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A more recent version of this article appeared on July 1, 2005
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Submitted on December 3, 2004
Accepted on April 27, 2005
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*Department of Immunology, Centro de Investigaciones Biológicas, CSIC, 28006 Madrid, Spain; Department of Immunology and Oncology, Centro Nacional de Biotecnología, CSIC-Pfizer, 28049 Madrid, Spain; Centro de Investigación del Cáncer, CSIC, 37007 Salamanca, Spain
Monitoring Editor: Mark Ginsberg
The chemokine CXCL12 promotes T lymphocyte adhesion mediated by the integrin 
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1. CXCL12 activates the GTPase Rac, as well as Vav1, a guanine-nucleotide exchange factor for Rac, concomitant with upregulation of 41-dependent adhesion. Inhibition of CXCL12-promoted Rac and Vav1 activation by transfection of dominant negative Rac or Vav1 forms, or by transfection of their siRNA, remarkably impaired the increase in T lymphocyte attachment to 41 ligands in response to this chemokine. Importantly, inhibition of Vav1 expression by RNA interference resulted in a blockade of Rac activation in response to CXCL12. Adhesions in flow chambers and soluble binding assays using these transfectants indicated that initial ligand binding and adhesion strengthening mediated by 41 were dependent on Vav1 and Rac activation by CXCL12. Finally, CXCL12-promoted T-cell transendothelial migration involving 41-mediated adhesion was notably inhibited by expression of dominant negative Vav1 and Rac. These results indicate that activation of Vav1-Rac signaling pathway by CXCL12 represents an important inside-out event controlling efficient upregulation of 41-dependent T lymphocyte adhesion.
Present address: Theodor Kocher Institute, University of Bern, Freiestrasse 1, 3012 Bern, Switzerland.
Address correspondence to:
Joaquin Teixidó (joaquint{at}cib.csic.es)
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