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Arachidonic acid induces phosphorylation of an 18 kDa protein in electrically permeabilised rat islets of Langerhans
Author(s) -
Basudev Harsha,
Jones Peter M.,
Persaud Shanta J.,
Howell Simon L.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80405-6
Subject(s) - protein kinase c , phosphorylation , arachidonic acid , phorbol , protein kinase a , chemistry , islet , biochemistry , stimulation , protein phosphorylation , microbiology and biotechnology , biology , endocrinology , enzyme , insulin
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 4β phorbol myristate acetate (4β PMA) did not result in 32 P 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 4β PMA. These results suggest that AA stimulates protein phosphorylation by a mechanism other than PKC activation.