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Blood, 15 September 2008, Vol. 112, No. 6, pp. 2327-2335. Prepublished online as a Blood First Edition Paper on May 28, 2008; DOI 10.1182/blood-2007-12-127183. This Article Full Text Full Text (PDF) All Versions of this Article: blood-2007-12-127183v1 112/6/2327    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 Pluskota, E. Articles by Plow, E. F. Search for Related Content PubMed PubMed Citation Articles by Pluskota, E. Articles by Plow, E. F. Related Collections Hemostasis, Thrombosis, and Vascular Biology Phagocytes Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Expression, activation, and function of integrin Mβ2 (Mac-1) on neutrophil-derived microparticles Elzbieta Pluskota1, Neil M. Woody1, Dorota Szpak1, Christie M. Ballantyne2, Dmitry A. Soloviev1, Daniel I. Simon3, and Edward F. Plow1 1 Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, Cleveland Clinic, OH; 2 Baylor College of Medicine and Methodist DeBakey Heart Center, Houston, TX; and 3 University Hospitals Case Medical Center, Case Western Reserve University School of Medicine, Cleveland, OH Leukocyte-derived microparticles (MPs) are markers of cardiovascular diseases and contribute to pathogenesis by their interaction with various cell types. The presence and activation state of a multifunctional leukocyte receptor, integrin Mβ2 (CD11b/18), on MPs derived from human neutrophils (PMNs) were examined. Mβ2 expression was significantly enhanced on MPs derived from stimulated compared with resting PMNs. Furthermore, Mβ2 on MPs from stimulated but not resting PMNs was in an activated conformation because it was capable of binding activation-specific monoclonal antibodies (CBRM1/5 and mAb24) and soluble fibrinogen. MPs expressing active Mβ2 interacted with and were potent activators of resting platelets as assessed by induction of P-selectin expression and activation of IIbβ3. With the use of function-blocking antibodies and MPs obtained from –/–-deficient mice, we found that engagement of GPIb on platelets by Mβ2 on MPs plays a pivotal role in MP binding. Platelet activation by MPs occurs by a pathway dependent on Akt phosphorylation. PSGL-1/P-selectin interaction also is involved in the conjugation of MPs to platelets, and the combination of blocking reagents to both Mβ2/GPIb and to PSGL-1/P-selectin completely abrogates MP-induced platelet activation. Thus, cooperation of these 2 receptor/counterreceptor systems regulates the prothrombotic properties of PMN-derived MPs. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Microparticles facilitate neutrophil/platelet crosstalk Robert K. Andrews and Michael C. Berndt Blood 2008 112: 2174-2175. [Full Text] [PDF] This article has been cited by other articles: C. T. Lefort, Y.-M. Hyun, J. B. Schultz, F.-Y. Law, R. E. Waugh, P. A. Knauf, and M. Kim Outside-In Signal Transmission by Conformational Changes in Integrin Mac-1 J. Immunol., November 15, 2009; 183(10): 6460 - 6468. [Abstract] [Full Text] [PDF] J. Hirahashi, K. Hishikawa, S. Kaname, N. Tsuboi, Y. Wang, D. I. Simon, G. Stavrakis, T. Shimosawa, L. Xiao, Y. Nagahama, et al. Mac-1 (CD11b/CD18) Links Inflammation and Thrombosis After Glomerular Injury Circulation, September 29, 2009; 120(13): 1255 - 1265. [Abstract] [Full Text] [PDF]

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