Arachidonic acid induces phosphorylation of an 18 kDa protein in electrically permeabilised rat islets of Langerhans.
Arachidonic acid (AA) was shown to induce concentration-dependent, calcium-independent, in situ phosphorylation of a protein of approximate molecular weight 18 kDa in electrically permeabilised rat islets of Langerhans. This protein did not appear to be a substrate for protein kinase C (PKC) since stimulation of PKC by 4 beta phorbol myristate acetate (4 beta PMA) did not result in 32P incorporation into an 18 kDa protein, and since AA-induced phosphorylation was observed in islets in which PKC had been down-regulated by prolonged exposure of islets to 4 beta PMA. These results suggest that AA stimulates protein phosphorylation by a mechanism other than PKC activation.
Basudev
H
H
Biomedical Sciences Division, King's College London, Kensington, UK.
Jones
P M
PM
Persaud
S J
SJ
Howell
S L
SL
D000818:Animals; D016718:Arachidonic Acid / Q000502:physiology*; D001345:Autoradiography; D003720:Densitometry; D004560:Electricity; D004789:Enzyme Activation; D007515:Islets of Langerhans / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D011506:Proteins; D016718:Arachidonic Acid; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate