In Vitro Activation of Rat Brain Protein Kinase C by Polyenoic Very-Long-Chain Fatty Acids
| Autor: | Stephen J. Hardy, David W. Johnson, Alf Poulos, B S Robinson, Antonio Ferrante, Katherine J. Clark, Andrew W. Murray |
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| Rok vydání: | 2008 |
| Předmět: |
Male
Docosahexaenoic Acids Biology Biochemistry Cellular and Molecular Neuroscience chemistry.chemical_compound Animals Humans Protein kinase A Protein Kinase C Protein kinase C chemistry.chemical_classification Arachidonic Acid Fatty Acids Brain Eicosapentaenoic acid In vitro Rats Enzyme Activation Enzyme Eicosapentaenoic Acid chemistry Docosahexaenoic acid Tetradecanoylphorbol Acetate Fatty Acids Unsaturated Arachidonic acid |
| Zdroj: | Journal of Neurochemistry. 62:1546-1551 |
| ISSN: | 0022-3042 |
| DOI: | 10.1046/j.1471-4159.1994.62041546.x |
| Popis: | 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 microM. 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. |
| Databáze: | OpenAIRE |
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