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Article: Characterization of an apamin-sensitive small-conductance Ca 2+-activated K + channel in porcine coronary artery endothelium: Relevance to EDHF

TitleCharacterization of an apamin-sensitive small-conductance Ca 2+-activated K + channel in porcine coronary artery endothelium: Relevance to EDHF
Authors
Issue Date2002
PublisherJohn Wiley & Sons Ltd. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0007-1188&site=1
Citation
British Journal Of Pharmacology, 2002, v. 135 n. 5, p. 1133-1143 How to Cite?
Abstract1. The apamin-sensitive small-conductance Ca 2+-activated K + channel (SK Ca) was characterized in porcine coronary arteries. 2. In intact arteries, 100 nM substance P and 600 μM 1-ethyl-2-benzimidazolinone (1-EBIO) produced endothelial cell hyperpolarizations (27.8±0.8 mV and 24.1±1.0 mV, respectively). Charybdotoxin (100 nM) abolished the 1-EBIO response but substance P continued to induce a hyperpolarization (25.8±0.3 mV). 3. In freshly-isolated endothelial cells, outside-out patch recordings revealed a unitary K + conductance of 6.8±0.04 pS. The open-probability was increased by Ca 2+ and reduced by apamin (100 nM). Substance P activated an outward current under whole-cell perforated-patch conditions and a component of this current (38%) was inhibited by apamin. A second conductance of 2.7±0.03 pS inhibited by d-tubocurarine was observed infrequently. 4. Messenger RNA encoding the SK2 and SK3, but not the SK1, subunits of SK Ca was detected by RT-PCR in samples of endothelium. Western blotting indicated that SK3 protein was abundant in samples of endothelium compared to whole arteries. SK2 protein was present in whole artery nuclear fractions. 5. Immunofluorescent labelling confirmed that SK3 was highly expressed at the plasmalemma of endothelial cells and was not expressed in smooth muscle. SK2 was restricted to the peri-nuclear regions of both endothelial and smooth muscle cells. 6. In conclusion, the porcine coronary artery endothelium expresses an apamin-sensitive SK Ca containing the SK3 subunit. These channels are likely to confer all or part of the apamin-sensitive component of the endothelium-derived hyperpolarizing factor (EDHF) response.
Persistent Identifierhttp://hdl.handle.net/10722/171276
ISSN
2015 Impact Factor: 5.259
2015 SCImago Journal Rankings: 2.368
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorBurnham, MPen_US
dc.contributor.authorBychkov, Ren_US
dc.contributor.authorFélétou, Men_US
dc.contributor.authorRichards, GRen_US
dc.contributor.authorVanhoutte, PMen_US
dc.contributor.authorWeston, AHen_US
dc.contributor.authorEdwards, Gen_US
dc.date.accessioned2012-10-30T06:13:07Z-
dc.date.available2012-10-30T06:13:07Z-
dc.date.issued2002en_US
dc.identifier.citationBritish Journal Of Pharmacology, 2002, v. 135 n. 5, p. 1133-1143en_US
dc.identifier.issn0007-1188en_US
dc.identifier.urihttp://hdl.handle.net/10722/171276-
dc.description.abstract1. The apamin-sensitive small-conductance Ca 2+-activated K + channel (SK Ca) was characterized in porcine coronary arteries. 2. In intact arteries, 100 nM substance P and 600 μM 1-ethyl-2-benzimidazolinone (1-EBIO) produced endothelial cell hyperpolarizations (27.8±0.8 mV and 24.1±1.0 mV, respectively). Charybdotoxin (100 nM) abolished the 1-EBIO response but substance P continued to induce a hyperpolarization (25.8±0.3 mV). 3. In freshly-isolated endothelial cells, outside-out patch recordings revealed a unitary K + conductance of 6.8±0.04 pS. The open-probability was increased by Ca 2+ and reduced by apamin (100 nM). Substance P activated an outward current under whole-cell perforated-patch conditions and a component of this current (38%) was inhibited by apamin. A second conductance of 2.7±0.03 pS inhibited by d-tubocurarine was observed infrequently. 4. Messenger RNA encoding the SK2 and SK3, but not the SK1, subunits of SK Ca was detected by RT-PCR in samples of endothelium. Western blotting indicated that SK3 protein was abundant in samples of endothelium compared to whole arteries. SK2 protein was present in whole artery nuclear fractions. 5. Immunofluorescent labelling confirmed that SK3 was highly expressed at the plasmalemma of endothelial cells and was not expressed in smooth muscle. SK2 was restricted to the peri-nuclear regions of both endothelial and smooth muscle cells. 6. In conclusion, the porcine coronary artery endothelium expresses an apamin-sensitive SK Ca containing the SK3 subunit. These channels are likely to confer all or part of the apamin-sensitive component of the endothelium-derived hyperpolarizing factor (EDHF) response.en_US
dc.languageengen_US
dc.publisherJohn Wiley & Sons Ltd. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0007-1188&site=1en_US
dc.relation.ispartofBritish Journal of Pharmacologyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshApamin - Pharmacologyen_US
dc.subject.meshBiological Factors - Physiologyen_US
dc.subject.meshCoronary Vessels - Drug Effects - Physiologyen_US
dc.subject.meshDna, Complementary - Analysisen_US
dc.subject.meshEndothelium, Vascular - Drug Effects - Physiologyen_US
dc.subject.meshFemaleen_US
dc.subject.meshMaleen_US
dc.subject.meshMembrane Potentials - Drug Effectsen_US
dc.subject.meshMicroelectrodesen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMuscle, Smooth, Vascular - Drug Effects - Physiologyen_US
dc.subject.meshPatch-Clamp Techniquesen_US
dc.subject.meshPotassium Channels - Drug Effects - Genetics - Physiologyen_US
dc.subject.meshPotassium Channels, Calcium-Activateden_US
dc.subject.meshReverse Transcriptase Polymerase Chain Reactionen_US
dc.subject.meshSmall-Conductance Calcium-Activated Potassium Channelsen_US
dc.subject.meshSubstance P - Pharmacologyen_US
dc.subject.meshSwineen_US
dc.titleCharacterization of an apamin-sensitive small-conductance Ca 2+-activated K + channel in porcine coronary artery endothelium: Relevance to EDHFen_US
dc.typeArticleen_US
dc.identifier.emailVanhoutte, PM:vanhoutt@hku.hken_US
dc.identifier.authorityVanhoutte, PM=rp00238en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1038/sj.bjp.0704551-
dc.identifier.pmid11877319-
dc.identifier.scopuseid_2-s2.0-0036196684en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036196684&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume135en_US
dc.identifier.issue5en_US
dc.identifier.spage1133en_US
dc.identifier.epage1143en_US
dc.identifier.isiWOS:000174384400007-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridBurnham, MP=7004848578en_US
dc.identifier.scopusauthoridBychkov, R=6603668408en_US
dc.identifier.scopusauthoridFélétou, M=7006461826en_US
dc.identifier.scopusauthoridRichards, GR=7201583688en_US
dc.identifier.scopusauthoridVanhoutte, PM=7202304247en_US
dc.identifier.scopusauthoridWeston, AH=7102913361en_US
dc.identifier.scopusauthoridEdwards, G=7402317535en_US

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