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Protein kinase C activates capacitative calcium entry in the insulin secreting cell line RINm5F
Author(s) -
Bode Hans-Peter,
Göke Burkhard
Publication year - 1994
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(94)80436-2
Subject(s) - thapsigargin , staurosporine , calcium , protein kinase c , medicine , endocrinology , stimulation , wortmannin , verapamil , enteroendocrine cell , protein kinase a , chemistry , cytosol , voltage dependent calcium channel , microbiology and biotechnology , biology , kinase , signal transduction , biochemistry , endocrine system , protein kinase b , hormone , enzyme
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.