• microtubule;
  • myelin;
  • microtubule organization;
  • oligodendrocyte development


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 βIV tubulin selectively labeled oligodendrocytes. First detected in premyelinating oligodendrocytes, βIV tubulin was abundant in myelinating oligodendrocyte perinuclear cytoplasm and processes extending to and along developing myelin internodes. βIV tubulin-positive MTs were diffusely distributed in oligodendrocyte perinuclear cytoplasm and not organized around the centrosome. βIV 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.