Protein kinase C activates capacitative calcium entry in the insulin secreting cell line RINm5F

FEBS Letters

Bode, Hans-Peter²  Göke, Burkhard¹ 

[1] Laboratory of Molecular Endocrinology, Department of Internal Medicine, Philipps University, Marburg, Germany;Department of Pharmacology, Department of Internal Medicine, Philipps University, Marburg, Germany

关键词: Calcium entry;    Thapsigargin;    Protein kinase C;    Insulin-secreting cell;    RINm5F cell;    DMSO;    dimethyl sulfoxide;    DTPA;    diethylenetriamine-pentaacetic acid;    EDTA;    ethylenediamine tetraacetic acid;    EGTA;    [ethylenebis(oxyethylenenitrilo)]tetraacetic acid;    HEPES;    4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid;    TPA 12-O-tetrade-canoylphorbol 13-acetate;   

DOI  :  10.1016/0014-5793(94)80436-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

This study examines the calcium store-regulated (capacitative) calcium influx pathway in the endocrine pancreatic cell line RINm5F, utilizing thapsigargin. After preincubation of the cells with the phorbol ester TPA, thapsigargin induced a sustained elevation of cytosolic calcium as well as a sustained stimulation of manganese entry, the latter being used to assess calcium influx. Thapsigargin given alone provoked a smaller and only transient elevation of cytosolic calcium and stimulation of manganese entry. The protein kinase C inhibitor staurosporine antagonized the effect of the phorbol ester. Verapamil, nifedipine, or measures to hyperpolarize the cells exerted no inhibitory action against this effect, which excludes an involvement of voltage-dependent calcium channels. In conclusion, our data shows for the first time that protein kinase C stimulation activates the capacitative calcium influx pathway of endocrine pancreatic insulin-producing cells.

【 授权许可】

Unknown