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Protein kinase C activation by 12-0-tetradecanoylphorbol 13-acetate in CG-4 line oligodendrocytes stimulates turnover of choline and ethanolamine phospholipids by phospholipase D and induces rapid process contraction

Kobayashi, M., Kidd, D., Hutson, E., Grafton, J., McNulty, S. and Rumsby, M. (2001) Protein kinase C activation by 12-0-tetradecanoylphorbol 13-acetate in CG-4 line oligodendrocytes stimulates turnover of choline and ethanolamine phospholipids by phospholipase D and induces rapid process contraction. Journal Of Neurochemistry, 76 (2). pp. 361-371. ISSN 0022-3042

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Abstract

Treatment of [3H]-choline- or [14C]-ethanolamine-labelled undifferentiated bipolar and differentiated multipolar CG-4 line oligodendrocytes with 12–0-tetradecanoylphorbol 13-acetate (TPA) to activate protein kinase C stimulated the release of choline or ethanolamine metabolites to the medium over controls. Ro31–8220, a PKC inhibitor, reduced TPA-stimulated release of choline- and ethanolamine-metabolites to basal levels. TPA treatment of both bipolar and multipolar cells caused rapid contraction of processes leaving rounded up cells: this effect was blocked by Ro31–8220. After 12–15 h exposure to TPA, bipolar undifferentiated CG-4 line cells extended short processes again and the cells became multipolar. Nocodozole, an agent which disrupts microtubules and caused CG-4 line cells to round up, caused increased choline or ethanolamine-metabolite release to the medium over basal levels suggesting that some release during TPA-treatment might occur due to process fragmentation. However, the transphosphatidylation reaction confirmed that phospholipase D was active in these cells. Exposure of bipolar undifferentiated CG-4 line cells to TPA resulted in down-regulatation of PKC-α and PKC-βΙΙ which could not be detected by Western blotting after a few hours; PKC-ε was down-regulated much more slowly but PKCs δ, ζ and ι were not influenced by 48 h exposure of cells to TPA. Formation of phosphatidylethanol in the transphosphatidylation reaction was markedly reduced in TPA down-regulated cells indicating a role for PKCs α and βΙΙ in phospholipase D activation in CG-4 line oligodendrocytes.

Item Type: Article
Copyright, Publisher and Additional Information: Open access copy available from the journal web site.
Keywords: CG-4 line oligodendrocytes, protein kinase C subspecies alpha and beta(II), phospholipase D, choline and ethanolamine phospholipid hydolysis, transphosphatidylation, process contraction
Institution: The University of York
Academic Units: The University of York > Biology (York)
Depositing User: Open Access From Journal
Date Deposited: 22 Dec 2008 15:05
Last Modified: 22 Dec 2008 15:05
Published Version: http://dx.doi.org/10.1046/j.1471-4159.2001.00007.x
Status: Published
Publisher: Wiley-Blackwell
Refereed: Yes
Identification Number: 10.1046/j.1471-4159.2001.00007.x
URI: http://eprints.whiterose.ac.uk/id/eprint/5108

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