In Vitro Activation of Rat Brain Protein Kinase C by Polyenoic Very-Long-Chain Fatty Acids |
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| Authors: | Stephen J Hardy Antonio Ferrante Brenton S Robinson† David W Johnson† Alf Poulos† Katherine J Clark† rew W Murray† |
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| Institution: | Department of Immunology and University of Adelaide Department of Paediatrics, Women's and Children 's Hospital, North Adelaide, Australia;Department of Chemical Pathology, Women's and Children 's Hospital, North Adelaide, Australia;School of Biological Sciences, The Flinders University of South Australia, Bedford Park, South Australia, Australia |
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| Abstract: | Abstract: A variety of fatty acids including the cis -polyunsaturated very-long-chain fatty acids (VLCFA) (>22 carbon atoms) common in retina, spermatozoa, and brain were examined for their ability to activate protein kinase C (PKC) purified from rat brain. Arachidonic 20:4(n-6)], eicosapentaenoic 20:5(n-3)], and docosahexaenoic 22:6(n- 3)] acids as well as the VLCFA dotriacontatetraenoic 32:4(n-6)] and tetratriacontahexaenoic 34:6(n-3)] were equally capable of activating PKC in vitro with maximal activity being between 25 and 50 μ M. The phorbol ester 12- O -tetradecanoylphorbol 13-acetate further enhanced the in vitro activation of PKC when added to the protein kinase assay system with the fatty acids. The fully saturated arachidic acid (20:0) was inactive in both assay systems. The potential significance of the in vitro activation of PKC by the VLCFA is discussed. |
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| Keywords: | Protein kinase C Very-long-chain fatty acids Enzyme activation Brain Phorbol esters |
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