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In Vitro Activation of Rat Brain Protein Kinase C by Polyenoic Very‐Long‐Chain Fatty Acids
Author(s) -
Hardy Stephen J.,
Ferrante Antonio,
Robinson Brenton S.,
Johnson David W.,
Poulos Alf,
Clark Katherine J.,
Murray Andrew W.
Publication year - 1994
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1994.62041546.x
Subject(s) - protein kinase c , docosahexaenoic acid , arachidic acid , in vitro , polyunsaturated fatty acid , arachidonic acid , biochemistry , eicosapentaenoic acid , protein kinase a , biology , fatty acid , kinase , chemistry , enzyme , palmitic acid
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.