ARACHIDONIC-ACID INDUCES PHOSPHORYLATION OF AN 18 KDA PROTEIN IN ELECTRICALLY PERMEABILIZED RAT ISLETS OF LANGERHANS

被引:10
作者
BASUDEV, H
JONES, PM
PERSAUD, SJ
HOWELL, SL
机构
[1] Biomedical Sciences Division, King's College London, London, W8 7AH, Campden Hill Road, Kensington
关键词
ISLETS OF LANGERHANS; PROTEIN PHOSPHORYLATION; ARACHIDONIC ACID; PROTEIN KINASE-C;
D O I
10.1016/0014-5793(92)80405-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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 4-beta phorbol myristate acetate (4-beta PMA) did not result in P-32 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.
引用
收藏
页码:69 / 72
页数:4
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