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dc.contributor.authorOliveras, Anna-
dc.contributor.authorRoura-Ferrer, Meritxell-
dc.contributor.authorCruz, Alicia de la-
dc.contributor.authorPrieto, Ángela-
dc.contributor.authorEtxeberría, Ainhoa-
dc.contributor.authorCogolludo, Angel-
dc.contributor.authorValenzuela, Carmen-
dc.contributor.authorVillarroel, Alvaro-
dc.contributor.authorFelipe, Antonio-
dc.date.accessioned2015-11-03T11:11:37Z-
dc.date.available2015-11-03T11:11:37Z-
dc.date.issued2014-
dc.identifierdoi: 10.1161/ATVBAHA.114.303801-
dc.identifierissn: 1079-5642-
dc.identifiere-issn: 1524-4636-
dc.identifier.citationArteriosclerosis, Thrombosis, and Vascular Biology 34(7): 1522-1530 (2014)-
dc.identifier.urihttp://hdl.handle.net/10261/124349-
dc.descriptionet al.-
dc.description.abstract[Objective]: Voltage-dependent K (Kv) channels from the Kv7 family are expressed in blood vessels and contribute to cardiovascular physiology. Although Kv7 channel blockers trigger muscle contractions, Kv7 activators act as vasorelaxants. Kv7.1 and Kv7.5 are expressed in many vessels. Kv7.1 is under intense investigation because Kv7.1 blockers fail to modulate smooth muscle reactivity. In this study, we analyzed whether Kv7.1 and Kv7.5 may form functional heterotetrameric channels increasing the channel diversity in vascular smooth muscles. [Approach and Results]: Kv7.1 and Kv7.5 currents elicited in arterial myocytes, oocyte, and mammalian expression systems suggest the formation of heterotetrameric complexes. Kv7.1/Kv7.5 heteromers, exhibiting different pharmacological characteristics, participate in the arterial tone. Kv7.1/Kv7.5 associations were confirmed by coimmunoprecipitation, fluorescence resonance energy transfer, and fluorescence recovery after photobleaching experiments. Kv7.1/Kv7.5 heterotetramers were highly retained at the endoplasmic reticulum. Studies in HEK-293 cells, heart, brain, and smooth and skeletal muscles demonstrated that the predominant presence of Kv7.5 stimulates release of Kv7.1/Kv7.5 oligomers out of lipid raft microdomains. Electrophysiological studies supported that KCNE1 and KCNE3 regulatory subunits further increased the channel diversity. Finally, the analysis of rat isolated myocytes and human blood vessels demonstrated that Kv7.1 and Kv7.5 exhibited a differential expression, which may lead to channel diversity. [Conclusions]: Kv7.1 and Kv7.5 form heterotetrameric channels increasing the diversity of structures which fine-tune blood vessel reactivity. Because the lipid raft localization of ion channels is crucial for cardiovascular physiology, Kv7.1/Kv7.5 heteromers provide efficient spatial and temporal regulation of smooth muscle function. Our results shed light on the debate about the contribution of Kv7 channels to vasoconstriction and hypertension.-
dc.description.sponsorshipThis work was supported by the Ministerio de Ciencia e Innovación (MINECO), Spain (BFU2011-23268 to A. Felipe, and BFU2012-39883 to A. Villarroel; CSD2008-00005 to A. Felipe and A. Villarroel; SAF2010-14916 and RD12/0042/0019 to C. Valenzuela; BFU2010-15674 to C. Soler). L. Solé, A. Oliveras, and A. Prieto are fellows from MINECO. N. Comes and A. de la Cruz are supported by Juan de la Cierva program (MINECO) and CSIC contract, respectively.-
dc.publisherAmerican Heart Association-
dc.rightsclosedAccess-
dc.titleFunctional assembly of Kv7.1/Kv7.5 channels with emerging properties on vascular muscle physiology-
dc.typeartículo-
dc.identifier.doi10.1161/ATVBAHA.114.303801-
dc.date.updated2015-11-03T11:11:37Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.contributor.funderMinisterio de Ciencia e Innovación (España)-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.contributor.funderConsejo Superior de Investigaciones Científicas (España)-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100004837es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003339es_ES
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