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This Article Full Text Full Text (PDF) 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 Miao, W.-M. Articles by Lawler, J. Search for Related Content PubMed PubMed Citation Articles by Miao, W.-M. Articles by Lawler, J. Related Collections Hemostasis, Thrombosis, and Vascular Biology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 March 2001, Vol. 97, No. 6, pp. 1689-1696 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY CD36 associates with CD9 and integrins on human blood platelets Wei-Min Miao, Eliza Vasile, William S. Lane, and Jack Lawler From the Department of Pathology, Beth Israel Deaconess Medical Center, and Harvard Medical School, Boston, MA; and Harvard Microchemistry Facility, Harvard University, Cambridge, MA. The membrane glycoprotein CD36 is involved in platelet aggregation, inhibition of angiogenesis, atherosclerosis, and sequestration of malaria-parasitized erythrocytes. In this study, immunoprecipitations with anti-CD36 antibodies were performed to identify proteins that associate with CD36 in the platelet membrane. Platelets were solubilized in 1% Triton X-100, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), Brij 96, or Brij 99, and the proteins that coprecipitated with CD36 were identified by peptide mass spectrometry and Western blotting. The tetraspanin protein CD9 and the integrins IIb3 and 61 specifically coprecipitated with CD36 from platelets that were solubilized in CHAPS and Brij 99 but not from platelets that were solubilized in Triton X-100. Only CD9 is coprecipitated with CD36 from platelets that were solubilized in Brij 96. Reciprocal immunoprecipitations with antibodies to CD9, 6, IIb, or 3 from Brij 99-solubilized platelets coprecipitated CD36. Coprecipitation of CD36, CD9, and 61 was also observed on platelets from a patient with Glanzmann thrombasthenia, indicating that IIb3 is not required for the other proteins to associate. Colocalization of 6 and CD36, of CD9 and CD36, and of 6 and CD9 was observed on intact platelets prior to solubilization, using double immunofluorescence microscopy. These data indicate that CD36 associates with CD9 and integrins on human blood platelets. These associated proteins may mediate or participate in some of the diverse biological functions of CD36. © 2001 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: R. F. Collins, N. Touret, H. Kuwata, N. N. Tandon, S. 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