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
- Institución
- Pontificia Universidad Católica Argentina
- OAI Identificador
- oai:ucacris:123456789/8727
Ver los metadatos del registro completo
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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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1836638347732189184 |
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13.070432 |