| pubmed-article:1710783 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1710783 | lifeskim:mentions | umls-concept:C0037659 | lld:lifeskim |
| pubmed-article:1710783 | lifeskim:mentions | umls-concept:C1158884 | lld:lifeskim |
| pubmed-article:1710783 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:1710783 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:1710783 | pubmed:issue | 6327 | lld:pubmed |
| pubmed-article:1710783 | pubmed:dateCreated | 1991-7-12 | lld:pubmed |
| pubmed-article:1710783 | pubmed:abstractText | The neuropeptide somatostatin inhibits secretion from electrically excitable cells in the pituitary, pancreas, gut and brain. In mammalian pituitary tumour cells somatostatin inhibits secretion through two distinct pertussis toxin-sensitive mechanisms. One involves inhibition of adenylyl cyclase, the other an unidentified cyclic AMP-independent mechanism that reduces Ca2+ influx by increasing membrane conductance to potassium. Here we demonstrate that the predominant electrophysiological effect of somatostatin on metabolically intact pituitary tumour cells is a large, sustained increase in the activity of the large-conductance Ca(2+)- and voltage-activated K+ channels (BK). This action of somatostatin does not involve direct effects of Ca2+, cAMP or G proteins on the channels. Our results indicate instead that somatostatin stimulates BK channel activity through protein dephosphorylation. | lld:pubmed |
| pubmed-article:1710783 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1710783 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1710783 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1710783 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1710783 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:1710783 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:1710783 | pubmed:author | pubmed-author:WhiteR ERE | lld:pubmed |
| pubmed-article:1710783 | pubmed:author | pubmed-author:SchonbrunnAA | lld:pubmed |
| pubmed-article:1710783 | pubmed:author | pubmed-author:ArmstrongD... | lld:pubmed |
| pubmed-article:1710783 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1710783 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:1710783 | pubmed:volume | 351 | lld:pubmed |
| pubmed-article:1710783 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1710783 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1710783 | pubmed:pagination | 570-3 | lld:pubmed |
| pubmed-article:1710783 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:1710783 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1710783 | pubmed:articleTitle | Somatostatin stimulates Ca(2+)-activated K+ channels through protein dephosphorylation. | lld:pubmed |
| pubmed-article:1710783 | pubmed:affiliation | Laboratory of Cellular and Molecular Pharmacology, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709. | lld:pubmed |
| pubmed-article:1710783 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1710783 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:1710783 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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