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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Shi, Jian | es |
dc.contributor.author | Miralles, Francesc | es |
dc.contributor.author | Kinet, Jean-Pierre | es |
dc.contributor.author | Birnbaumer, Lutz | es |
dc.contributor.author | Large, William A. | es |
dc.contributor.author | Albert, Anthony P. | es |
dc.date.accessioned | 2019-09-12T17:56:42Z | - |
dc.date.available | 2019-09-12T17:56:42Z | - |
dc.date.issued | 2017 | - |
dc.identifier.citation | Shi J, Miralles F, Kinet J-P, Birnbaumer L, Large WA, Albert AP. Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells [en línea]. Channels. 2017;11(4):329-339. doi:10.1080/19336950.2017.1303025 Disponible en: https://repositorio.uca.edu.ar/handle/123456789/8727 | es |
dc.identifier.issn | 1933-6950 | - |
dc.identifier.issn | 1933-6969 (online) | - |
dc.identifier.uri | https://repositorio.uca.edu.ar/handle/123456789/8727 | - |
dc.description.abstract | Abstract: Ca2+-permeable store-operated channels (SOCs) mediate Ca2+ entry pathways which are involved in many cellular functions such as contraction, growth, and proliferation. Prototypical SOCs are formed of Orai1 proteins and are activated by the endo/sarcoplasmic reticulum Ca2+ sensor stromal interaction molecule 1 (STIM1). There is considerable debate about whether canonical transient receptor potential 1 (TRPC1) proteins also form store-operated channels (SOCs), and if they do, is Orai1 involved. We recently showed that stimulation of TRPC1-based SOCs involves store depletion inducing STIM1-evoked Gαq/PLCβ1 activity in contractile vascular smooth muscle cells (VSMCs). Therefore the present work investigates the role of Orai1 in activation of TRPC1-based SOCs in freshly isolated mesenteric artery VSMCs from wild-type (WT) and Orai1-/- mice. Store-operated whole-cell and single channel currents recorded from WT and Orai1-/- VSMCs had similar properties, with relatively linear current-voltage relationships, reversal potentials of about +20mV, unitary conductances of about 2pS, and inhibition by anti-TRPC1 and anti-STIM1 antibodies. In Orai1-/- VSMCs, store depletion induced PLCβ1 activity measured with the fluorescent phosphatidylinositol 4,5-bisphosphate/inositol 1,4,5-trisphosphate biosensor GFP-PLCδ1-PH, which was prevented by knockdown of STIM1. In addition, in Orai1-/- VSMCs, store depletion induced translocation of STIM1 from within the cell to the plasma membrane where it formed STIM1-TRPC1 interactions at discrete puncta-like sites. These findings indicate that activation of TRPC1-based SOCs through a STIM1-activated PLCβ1 pathway are likely to occur independently of Orai1 proteins, providing evidence that TRPC1 channels form genuine SOCs in VSMCs with a contractile phenotype. | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Taylor & Francis | es |
dc.rights | Acceso Abierto | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.source | Channels. 2017;11(4):329-339 | es |
dc.subject | CALCIO | es |
dc.subject | MEMBRANA CELULAR | es |
dc.subject | PROTEINAS | es |
dc.subject | MUSCULOS | es |
dc.title | Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells | es |
dc.type | Artículo | es |
dc.identifier.doi | 10.1080/19336950.2017.1303025 | - |
dc.identifier.pmid | 28301277 | - |
uca.disciplina | MEDICINA | es |
uca.issnrd | 1 | es |
uca.affiliation | Fil: Shi, Jian. University of Leeds. School of Medicine. Institute of Cardiovascular & Metabolic Medicine; Reino Unido | es |
uca.affiliation | Fil: Miralles, Francesc. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino Unido | es |
uca.affiliation | Fil: Miralles, Francesc. University of London. Institute of Medical & Biomedical Education; Reino Unido | es |
uca.affiliation | Fil: Kinet, Jean-Pierre. Harvard Medical School. Beth Israel Deaconess Medical Center. Department of Pathology. Laboratory of Allergy and Immunology; Estados Unidos | es |
uca.affiliation | Fil: Birnbaumer, Lutz. National Institute of Environmental Health Sciences. Laboratory of Neurobiology; Estados Unidos | es |
uca.affiliation | Fil: Birnbaumer, Lutz. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina | es |
uca.affiliation | Fil: Large, William A. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino Unido | es |
uca.affiliation | Fil: Albert, Anthony P. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino Unido | es |
uca.version | publishedVersion | es |
item.grantfulltext | open | - |
item.fulltext | With Fulltext | - |
item.languageiso639-1 | en | - |
crisitem.author.dept | Instituto de Investigaciones Biomédicas - BIOMED | - |
crisitem.author.dept | Laboratorio de Función y Farmacología de Canales Iónicos | - |
crisitem.author.dept | Consejo Nacional de Investigaciones Científicas y Técnicas | - |
crisitem.author.dept | Facultad de Ciencias Médicas | - |
crisitem.author.orcid | 0000-0002-0775-8661 | - |
crisitem.author.parentorg | Facultad de Ciencias Médicas | - |
crisitem.author.parentorg | Instituto de Investigaciones Biomédicas - BIOMED | - |
crisitem.author.parentorg | Pontificia Universidad Católica Argentina | - |
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