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Article: Endothelium-dependent hyperpolarization to acetylcholine in carotid artery of guinea pig: Role of lipoxygenase

TitleEndothelium-dependent hyperpolarization to acetylcholine in carotid artery of guinea pig: Role of lipoxygenase
Authors
KeywordsArachidonic acid
BKCa
Electrophysiology
Endothelial-derived hyperpolarizing factor
IKCa
Lipoxygenase
Phospholipase A2
Phospholipase C
Issue Date2002
PublisherLippincott Williams & Wilkins. The Journal's web site is located at http://www.cardiovascularpharm.com/
Citation
Journal Of Cardiovascular Pharmacology, 2002, v. 40 n. 3, p. 467-477 How to Cite?
AbstractThis study was designed to determine whether lipoxygenase-dependent metabolites of arachidonic acid are involved in the endothelium-dependent hyperpolarization of the guinea pig carotid artery. The membrane potential of vascular smooth muscle cells was measured with intracellular microelectrodes and potassium channels were studied on freshly isolated cells with the patch-clamp technique. Acetylcholine-induced hyperpolarizations were not affected by arachidonyl trifluoromethyl ketone (AACOCF3), quinacrine (phospholipase A2 inhibitors), or eicosatetraenoic acid (nonspecific inhibitor of lipoxygenase, cytochrome P450, and cyclooxygenase). In contrast, cinnamyl-3,4 dihydroxy-α-cyanocinnamate (CDC) and AA861 (lipoxygenase inhibitors) as well as 1-(6-(17β-3-methoxyestra-1,3,5(10)-trien-17-yl)amino) hexyl)-1H-pyrrole-2,5-dione (U-73122) (phospholipase C inhibitor) produced a significant inhibition of the hyperpolarization. An opener of intermediate conductance calcium-activated potassium channels, 1-ethyl-2-benzamidazolinone (1-EBIO), induced a hyperpolarization that was unaffected by AACOCF3, CDC, AA861, or U-73122 but was inhibited by charybdotoxin. (±)12-hydroxy-eicosatetraenoic acid (12-HETE) and 12(S)-hydroperoxy-eicosatetraenoic acid (12(S)-HpETE) did not induce any significant changes in membrane potential. CDC inhibited the voltage-gated potassium current and increased the large conductance calcium-activated potassium current whereas AA861 inhibited both potassium currents. These results confirm that, in the isolated carotid artery of the guinea pig, stimulation of endothelial muscarinic receptors involves phospholipase C activation and indicate that the activation of phospholipase A2 and the release of lipoxygenase metabolites is unlikely to explain endothelium-dependent hyperpolarization.
Persistent Identifierhttp://hdl.handle.net/10722/171283
ISSN
2023 Impact Factor: 2.6
2023 SCImago Journal Rankings: 0.610
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorQuignard, JFen_US
dc.contributor.authorChataigneau, Ten_US
dc.contributor.authorCorriu, Cen_US
dc.contributor.authorEdwards, Gen_US
dc.contributor.authorWeston, Aen_US
dc.contributor.authorFélétou, Men_US
dc.contributor.authorVanhoutte, PMen_US
dc.date.accessioned2012-10-30T06:13:10Z-
dc.date.available2012-10-30T06:13:10Z-
dc.date.issued2002en_US
dc.identifier.citationJournal Of Cardiovascular Pharmacology, 2002, v. 40 n. 3, p. 467-477en_US
dc.identifier.issn0160-2446en_US
dc.identifier.urihttp://hdl.handle.net/10722/171283-
dc.description.abstractThis study was designed to determine whether lipoxygenase-dependent metabolites of arachidonic acid are involved in the endothelium-dependent hyperpolarization of the guinea pig carotid artery. The membrane potential of vascular smooth muscle cells was measured with intracellular microelectrodes and potassium channels were studied on freshly isolated cells with the patch-clamp technique. Acetylcholine-induced hyperpolarizations were not affected by arachidonyl trifluoromethyl ketone (AACOCF3), quinacrine (phospholipase A2 inhibitors), or eicosatetraenoic acid (nonspecific inhibitor of lipoxygenase, cytochrome P450, and cyclooxygenase). In contrast, cinnamyl-3,4 dihydroxy-α-cyanocinnamate (CDC) and AA861 (lipoxygenase inhibitors) as well as 1-(6-(17β-3-methoxyestra-1,3,5(10)-trien-17-yl)amino) hexyl)-1H-pyrrole-2,5-dione (U-73122) (phospholipase C inhibitor) produced a significant inhibition of the hyperpolarization. An opener of intermediate conductance calcium-activated potassium channels, 1-ethyl-2-benzamidazolinone (1-EBIO), induced a hyperpolarization that was unaffected by AACOCF3, CDC, AA861, or U-73122 but was inhibited by charybdotoxin. (±)12-hydroxy-eicosatetraenoic acid (12-HETE) and 12(S)-hydroperoxy-eicosatetraenoic acid (12(S)-HpETE) did not induce any significant changes in membrane potential. CDC inhibited the voltage-gated potassium current and increased the large conductance calcium-activated potassium current whereas AA861 inhibited both potassium currents. These results confirm that, in the isolated carotid artery of the guinea pig, stimulation of endothelial muscarinic receptors involves phospholipase C activation and indicate that the activation of phospholipase A2 and the release of lipoxygenase metabolites is unlikely to explain endothelium-dependent hyperpolarization.en_US
dc.languageengen_US
dc.publisherLippincott Williams & Wilkins. The Journal's web site is located at http://www.cardiovascularpharm.com/en_US
dc.relation.ispartofJournal of Cardiovascular Pharmacologyen_US
dc.subjectArachidonic acid-
dc.subjectBKCa-
dc.subjectElectrophysiology-
dc.subjectEndothelial-derived hyperpolarizing factor-
dc.subjectIKCa-
dc.subjectLipoxygenase-
dc.subjectPhospholipase A2-
dc.subjectPhospholipase C-
dc.subject.meshAcetylcholine - Pharmacologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCarotid Arteries - Drug Effects - Enzymologyen_US
dc.subject.meshEndothelium, Vascular - Drug Effects - Enzymologyen_US
dc.subject.meshGuinea Pigsen_US
dc.subject.meshLipoxygenase - Physiologyen_US
dc.subject.meshMaleen_US
dc.subject.meshMembrane Potentials - Drug Effects - Physiologyen_US
dc.subject.meshMuscle, Smooth, Vascular - Cytology - Drug Effects - Enzymologyen_US
dc.subject.meshPatch-Clamp Techniquesen_US
dc.subject.meshVasoconstriction - Drug Effects - Physiologyen_US
dc.titleEndothelium-dependent hyperpolarization to acetylcholine in carotid artery of guinea pig: Role of lipoxygenaseen_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.doi10.1097/00005344-200209000-00016en_US
dc.identifier.pmid12198333-
dc.identifier.scopuseid_2-s2.0-0036708267en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036708267&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume40en_US
dc.identifier.issue3en_US
dc.identifier.spage467en_US
dc.identifier.epage477en_US
dc.identifier.isiWOS:000177704100016-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridQuignard, JF=13606215800en_US
dc.identifier.scopusauthoridChataigneau, T=6602561430en_US
dc.identifier.scopusauthoridCorriu, C=6602961498en_US
dc.identifier.scopusauthoridEdwards, G=7402317535en_US
dc.identifier.scopusauthoridWeston, A=7102913361en_US
dc.identifier.scopusauthoridFélétou, M=7006461826en_US
dc.identifier.scopusauthoridVanhoutte, PM=7202304247en_US
dc.identifier.issnl0160-2446-

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