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Blood, 15 December 2003, Vol. 102, No. 13, pp. 4336-4344. Prepublished online as a Blood First Edition Paper on July 24, 2003; DOI 10.1182/blood-2003-03-0871. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-03-0871v1 102/13/4336    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 de Gassart, A. Articles by Vidal, M. Search for Related Content PubMed PubMed Citation Articles by de Gassart, A. Articles by Vidal, M. Related Collections Hematopoiesis and Stem Cells Immunobiology Apoptosis Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMATOPOIESIS Lipid raft-associated protein sorting in exosomes Aude de Gassart, Charles Géminard, Benoit Février, Graça Raposo, and Michel Vidal From the Unité Mixte de Recherches (UMR) Centre National de la Recherche Scientifique (CNRS) 5539, Université Montpellier II, Montpellier, France; and the UMR CNRS 144, Institut Curie, Paris, France. Exosomes are small membrane vesicles secreted by cells upon fusion of multivesicular endosomes with the cell surface. The mechanisms underlying the specific sorting of proteins in exosomal membranes are far from being unraveled. We demonstrate here, using different cells, that some molecules are released in the extracellular medium via their association with lipid raft domains of the exosomal membrane. Various typical raft-associated molecules could be detected by immunoblot in exosomes and Triton X-100-insoluble fractions isolated from exosomes of different origins. Partial localization of major histocompatibility complex (MHC) class II molecules with detergent-resistant fractions isolated from Daudi-secreted exosomes was demonstrated by immunoblot and confirmed by electron microscopy colocalization of MHC class II molecules and ganglioside GM1. Moreover, we found that exosome-associated Lyn (1) had a lower molecular weight compared with Lyn detected in cell-isolated detergent-resistant domains, (2) was absent from the Triton X-100-insoluble fraction isolated from exosomes, and (3) had lost its partitioning capacity in Triton X-114. Exosomal Lyn is probably cleaved by a caspase-3-like activity contained in secreted vesicles. All together, the data highlight the presence of lipid microdomains in exosomal membranes and suggest their participation in vesicle formation and structure, as well as the direct implication of exosomes in regulatory mechanisms. (Blood. 2003;102:4336-4344) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. Clayton, J. P. Mitchell, J. Court, S. Linnane, M. D. Mason, and Z. Tabi Human Tumor-Derived Exosomes Down-Modulate NKG2D Expression J. Immunol., June 1, 2008; 180(11): 7249 - 7258. [Abstract] [Full Text] [PDF] R. A. Sharples, L. J. Vella, R. M. Nisbet, R. Naylor, K. Perez, K. J. Barnham, C. L. Masters, and A. F. Hill Inhibition of {gamma}-secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes FASEB J, May 1, 2008; 22(5): 1469 - 1478. [Abstract] [Full Text] [PDF] K. Trajkovic, C. Hsu, S. Chiantia, L. Rajendran, D. Wenzel, F. Wieland, P. 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