Regulation of ATP-sensitive K sup + channels in insulinoma cells: Activation by somatostatin and protein kinase C and the role of cAMP
- Centre de Biochimie du Centre National de la Recherche Scientifique, Nice (France)
The actions of somatostatin and of the phorbol ester 4{beta}-phorbol 12-myristate 13-acetate (PMA) were studied in rat insulinoma (RINm5F) cells by electrophysiological and {sup 86}Rb{sup +} flux techniques. Both PMA and somatostatin hyperpolarize insulinoma cells by activating ATP-sensitive K{sup +} channels. The presence of intracellular GTP is required for the somatostatin effects. PMA- and somatostatin-induced hyperpolarization and channel activity are inhibited by the sulfonylurea glibenclamide. Glibenclamide-sensitive {sup 86}Rb{sup +} efflux from insulinoma cells is stimulated by somatostatin in a dose-dependent manner (half maximal effect at 0.7 nM) and abolished by pertussis toxin pretreatment. Mutual roles of a GTP-binding protein, of protein kinase C, and of cAMP in the regulation of ATP-sensitive K{sup +} channels are discussed.
- OSTI ID:
- 5300376
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (USA), Vol. 86:8; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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MEMBRANE TRANSPORT
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PHORBOL ESTERS
BIOLOGICAL EFFECTS
RUBIDIUM 86
UPTAKE
SOMATOSTATIN
AMP
ATP
PHOSPHOTRANSFERASES
POTASSIUM COMPOUNDS
RATS
TUMOR CELLS
ALKALI METAL COMPOUNDS
ALKALI METAL ISOTOPES
ANIMAL CELLS
ANIMALS
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BETA-MINUS DECAY RADIOISOTOPES
CARCINOGENS
DAYS LIVING RADIOISOTOPES
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ISOMERIC TRANSITION ISOTOPES
ISOTOPES
MAMMALS
MINUTES LIVING RADIOISOTOPES
NUCLEI
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PHOSPHORUS-GROUP TRANSFERASES
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550201* - Biochemistry- Tracer Techniques