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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 (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 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 Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted December 4, 2007 Accepted May 2, 2008 Expression, activation and function of integrin M2 (Mac-1) on neutrophil-derived microparticles Elzbieta Pluskota, Neil M. Woody, Dorota Szpak, Christie M. Ballantyne, Dmitry A. Soloviev, Daniel I. Simon, and Edward F. Plow* Department of Molecular Cardiology/Lerner Research Institute, Cleveland Clinic, Cleveland, OH, United States Baylor College of Medicine, Methodist DeBakey Heart Center, Houston, TX, United States Cardiovascular Medicine, University Hospitals of Cleveland, Cleveland, OH, United States * Corresponding author; email: plowe{at}ccf.org. Leukocyte-derived microparticles (MPs) are markers of cardiovascular diseases and contribute to pathogenesis via their interaction with various cell types. The presence and activation state of a multifunctional leukocyte receptor, integrin M2 (CD11b/18), on MPs derived from human neutrophils (PMN) was examined. M2 expression was significantly enhanced on MPs derived from stimulated as compared to resting PMN. Furthermore, M2 on MPs from stimulated but not resting PMNs was in an activated conformation since it was capable of binding activation-specific monoclonal antibodies (CBRM1/5 and mAb24) and soluble fibrinogen. MPs expressing active M2 interacted with and were potent activators of resting platelets as assessed by induction of P-selectin expression and activation of IIb3. Utilizing function blocking antibodies and MPs obtained from M-/- deficient mice, we found that engagement of GPIb on platelets by M2 on MPs plays a pivotal role in MP binding. Platelet activation by MPs occurs via a pathway dependent of 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 M2/GPIb and to PSGL-1/P-selectin completely abrogates MP-induced platelet activation. Thus, cooperation of these two receptor:counter-receptor systems regulates the pro-thrombotic 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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