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J Biol Chem, Vol. 273, Issue 32, 20121-20127, August 7, 1998
From the Association of major histocompatibility complex
(MHC) class II molecules with peptides occurs in a series of endocytic
vacuoles, termed MHC class II-enriched compartments (MIICs).
Morphological criteria have defined several types of MIICs, including
multivesicular MIICs, which are composed of 50-60-nm vesicles
surrounded by a limiting membrane. Multivesicular MIICs can fuse with
the plasma membrane, thereby releasing their internal vesicles into the
extracellular space. The externalized vesicles, termed exosomes, carry
MHC class II and can stimulate T-cells in vitro. In this
study, we show that exosomes are enriched in the co-stimulatory
molecule CD86 and in several tetraspan proteins, including CD37, CD53,
CD63, CD81, and CD82. Interestingly, subcellular localization of these molecules revealed that they were concentrated on the internal membranes of multivesicular MIICs. In contrast to the tetraspans, other
membrane proteins of MIICs, such as HLA-DM, Lamp-1, and Lamp-2, were
mainly localized to the limiting membrane and were hardly detectable on
the internal membranes of MIICs nor on exosomes. Because internal
vesicles of multivesicular MIICs are thought to originate from inward
budding of the limiting membrane, the differential distribution of
membrane proteins on the internal and limiting membranes of MIICs has
to be driven by active protein sorting.
Selective Enrichment of Tetraspan Proteins on the Internal
Vesicles of Multivesicular Endosomes and on Exosomes Secreted by
Human B-lymphocytes
,,,,
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Department of Cell Biology, Utrecht
University School of Medicine, AZU, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands and Shionogi Institute for
Medical Science, 2-5-1 Mishima, Settsu-shi, Osaka 566, Japan
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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