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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2006-2-6
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pubmed:abstractText |
We investigated the effects of the vasoconstrictor angiotensin (Ang) II on the whole cell inward rectifier K(+) (Kir) current enzymatically isolated from small-diameter (<100 microm) coronary arterial smooth muscle cells (CASMCs). Ang II inhibited the Kir current in a dose-dependent manner (half inhibition value: 154 nM). Pretreatment with phospholipase C inhibitor and protein kinase C (PKC) inhibitors prevented the Ang II-induced inhibition of the Kir current. The PKC activator reduced the Kir currents. The inhibitory effect of Ang II was reduced by intracellular and extracellular Ca(2+) free condition and by Gö6976, which inhibits Ca(2+)-dependent PKC isoforms alpha and beta. However, the inhibitory effect of Ang II was unaffected by a peptide that selectively inhibits the translocation of the epsilon isoform of PKC. Western blot analysis confirmed that PKCalpha, and not PKCbeta, was expressed in small-diameter CASMCs. The Ang II type 1 (AT(1))-receptor antagonist CV-11974 prevented the Ang II-induced inhibition of the Kir current. From these results, we conclude that Ang II inhibits Kir channels through AT(1) receptors by the activation of PKCalpha.
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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/Angiotensin II,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Inwardly...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Angiotensin, Type 1,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
341
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
728-35
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16442501-Angiotensin II,
pubmed-meshheading:16442501-Animals,
pubmed-meshheading:16442501-Calcium,
pubmed-meshheading:16442501-Cations, Divalent,
pubmed-meshheading:16442501-Cells, Cultured,
pubmed-meshheading:16442501-Electrophysiology,
pubmed-meshheading:16442501-Female,
pubmed-meshheading:16442501-Isoenzymes,
pubmed-meshheading:16442501-Male,
pubmed-meshheading:16442501-Muscle, Smooth, Vascular,
pubmed-meshheading:16442501-Myocytes, Smooth Muscle,
pubmed-meshheading:16442501-Patch-Clamp Techniques,
pubmed-meshheading:16442501-Potassium Channels, Inwardly Rectifying,
pubmed-meshheading:16442501-Protein Kinase C-alpha,
pubmed-meshheading:16442501-Protein Kinase Inhibitors,
pubmed-meshheading:16442501-Rabbits,
pubmed-meshheading:16442501-Receptor, Angiotensin, Type 1,
pubmed-meshheading:16442501-Type C Phospholipases
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pubmed:year |
2006
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pubmed:articleTitle |
Angiotensin II inhibits inward rectifier K+ channels in rabbit coronary arterial smooth muscle cells through protein kinase Calpha.
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pubmed:affiliation |
Mitochondrial Signaling Laboratory, Department of Physiology and Biophysics, College of Medicine, Biohealth Products Research Center, Cardiovascular and Metabolic Disease Center, Inje University, Busan, Republic of Korea.
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pubmed:publicationType |
Journal Article
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