| http://purl.uniprot.org/citations/18162464 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18162464 | http://www.w3.org/2000/01/rdf-schema#comment | "The effects of norepinephrine (NE), an inhibitor of insulin secretion, were examined on membrane potential and the ATP-sensitive K+ channel (K ATP) in INS 832/13 cells. Membrane potential was monitored under the whole cell current clamp mode. NE hyperpolarized the cell membrane, an effect that was abolished by tolbutamide. The effect of NE on K ATP channels was investigated in parallel using outside-out single channel recording. This revealed that NE enhanced the open activities of the K ATP channels approximately 2-fold without changing the single channel conductance, demonstrating that NE-induced hyperpolarization was mediated by activation of the K ATP channels. The NE effect was abolished in cells preincubated with pertussis toxin, indicating coupling to heterotrimeric G i/G o proteins. To identify the G proteins involved, antisera raised against alpha and beta subunits (anti-G alpha common, anti-G beta, anti-G alpha i1/2/3, and anti-G alpha o) were used. Anti-G alpha common totally blocked the effects of NE on membrane potential and K ATP channels. Individually, anti-G alpha i1/2/3 and anti-G alpha o only partially inhibited the action of NE on K ATP channels. However, the combination of both completely eliminated the action. Antibodies against G beta had no effects. To confirm these results and to further identify the G protein subunits involved, the blocking effects of peptides containing the sequence of 11 amino acids at the C termini of the alpha subunits were used. The data obtained were similar to those derived from the antibody work with the additional information that G alpha i3 and G alpha o1 were not involved. In conclusion, both G i and G o proteins are required for the full effect of norepinephrine to activate the K ATP channel."xsd:string |
| http://purl.uniprot.org/citations/18162464 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m707695200"xsd:string |
| http://purl.uniprot.org/citations/18162464 | http://purl.uniprot.org/core/author | "Fang Q."xsd:string |
| http://purl.uniprot.org/citations/18162464 | http://purl.uniprot.org/core/author | "Zhao Y."xsd:string |
| http://purl.uniprot.org/citations/18162464 | http://purl.uniprot.org/core/author | "Sharp G.W."xsd:string |
| http://purl.uniprot.org/citations/18162464 | http://purl.uniprot.org/core/author | "Straub S.G."xsd:string |
| http://purl.uniprot.org/citations/18162464 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18162464 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/18162464 | http://purl.uniprot.org/core/pages | "5306-5316"xsd:string |
| http://purl.uniprot.org/citations/18162464 | http://purl.uniprot.org/core/title | "Both G i and G o heterotrimeric G proteins are required to exert the full effect of norepinephrine on the beta-cell K ATP channel."xsd:string |
| http://purl.uniprot.org/citations/18162464 | http://purl.uniprot.org/core/volume | "283"xsd:string |
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