Arachidonic acid induces phosphorylation of an 18 kDa protein in electrically permeabilised rat islets of Langerhans

FEBS Letters

Howell, Simon L.¹  Jones, Peter M.¹  Basudev, Harsha¹  Persaud, Shanta J.¹ 

[1] Biomedical Sciences Division, King's College London, Campden Hill Road, Kensington, London, W8 7AH, UK

关键词: Islets of Langerhans;    Protein phosphorylation;    Arachidonic acid;    Protein kinase C;   

DOI  :  10.1016/0014-5793(92)80405-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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 4β PMA. These results suggest that AA stimulates protein phosphorylation by a mechanism other than PKC activation.

【 授权许可】

Unknown