Abstract:
:Oligodendrocyte differentiation and myelination involve dramatic changes in cell signaling pathways, gene expression patterns, cell shape, and cytoskeletal organization. In a pilot study investigating CNS angiogenesis, oligodendrocytes were intensely labeled by antisera directed against the C-terminal of Tie-2, a 140-kDa transmembrane receptor for angiopoietin. Immunoprecipitation of rat brain proteins with Tie-2 C-terminal antisera, however, produced a single spot of approximately 55-kDa pI approximately 5 by two-dimensional (2D) electrophoresis, which was identified as beta-tubulin by mass spectrometry. Isotype-specific antibodies for beta(IV) tubulin selectively labeled oligodendrocytes. First detected in premyelinating oligodendrocytes, beta(IV) tubulin was abundant in myelinating oligodendrocyte perinuclear cytoplasm and processes extending to and along developing myelin internodes. Beta(IV) tubulin-positive MTs were diffusely distributed in oligodendrocyte perinuclear cytoplasm and not organized around the centrosome. Beta(IV) tubulin may play a role in establishing the oligodendrocyte MT network, which is essential for the transport of myelin proteins, lipids, and RNA during myelination.
journal_name
Gliajournal_title
Gliaauthors
Terada N,Kidd GJ,Kinter M,Bjartmar C,Moran-Jones K,Trapp BDdoi
10.1002/glia.20175subject
Has Abstractpub_date
2005-05-01 00:00:00pages
212-22issue
3eissn
0894-1491issn
1098-1136journal_volume
50pub_type
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