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Blood, 15 October 2004, Vol. 104, No. 8, pp. 2549-2556. Prepublished online as a Blood First Edition Paper on June 24, 2004; DOI 10.1182/blood-2004-03-1108. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-03-1108v1 104/8/2549    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 Ma, Y.-Q. Articles by Geng, J.-G. Search for Related Content PubMed PubMed Citation Articles by Ma, Y.-Q. Articles by Geng, J.-G. Related Collections Immunobiology Phagocytes Cell Adhesion and Motility Signal Transduction Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  PHAGOCYTES P-selectin binding to P-selectin glycoprotein ligand-1 induces an intermediate state of M2 activation and acts cooperatively with extracellular stimuli to support maximal adhesion of human neutrophils Yan-Qing Ma, Edward F. Plow, and Jian-Guo Geng From the Department of Molecular Cardiology and the Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Cleveland Clinic Foundation, Cleveland, OH; and the Vascular Biology Center and the Division of Hematology, Oncology and Transplantation, University of Minnesota Medical School, Minneapolis. P-selectin glycoprotein ligand 1 (PSGL-1, CD162) and integrin M2 (Mac-1, CD11bCD18) are leukocyte adhesion molecules essential for innate immunity and inflammation. The interaction of PSGL-1 with P-selectin (CD62P) mediates tethering, rolling, and weak adhesion of leukocytes, during which they become sufficiently activated in situ by locally released or displayed cytokines and chemoattractants for integrin-mediated firm adhesion. However, communication between P-selectin and the integrin, whether P-selectin can trigger 2-integrin activation, remains controversial. We found that P-selectin immunoglobulin chimera and PSGL-1 monoclonal antibodies (mAbs) increased adhesion of human neutrophils to immobilized, but not soluble, fibrinogen. This intermediate state of neutrophil adhesion was defined by moderate clustering of integrin M2, no increase in CBRM1/5 (a mAb specific for the activation epitope on the M subunit) recognition, and no increase in surface expression of M2, whereas phorbol myristate acetate (PMA) induced extensive changes in these 3 parameters. Furthermore, platelet-activating factor or interleukin 8 acted in concert with P-selectin for further enhancing the activation of M2. We thus propose a model in which P-selectin induces an intermediate state of integrin activation and then cooperates with other extracellular stimuli to support maximal adhesion of human neutrophils. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: P-selectin/PSGL-1: full or foul integrin activation? János Polgár Blood 2004 104: 2212-2213. [Full Text] [PDF] This article has been cited by other articles: N. Maugeri, P. Rovere-Querini, V. Evangelista, C. Covino, A. Capobianco, M. T. S. Bertilaccio, A. Piccoli, L. Totani, D. Cianflone, A. Maseri, et al. Neutrophils phagocytose activated platelets in vivo: a phosphatidylserine, P-selectin, and {beta}2 integrin-dependent cell clearance program Blood, May 21, 2009; 113(21): 5254 - 5265. [Abstract] [Full Text] [PDF] Y.-D. Li, B.-Q. Ye, S.-X. 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