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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1989-5-24
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pubmed:abstractText |
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 86Rb+ flux techniques. Both PMA and somatostatin hyperpolarize insulinoma cells by activating ATP-sensitive K+ 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 86Rb+ 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+ channels are discussed.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-1093547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2428009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2430073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2431383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2431411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2432604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2436138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2440063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2445740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2448801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2452599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2456203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2456243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2456612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2460348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2469152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2470586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2833498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2845929,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2846562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2874559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2874591,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2891695,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2896064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-2898785,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-3029056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-3049931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-3056715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-6115784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-6134520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-6270629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2565041-6277201
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Glyburide,
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Rubidium,
http://linkedlifedata.com/resource/pubmed/chemical/Somatostatin,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
86
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2971-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2565041-Adenoma, Islet Cell,
pubmed-meshheading:2565041-Adenosine Triphosphate,
pubmed-meshheading:2565041-Animals,
pubmed-meshheading:2565041-Cyclic AMP,
pubmed-meshheading:2565041-Glyburide,
pubmed-meshheading:2565041-Insulinoma,
pubmed-meshheading:2565041-Pertussis Toxin,
pubmed-meshheading:2565041-Potassium Channels,
pubmed-meshheading:2565041-Protein Kinase C,
pubmed-meshheading:2565041-Rats,
pubmed-meshheading:2565041-Rubidium,
pubmed-meshheading:2565041-Somatostatin,
pubmed-meshheading:2565041-Tetradecanoylphorbol Acetate,
pubmed-meshheading:2565041-Tumor Cells, Cultured,
pubmed-meshheading:2565041-Virulence Factors, Bordetella
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pubmed:year |
1989
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pubmed:articleTitle |
Regulation of ATP-sensitive K+ channels in insulinoma cells: activation by somatostatin and protein kinase C and the role of cAMP.
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pubmed:affiliation |
Centre de Biochimie du Centre National de la Recherche Scientifique, Nice, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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