| pubmed-article:15140874 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15140874 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:15140874 | lifeskim:mentions | umls-concept:C0521116 | lld:lifeskim |
| pubmed-article:15140874 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:15140874 | pubmed:dateCreated | 2004-5-17 | lld:pubmed |
| pubmed-article:15140874 | pubmed:abstractText | Stimulation of muscarinic acetylcholine receptors (mAChRs) can activate an inward rectifier K(+) current (I(KACh)), which is mediated by the M(2) subtype of mAChR in cardiac myocytes. Recently, a novel delayed rectifier-like K(+) current mediated by activation of the cardiac M(3) receptors (designated I(KM3)) was identified, which is distinct from I(KACh) and other known K(+) currents. While I(KACh) is known to be a G(i) protein-gated K(+) channel, the signal transduction mechanisms for I(KM3) activation remained unexplored. We studied I(KM3) with whole-cell patch clamp and macropatch clamp techniques. Whole cell I(KM3) activated by choline persisted with minimal rundown over 2 h in presence of internal GTP. When GTP was replaced by guanyl-5'-yl thiophosphate, I(KM3) demonstrated rapid and extensive rundown. While I(KACh) (induced by ACh) was markedly reduced in cells pretreated with pertussis toxin, I(KM3) was unaltered. Intracellular application of antibodies targeting alpha-subunit of G(i/o) protein suppressed I(KACh) without affecting I(KM3). Antibodies targeting the N and the C terminus, respectively, of G(q) protein alpha-subunit substantially depressed I(KM3) but failed to alter I(KACh). The antibody against beta-subunits of G proteins inhibited both I(KACh) and I(KM3). I(KM3) activated by choline in the cell-attached mode of macropatches persisted in the cell-free configuration. Application of purified G(q) protein alpha-subunit or betagamma-subunit of G proteins or guanosine 5'-O-(thiotriphosphate) to the internal solution activated I(KM3)-like currents in inside-out patches. Our findings revealed a novel aspect of receptor-channel signal transduction mechanisms, and I(KM3) represents the first G(q) protein-coupled K(+) channel. We propose that the G protein-coupled K(+) channel family could be divided into two subfamilies: G(i) protein-coupled K(+) channel subfamily and G(q) protein-coupled K(+) channel subfamily. | lld:pubmed |
| pubmed-article:15140874 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15140874 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15140874 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15140874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15140874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15140874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15140874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15140874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15140874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15140874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15140874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15140874 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15140874 | pubmed:month | May | lld:pubmed |
| pubmed-article:15140874 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15140874 | pubmed:author | pubmed-author:HallJ CJC | lld:pubmed |
| pubmed-article:15140874 | pubmed:author | pubmed-author:WangZhiguoZ | lld:pubmed |
| pubmed-article:15140874 | pubmed:author | pubmed-author:WangHuizhenH | lld:pubmed |
| pubmed-article:15140874 | pubmed:author | pubmed-author:YangBaofengB | lld:pubmed |
| pubmed-article:15140874 | pubmed:author | pubmed-author:XuDonghuiD | lld:pubmed |
| pubmed-article:15140874 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15140874 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:15140874 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:15140874 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15140874 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15140874 | pubmed:pagination | 21774-8 | lld:pubmed |
| pubmed-article:15140874 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:meshHeading | pubmed-meshheading:15140874... | lld:pubmed |
| pubmed-article:15140874 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15140874 | pubmed:articleTitle | The M3 receptor-mediated K(+) current (IKM3), a G(q) protein-coupled K(+) channel. | lld:pubmed |
| pubmed-article:15140874 | pubmed:affiliation | Research Center, Montreal Heart Institute, Montreal, Quebec H1T 1C8, Canada. | lld:pubmed |
| pubmed-article:15140874 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15140874 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:403827 | entrezgene:pubmed | pubmed-article:15140874 | lld:entrezgene |
| entrez-gene:403858 | entrezgene:pubmed | pubmed-article:15140874 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15140874 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15140874 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15140874 | lld:pubmed |
