pubmed-article:2090953 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2090953 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
pubmed-article:2090953 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
pubmed-article:2090953 | lifeskim:mentions | umls-concept:C0030281 | lld:lifeskim |
pubmed-article:2090953 | lifeskim:mentions | umls-concept:C0001443 | lld:lifeskim |
pubmed-article:2090953 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
pubmed-article:2090953 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:2090953 | pubmed:dateCreated | 1991-6-3 | lld:pubmed |
pubmed-article:2090953 | pubmed:abstractText | The patch-clamp technique was used to examine the tolbutamide-sensitivity of the adenosine 5'-triphosphate (ATP)-dependent K+ channel in mouse pancreatic B-cells. When studied at 37 degrees C in cell-attached membrane patches, this channel had a single-channel conductance of 88 pS and was half-maximally inhibited by 2.2 mumol/l tolbutamide in the presence of 3 mmol/l D-glucose and 10 mumol/l nifedipine. The tolbutamide-induced decrease in the amplitude of the single-channel currents indicated that the membrane potential was sufficiently depolarized for initiation of insulin release by 30 but not by 10 mumol/l of tolbutamide. Using 300 mumol/l diazoxide to open the ATP-dependent K+ channels already closed by 3 mmol/l D-glucose alone, it was demonstrated that initiation of insulin release requires closure of more than 98% of all ATP-dependent K+ channels. In excised inside-out membrane patches, the K+ channel-blocking potency of tolbutamide was maximally enhanced by 0.3 mmol/l adenosine 5'-diphosphate (ADP) at the cytoplasmic side. This ADP effect required the presence of Mg2+. Inhibition of K+ channel activity by ATP, ADP (Mg2(+)-free) or their non-hydrolyzable analogues adenylyl-imidodiphosphate (AMP-PNP) and alpha, beta methylene adenosine 5'-diphosphate (AMP-CP) was not accompanied by enhancement of tolbutamide-sensitivity. The results suggest that cytosolic MgADP controls tolbutamide-sensitivity by interaction with a receptor site not identical with the site mediating channel closure and that this control plays a role in the intact B-cell. | lld:pubmed |
pubmed-article:2090953 | pubmed:language | eng | lld:pubmed |
pubmed-article:2090953 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2090953 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2090953 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2090953 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2090953 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2090953 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2090953 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2090953 | pubmed:month | Nov | lld:pubmed |
pubmed-article:2090953 | pubmed:issn | 0028-1298 | lld:pubmed |
pubmed-article:2090953 | pubmed:author | pubmed-author:PantenUU | lld:pubmed |
pubmed-article:2090953 | pubmed:author | pubmed-author:SchefferKK | lld:pubmed |
pubmed-article:2090953 | pubmed:author | pubmed-author:ZünklerB JBJ | lld:pubmed |
pubmed-article:2090953 | pubmed:author | pubmed-author:Schwanstecher... | lld:pubmed |
pubmed-article:2090953 | pubmed:author | pubmed-author:RosenbergerFF | lld:pubmed |
pubmed-article:2090953 | pubmed:author | pubmed-author:HeipelCC | lld:pubmed |
pubmed-article:2090953 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2090953 | pubmed:volume | 342 | lld:pubmed |
pubmed-article:2090953 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2090953 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2090953 | pubmed:pagination | 566-74 | lld:pubmed |
pubmed-article:2090953 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
pubmed-article:2090953 | pubmed:meshHeading | pubmed-meshheading:2090953-... | lld:pubmed |
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pubmed-article:2090953 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2090953 | pubmed:articleTitle | Tolbutamide-sensitivity of the adenosine 5'-triphosphate-dependent K+ channel in mouse pancreatic B-cells. | lld:pubmed |
pubmed-article:2090953 | pubmed:affiliation | Institut für Pharmakologie und Toxikologie, Universität Göttingen, Federal Republic of Germany. | lld:pubmed |
pubmed-article:2090953 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2090953 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:2090953 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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