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Blood, 15 December 2004, Vol. 104, No. 13, pp. 4046-4053.
Prepublished online as a Blood First Edition Paper on August 12, 2004; DOI 10.1182/blood-2004-05-1822.
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Submitted May 14, 2004
Accepted July 26, 2004
Ligation of lymphocyte function-associated antigen-1 on monocytes decreases very late antigen-4-mediated adhesion through a reactive oxygen species dependent pathway
Kuo-Pin Chuang, Ya-Fang Huang, Yi-Ling Hsu, Hsiao-Sheng Liu, Hong-Chen Chen, and Chi-Chang Shieh*
Institute of Basic Medicine, National Cheng-Kung University Medical College, Tainan, Taiwan
Institute of Microbiology and Immunology, National Cheng-Kung University Medical College, Tainan, Taiwan
Institute of Biomedical Sciences, National Chung Hsing University, Taichung, Taiwan
Institute of Basic Medicine, National Cheng-Kung University Medical College, Tainan, Taiwan; Institute of Microbiology and Immunology, National Cheng-Kung University Medical College, Tainan, Taiwan; Department of Pediatrics, National Cheng-Kung University Medical College, Tainan, Taiwan
* Corresponding author; email: cshieh{at}mail.ncku.edu.tw.
Monocyte-endothelial adhesion plays an important role in monocyte trafficking and hence is important for immune responses and pathogenesis of inflammatory diseases including atherosclerosis. The cross-talk between different integrins on monocytes may be crucial for a coordinated regulation of the cellular adhesion during the complex process of transendothelial migration. By using monoclonal antibodies and recombinant intercellular adhesion molecule (ICAM)-1 to engage lymphocyte function associated antigen -1 (LFA-1) on monocytic cells, we found that the cellular adhesion to VCAM-1 mediated by vary late antigen-4 (VLA-4) was suppressed after this treatment and the suppression was dependent on the presence of reactive oxygen species (ROS). Inhibition of reactive oxygen species (ROS) production through the use of inhibitor of the NADPH oxidase, but not inhibitors of mitochondrial electron transport chain or xanthine oxidase, revealed that this suppression on VLA-4 mediated cellular binding was mediated by ROS produced by phagocyte NADPH oxidase. Activation of PI3K and Akt appears to mediate this NADPH oxidase activation through p47phox phosphorylation and Rac-1 activation. Our results provide a novel pathway in which ROS play a critical role in integrin cross-talk in monocytes. This signaling pathway may be important for cellular transition from firm arrest to diapedesis during monocyte trafficking.
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