Translocation of protein kinase C in rat islets of Langerhans Effects of a phorbol ester, carbachol and glucose

FEBS Letters

Sugden, David¹  Howell, Simon L.¹  Jones, Peter M.¹  Persaud, Shanta J.¹ 

[1] Biomedical Sciences Division, King's College London, Kensington, London W8 7AH, England

关键词: Protein kinase C;    Translocation;    Glucose;    Carbachol;    Phorbol ester;    (Islets of Langerhans);   

DOI  :  10.1016/0014-5793(89)80196-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In unstimulated rat islets (2 mM glucose), most of the ion-exchange purified protein kinase C (PKC) activity was associated with the cytosolic fraction. Both carbachol and phorbol myristate acetate caused a significant translocation of PKC activity from cytosolic to membrane fractions, but under the same conditions, glucose (20 mM) did not cause such a redistribution of PKC activity. PMA-induced translocation of PKC to the membrane fraction was also observed in electrically permeabilised islets, in which recovery of the enzyme activity was enhanced by buffering the intracellular Ca²⁺ concentration to 50 nM and supplying the permeabilised islets with protease inhibitors.

【 授权许可】

Unknown