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Blood, 1 November 2004, Vol. 104, No. 9, pp. 2818-2824. Prepublished online as a Blood First Edition Paper on July 8, 2004; DOI 10.1182/blood-2003-12-4402. This Article Full Text (PDF) All Versions of this Article: 2003-12-4402v1 104/9/2818    most recent Alert me when this article is cited Alert me if a correction is posted 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 Hyduk, S. J Articles by Cybulsky, M. I Search for Related Content PubMed PubMed Citation Articles by Hyduk, S. J Articles by Cybulsky, M. I Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted December 29, 2003 Accepted June 10, 2004 Paxillin selectively associates with constitutive and chemoattractant-induced high affinity 41 integrins: implications for integrin signaling Sharon J Hyduk*, Jiwon Oh, Haiyan Xiao, Mian Chen, and Myron I Cybulsky Toronto General Research Institute and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada * Corresponding author; email: sharon.hyduk{at}utoronto.ca. Leukocyte 41 integrins regulate hematopoietic and lymphoid development, as well as the emigration of circulating cells to sites of inflammation. Because VCAM-1 binding to high affinity 41 is stable, these integrins can be detected and selectively precipitated from cell lysates using VCAM-1/Fc. With this approach, high affinity 41 integrin expression was demonstrated on lymphocytes in the bone marrow, thymus, spleen, and the peritoneal cavity of normal mice, but not in peripheral lymph nodes. Immature lymphocytes preferentially expressed high affinity 41 in the bone marrow and thymus. Paxillin is a cytoplasmic adaptor molecule that can bind to the 4 tail and initiate signaling. Paxillin was associated selectively with high affinity integrins that were isolated from human Jurkat T cells or from murine tissues, and blotting with a phospho-specific antibody demonstrated that serine-988 in the 4 cytoplasmic tail was dephosphorylated in high, but not low, affinity integrins. A rapid and transient 41 affinity up-regulation in formyl peptide receptor-transfected U937 cells stimulated with fMLP correlated temporally with induced paxillin binding to 4 integrins. These data suggest that ligand binding to high affinity 41 integrins may initiate outside-in signaling cascades through paxillin that regulate leukocyte maturation and emigration. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: E. Manevich, V. Grabovsky, S. W. Feigelson, and R. Alon Talin 1 and Paxillin Facilitate Distinct Steps in Rapid VLA-4-mediated Adhesion Strengthening to Vascular Cell Adhesion Molecule 1 J. Biol. Chem., August 31, 2007; 282(35): 25338 - 25348. [Abstract] [Full Text] [PDF]

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