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A more recent version of this article appeared on January 1, 2003
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Submitted on May 13, 2002
Revised on August 29, 2002
Accepted on September 13, 2002
4 integrin-mediated leukocyte adhesion by transforming growth factor-ß1
1 Centro de Investigaciones Biológicas, Department of Immunology, Madrid, Spain
* Corresponding author. E-mail address: joaquint{at}cib.csic.es.
The 
4 integrins (4ß1 and 4ß7) are cell surface heterodimers expressed mostly on leukocytes that mediate cell-cell and cell-extracellular matrix adhesion. A characteristic feature of 4 integrins is that their adhesive activity can be subjected to rapid modulation during the process of cell migration. Here we show that transforming growth factor-ß1 (TGF-ß1) rapidly (0.5-5 min) and transiently upregulated 4 integrin-dependent adhesion of different human leukocyte cell lines and human peripheral blood lymphocytes (PBL) to their ligands VCAM-1 and CS-1/fibronectin. In addition, TGF-ß1 enhanced the 4 integrin-mediated adhesion of PBL to TNF--treated human umbilical vein endothelial cells, indicating the stimulation of 4ß1/VCAM-1 interaction. Although TGF-ß1 rapidly activated the small GTP-ase RhoA and the p38 MAP kinase, enhanced adhesion did not require activation of both signalling molecules. Instead, polymerization of actin cytoskeleton triggered by TGF-ß1 was necessary for 4 integrin-dependent upregulated adhesion, and elevation of intracellular cAMP opposed this upregulation. Moreover, TGF-ß1 further increased cell adhesion mediated by 4 integrins in response to the chemokine SDF-1. These data suggest that TGF-ß1 can potentially contribute to cell migration by dinamically regulating cell adhesion mediated by 4 integrins.
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