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: 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 [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. (C) 2005 Wiley-Liss, Inc.

Copyright (C) 2005 John Wiley & Sons, Inc.