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J. Biol. Chem., Vol. 278, Issue 13, 10963-10972, March 28, 2003
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From the Exosomes are 60-100-nm membrane vesicles
that are secreted into the extracellular milieu as a consequence of
multivesicular body fusion with the plasma membrane. Here we determined
the protein and lipid compositions of highly purified human B
cell-derived exosomes. Mass spectrometric analysis indicated the
abundant presence of major histocompatibility complex (MHC)
class I and class II, heat shock cognate 70, heat shock protein
90, integrin
Proteomic and Biochemical Analyses of Human B Cell-derived
Exosomes
POTENTIAL IMPLICATIONS FOR THEIR FUNCTION AND MULTIVESICULAR
BODY FORMATION*
,,,,,, and¶
Department of Cell Biology, Utrecht
University Medical Centre and Institute of Biomembranes, Room
G02.525, Heidelberglaan 100, 3585 CX Utrecht, The Netherlands and
§ Kekule-Institut fuer Organische Chemie und Biochemie
der Universitaet Bonn, Gerhard-Domagk-Strasse 1, D-53121 Bonn,
Germany
4, CD45, moesin, tubulin ( and 
), actin,
Gi2, and a multitude of other proteins. An 4-integrin may direct B cell-derived exosomes to follicular dendritic cells, which were described previously as potential target cells. Clathrin, heat shock cognate 70, and heat shock
protein 90 may be involved in protein sorting at multivesicular bodies.
Exosomes were also enriched in cholesterol, sphingomyelin, and
ganglioside GM3, lipids that are typically enriched in
detergent-resistant membranes. Most exosome-associated proteins,
including MHC class II and tetraspanins, were insoluble in
3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid
(CHAPS)-containing buffers. Multivesicular body-linked MHC class II was
also resistant to CHAPS whereas plasma membrane-associated MHC class II
was solubilized readily. Together, these data suggest that recruitment
of membrane proteins from the limiting membranes into the internal
vesicles of multivesicular bodies may involve their incorporation into
tetraspanin-containing detergent-resistant membrane domains.
*
This work was supported by the European Union
(QLRT-2001-00093) and by the Deutsche Forschungsgemeinschaft,
Sonderforschungsbereich 284.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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