC Results in Loss of Chemoattractant Activity and Altered Glycosaminoglycan Binding J. Biol. Chem., July 11, 2008; 283(28): 19389 - 19399. [Abstract] [Full Text] [PDF] M. Popovic, Y. 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