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Blood, 15 March 2004, Vol. 103, No. 6, pp. 2096-2104. Prepublished online as a Blood First Edition Paper on November 20, 2003; DOI 10.1182/blood-2003-08-2804. This Article Full Text Full Text (PDF) Supplemental Table All Versions of this Article: 2003-08-2804v1 103/6/2096    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 Coppinger, J. A. Articles by Maguire, P. B. Search for Related Content PubMed PubMed Citation Articles by Coppinger, J. A. Articles by Maguire, P. B. Related Collections Hemostasis, Thrombosis, and Vascular Biology Genomics Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions Judith A. Coppinger, Gerard Cagney, Sinead Toomey, Thomas Kislinger, Orina Belton, James P. McRedmond, Dolores J. Cahill, Andrew Emili, Desmond J. Fitzgerald, and Patricia B. Maguire From the Department of Clinical Pharmacology, Royal College of Surgeons in Ireland, Dublin; Banting and Best Department of Medical Research, University of Toronto, and the Department of Molecular and Medical Genetics, University of Toronto, Ontario, Canada. Proteins secreted by activated platelets can adhere to the vessel wall and promote the development of atherosclerosis and thrombosis. Despite this biologic significance, however, the complement of proteins comprising the platelet releasate is largely unknown. Using a proteomics approach, we have identified more than 300 proteins released by human platelets following thrombin activation. Many of the proteins identified were not previously attributed to platelets, including secretogranin III, a potential monocyte chemoattractant precursor; cyclophilin A, a vascular smooth muscle cell growth factor; calumenin, an inhibitor of the vitamin K epoxide reductase-warfarin interaction, as well as proteins of unknown function that map to expressed sequence tags. Secretogranin III, cyclophilin A, and calumenin were confirmed to localize in platelets and to be released upon activation. Furthermore, while absent in normal vasculature, they were identified in human atherosclerotic lesions. Therefore, these and other proteins released from platelets may contribute to atherosclerosis and to the thrombosis that complicates the disease. Moreover, as soluble extracellular proteins, they may prove suitable as novel therapeutic targets. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Propelling the platelet proteome Andrew S. Weyrich and Guy A. Zimmerman Blood 2004 103: 1979. [Full Text] [PDF] This article has been cited by other articles: S. Paco, E. Pozas, and F. Aguado Secretogranin III Is an Astrocyte Granin That Is Overexpressed in Reactive Glia Cereb Cortex, November 5, 2009; (2009) bhp202v1. [Abstract] [Full Text] [PDF] G. L. Hortin, D. Sviridov, and N. L. Anderson High-Abundance Polypeptides of the Human Plasma Proteome Comprising the Top 4 Logs of Polypeptide Abundance Clin. Chem., October 1, 2008; 54(10): 1608 - 1616. [Abstract] [Full Text] [PDF] J.-M. Howes, J. N Keen, J. B. Findlay, and A. 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