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Blood, 15 March 2004, Vol. 103, No. 6, pp. 2088-2095. Prepublished online as a Blood First Edition Paper on November 26, 2003; DOI 10.1182/blood-2003-07-2392. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-07-2392v1 103/6/2088    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 García, A. Articles by Zitzmann, N. Search for Related Content PubMed PubMed Citation Articles by García, A. Articles by Zitzmann, N. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Signal Transduction Genomics Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Differential proteome analysis of TRAP-activated platelets: involvement of DOK-2 and phosphorylation of RGS proteins Angel García, Sripadi Prabhakar, Sascha Hughan, Tom W. Anderson, Chris J. Brock, Andrew C. Pearce, Raymond A. Dwek, Steve P. Watson, Holger F. Hebestreit, and Nicole Zitzmann From the Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, United Kingdom; Department of Pharmacology, University of Oxford, Oxford, United Kingdom; Division of Medical Sciences, The Medical School, University of Birmingham, Edgbaston, Birmingham, United Kingdom. We have applied a proteomics approach to analyze signaling cascades in human platelets stimulated by thrombin receptor activating peptide (TRAP). By analyzing basal and TRAP-activated platelets using 2-dimensional gel electrophoresis (2-DE), we detected 62 differentially regulated protein features. From these, 41 could be identified by liquid chromatography–coupled tandem mass spectrometry (LC-MS/MS) and were found to derive from 31 different genes, 8 of which had not previously been reported in platelets, including the adapter downstream of tyrosine kinase 2 (Dok-2). Further studies revealed that the change in mobility of Dok-2 was brought about by tyrosine phosphorylation. Dok-2 tyrosine phosphorylation was also found to be involved in collagen receptor, glycoprotein VI (GPVI), signaling as well as in outside-in signaling through the major platelet integrin, IIb3. These studies also provided the first demonstration of posttranslational modification of 2 regulator of G protein signaling (RGS) proteins, RGS10 and 18. Phosphorylation of RGS18 was mapped to Ser49 by MS/MS analysis. This study provides a new approach for the identification of novel signaling molecules in activated platelets, providing new insights into the mechanisms of platelet activation and building the basis for the development of therapeutic agents for thrombotic diseases. 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: P. Luik, C. Chew, J. Aittoniemi, J. Chang, P. Wentworth Jr, R. A. Dwek, P. C. Biggin, C. Venien-Bryan, and N. 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