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Related Collections Hemostasis, Thrombosis, and Vascular Biology Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 September 2002, Vol. 100, No. 5, pp. 1707-1714 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY The small proteoglycan decorin supports adhesion and activation of human platelets Gianni Guidetti, Alessandra Bertoni, Manuela Viola, Enrica Tira, Cesare Balduini, and Mauro Torti From the Department of Biochemistry, University of Pavia, Italy. Decorin is a small leucine-rich proteoglycan able to interact with several molecules of the subendothelial matrix, such as collagen and fibronectin. In this work, we investigated the ability of purified decorin to support adhesion of human platelets. We found that gel-filtered platelets were actually able to interact with immobilized decorin. Platelet adhesion to decorin was time dependent, required the presence of Mg2+ ions, and was totally mediated by the protein core of the proteoglycan. Platelet stimulation with either adenosine diphosphate (ADP) or a thrombin receptor-activating peptide significantly increased interaction of these cells with the proteoglycan. Upon adhesion to immobilized decorin a number of platelet proteins were found to become tyrosine-phosphorylated. By immunoprecipitation experiments with specific antibodies, the tyrosine phosphorylation of the tyrosine kinase Syk and the phospholipase C2 (PLC2) isozyme was demonstrated in decorin-adherent platelets. Interaction of platelets with decorin was selectively prevented by 2 different antibodies against membrane integrin 21, but not by a number of antibodies against other membrane receptors. In addition, integrin 21, purified from platelet membranes, was able to specifically interact with immobilized decorin. Finally, purified decorin bound to Sepharose beads could precipitate integrin 21 from a platelet membrane glycoprotein preparation. Therefore, these results demonstrate that human platelets can bind to immobilized decorin through integrin 21, and that this interaction results in the tyrosine phosphorylation of intracellular proteins. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. Goldoni, D. G. Seidler, J. Heath, M. Fassan, R. Baffa, M. L. Thakur, R. T. Owens, D. J. McQuillan, and R. V. Iozzo An Antimetastatic Role for Decorin in Breast Cancer Am. J. Pathol., September 1, 2008; 173(3): 844 - 855. [Abstract] [Full Text] [PDF] L. R. Fiedler, E. Schonherr, R. Waddington, S. Niland, D. G. Seidler, D. Aeschlimann, and J. A. 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	Copyright © 2002 by American Society of Hematology         Online ISSN: 1528-0020