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Prepublished online as a Blood First Edition Paper on July 24, 2003; DOI 10.1182/blood-2003-03-0871. This Article 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 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. Social Bookmarking                   What's this? Submitted March 21, 2003 Accepted July 18, 2003 Lipid raft-associated proteins are sorted in exosomes Aude de Gassart, Charles Geminard, Benoit Fevrier, Graca Raposo, and Michel Vidal* UMR 5539 CNRS, Universite Montpellier II, Montpellier, France UMR144 CNRS, Institut Curie, Paris, France * Corresponding author; email: mvidal{at}univ-montp2.fr. 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 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: (i) had a lower molecular weight compared to Lyn detected in cell-isolated detergent-resistant domains, (ii) was absent from the Triton X-100-insoluble fraction isolated from exosomes, and (iii) had lost its partitioning capacity in Triton X-114. Exosomal Lyn is likely cleaved by a caspase-3-like activity contained in secreted vesicles. Altogether 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. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: M. 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