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β IV tubulin is selectively expressed by oligodendrocytes in the central nervous system
Author(s) -
Terada Nobuo,
Kidd Grahame J.,
Kinter Mike,
Bjartmar Carl,
MoranJones Kim,
Trapp Bruce D.
Publication year - 2005
Publication title -
glia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.954
H-Index - 164
eISSN - 1098-1136
pISSN - 0894-1491
DOI - 10.1002/glia.20175
Subject(s) - biology , oligodendrocyte , tubulin , myelin , microbiology and biotechnology , myelin basic protein , cytoplasm , immunoprecipitation , transmembrane protein , cytoskeleton , microtubule , central nervous system , neuroscience , immunology , cell , biochemistry , receptor , antibody
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 ∼55‐kDa pI ∼5 by two‐dimensional (2D) electrophoresis, which was identified as β‐tubulin by mass spectrometry. Isotype‐specific antibodies for β IV tubulin selectively labeled oligodendrocytes. First detected in premyelinating oligodendrocytes, β IV tubulin was abundant in myelinating oligodendrocyte perinuclear cytoplasm and processes extending to and along developing myelin internodes. β IV tubulin‐positive MTs were diffusely distributed in oligodendrocyte perinuclear cytoplasm and not organized around the centrosome. β 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. © 2005 Wiley‐Liss, Inc.