Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells

Autores
Shi, Jian; Miralles, Francesc; Kinet, Jean-Pierre; Birnbaumer, Lutz; Large, William A.; Albert, Anthony P.
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Shi, Jian. University of Leeds. School of Medicine. Institute of Cardiovascular & Metabolic Medicine; Reino Unido
Fil: Miralles, Francesc. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino Unido
Fil: Miralles, Francesc. University of London. Institute of Medical & Biomedical Education; Reino Unido
Fil: Kinet, Jean-Pierre. Harvard Medical School. Beth Israel Deaconess Medical Center. Department of Pathology. Laboratory of Allergy and Immunology; Estados Unidos
Fil: Birnbaumer, Lutz. National Institute of Environmental Health Sciences. Laboratory of Neurobiology; Estados Unidos
Fil: Birnbaumer, Lutz. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina
Fil: Large, William A. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino Unido
Fil: Albert, Anthony P. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino Unido
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.
Fuente
Channels. 2017;11(4):329-339
Materia
CALCIO
MEMBRANA CELULAR
PROTEINAS
MUSCULOS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
Repositorio Institucional (UCA)
Institución
Pontificia Universidad Católica Argentina
OAI Identificador
oai:ucacris:123456789/8727

id RIUCA_1196e9e4ac486ffbca32acfec380ebe1
oai_identifier_str oai:ucacris:123456789/8727
network_acronym_str RIUCA
repository_id_str 2585
network_name_str Repositorio Institucional (UCA)
spelling Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cellsShi, JianMiralles, FrancescKinet, Jean-PierreBirnbaumer, LutzLarge, William A.Albert, Anthony P.CALCIOMEMBRANA CELULARPROTEINASMUSCULOSFil: Shi, Jian. University of Leeds. School of Medicine. Institute of Cardiovascular & Metabolic Medicine; Reino UnidoFil: Miralles, Francesc. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino UnidoFil: Miralles, Francesc. University of London. Institute of Medical & Biomedical Education; Reino UnidoFil: Kinet, Jean-Pierre. Harvard Medical School. Beth Israel Deaconess Medical Center. Department of Pathology. Laboratory of Allergy and Immunology; Estados UnidosFil: Birnbaumer, Lutz. National Institute of Environmental Health Sciences. Laboratory of Neurobiology; Estados UnidosFil: Birnbaumer, Lutz. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; ArgentinaFil: Large, William A. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino UnidoFil: Albert, Anthony P. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino UnidoAbstract: 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.Taylor & Francis2017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://repositorio.uca.edu.ar/handle/123456789/87271933-69501933-6969 (online)10.1080/19336950.2017.130302528301277Shi 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/123456789/8727Channels. 2017;11(4):329-339reponame:Repositorio Institucional (UCA)instname:Pontificia Universidad Católica Argentinaenginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/4.0/2025-07-03T10:56:54Zoai:ucacris:123456789/8727instacron:UCAInstitucionalhttps://repositorio.uca.edu.ar/Universidad privadaNo correspondehttps://repositorio.uca.edu.ar/oaiclaudia_fernandez@uca.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:25852025-07-03 10:56:55.126Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentinafalse
dc.title.none.fl_str_mv Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells
title Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells
spellingShingle Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells
Shi, Jian
CALCIO
MEMBRANA CELULAR
PROTEINAS
MUSCULOS
title_short Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells
title_full Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells
title_fullStr Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells
title_full_unstemmed Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells
title_sort Evidence that Orai1 does not contribute to store-operated TRPC1 channels in vascular smooth muscle cells
dc.creator.none.fl_str_mv Shi, Jian
Miralles, Francesc
Kinet, Jean-Pierre
Birnbaumer, Lutz
Large, William A.
Albert, Anthony P.
author Shi, Jian
author_facet Shi, Jian
Miralles, Francesc
Kinet, Jean-Pierre
Birnbaumer, Lutz
Large, William A.
Albert, Anthony P.
author_role author
author2 Miralles, Francesc
Kinet, Jean-Pierre
Birnbaumer, Lutz
Large, William A.
Albert, Anthony P.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv CALCIO
MEMBRANA CELULAR
PROTEINAS
MUSCULOS
topic CALCIO
MEMBRANA CELULAR
PROTEINAS
MUSCULOS
dc.description.none.fl_txt_mv Fil: Shi, Jian. University of Leeds. School of Medicine. Institute of Cardiovascular & Metabolic Medicine; Reino Unido
Fil: Miralles, Francesc. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino Unido
Fil: Miralles, Francesc. University of London. Institute of Medical & Biomedical Education; Reino Unido
Fil: Kinet, Jean-Pierre. Harvard Medical School. Beth Israel Deaconess Medical Center. Department of Pathology. Laboratory of Allergy and Immunology; Estados Unidos
Fil: Birnbaumer, Lutz. National Institute of Environmental Health Sciences. Laboratory of Neurobiology; Estados Unidos
Fil: Birnbaumer, Lutz. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina
Fil: Large, William A. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino Unido
Fil: Albert, Anthony P. University of London. Institute of Molecular & Clinical Sciences Research Institute. Vascular Biology Research Centre; Reino Unido
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.
description Fil: Shi, Jian. University of Leeds. School of Medicine. Institute of Cardiovascular & Metabolic Medicine; Reino Unido
publishDate 2017
dc.date.none.fl_str_mv 2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://repositorio.uca.edu.ar/handle/123456789/8727
1933-6950
1933-6969 (online)
10.1080/19336950.2017.1303025
28301277
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
url https://repositorio.uca.edu.ar/handle/123456789/8727
identifier_str_mv 1933-6950
1933-6969 (online)
10.1080/19336950.2017.1303025
28301277
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
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/4.0/
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
dc.source.none.fl_str_mv Channels. 2017;11(4):329-339
reponame:Repositorio Institucional (UCA)
instname:Pontificia Universidad Católica Argentina
reponame_str Repositorio Institucional (UCA)
collection Repositorio Institucional (UCA)
instname_str Pontificia Universidad Católica Argentina
repository.name.fl_str_mv Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentina
repository.mail.fl_str_mv claudia_fernandez@uca.edu.ar
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score 13.070432