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SNARE Complex Proteins, Including the Cognate Pair VAMP‐2and Syntaxin‐4, Are Expressed in Cultured Oligodendrocytes
Author(s) -
Madison Dana L.,
Krueger Winfried H.,
Cheng David,
Trapp Bruce D.,
Pfeiffer S. E.
Publication year - 1999
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1999.0720988.x
Subject(s) - microbiology and biotechnology , synaptobrevin , snare complex , syntaxin , biology , synaptophysin , proteolipid protein 1 , membrane protein , synaptic vesicle , vesicle , chemistry , myelin , myelin basic protein , biochemistry , membrane , neuroscience , immunology , immunohistochemistry , central nervous system
: Myelin membrane synthesis in the CNS by oligodendrocytes (OLs) involves directed intracellular transport and targeting of copious amounts of specialized lipids and proteins over a relatively short time span. As in other plasma membrane‐directed fusion, this process is expected to use specific trafficking and vesicle fusion proteins characteristic of the SNARE model. We have investigated the developmental expression of SNARE proteins in highly enriched primary cultures of OLs at discrete stages of differentiation. VAMP‐2/synaptobrevin‐2, syntaxin‐2 and ‐4, nsec‐1/munc‐18‐1, Rab3a, synaptophysin, and synapsin were expressed. During differentiation, expression of the vesicular SNARE VAMP‐2, the small GTP‐binding protein Rab3a, and the target SNARE syntaxin‐4 were up‐regulated. VAMP‐2 and Rab3 proteins detected immunocytochemically in cultured OLs were localized within the developing process network ; in situ anti‐VAMP‐2 antibody stained the perikarya of rows of cells with the distribution and appearance of OLs. We discuss the potential involvement of SNARE complex proteins in a plasma membrane‐directed transport mechanism targeting nascent myelin vesicles to the forming myelin sheath.