Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes
- Autores
- Kotsias, Basilio Aristides; Peracchia, C.
- Año de publicación
- 2005
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride (Cl−) channel known to influence the function of other channels, including connexin channels. To further study potential functional interactions between CFTR and gap junction channels, we have co-expressed CFTR and connexin45 (Cx45) in Xenopus oocytes and monitored junctional conductance and voltage sensitivity by dual voltage clamp electrophysiology. In single oocytes expressing CFTR, an increase in cAMP caused by forskolin application induced a Cl− current and increased membrane conductance; application of diphenylamine carboxylic acid (CFTR blocker) readily blocked the Cl− current. With co-expression of CFTR and Cx45, application of forskolin to paired oocytes induced a typical outward current and increased junctional conductance (Gj). In addition, the presence of CFTR reduced the transjunctional voltage sensitivity of Cx45 channels without affecting the kinetics of junctional current inactivation. The drop in voltage sensitivity was further enhanced by forskolin application. The data indicate that CFTR influences cell-to-cell coupling mediated by Cx45 channels.
Fil: Kotsias, Basilio Aristides. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Médicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Médicas; Argentina
Fil: Peracchia, C.. University of Rochester School of Medicine; Estados Unidos - Materia
-
CELL COMMUNICATION
CFTR
CHANNEL GATING
CHLORIDE CHANNELS
CONNEXINS
GAP JUNCTIONS
XENOPUS OOCYTES - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/151033
Ver los metadatos del registro completo
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Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytesKotsias, Basilio AristidesPeracchia, C.CELL COMMUNICATIONCFTRCHANNEL GATINGCHLORIDE CHANNELSCONNEXINSGAP JUNCTIONSXENOPUS OOCYTEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride (Cl−) channel known to influence the function of other channels, including connexin channels. To further study potential functional interactions between CFTR and gap junction channels, we have co-expressed CFTR and connexin45 (Cx45) in Xenopus oocytes and monitored junctional conductance and voltage sensitivity by dual voltage clamp electrophysiology. In single oocytes expressing CFTR, an increase in cAMP caused by forskolin application induced a Cl− current and increased membrane conductance; application of diphenylamine carboxylic acid (CFTR blocker) readily blocked the Cl− current. With co-expression of CFTR and Cx45, application of forskolin to paired oocytes induced a typical outward current and increased junctional conductance (Gj). In addition, the presence of CFTR reduced the transjunctional voltage sensitivity of Cx45 channels without affecting the kinetics of junctional current inactivation. The drop in voltage sensitivity was further enhanced by forskolin application. The data indicate that CFTR influences cell-to-cell coupling mediated by Cx45 channels.Fil: Kotsias, Basilio Aristides. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Médicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Médicas; ArgentinaFil: Peracchia, C.. University of Rochester School of Medicine; Estados UnidosSpringer2005-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/151033Kotsias, Basilio Aristides; Peracchia, C.; Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes; Springer; Journal of Membrane Biology; 203; 3; 12-2005; 143-1500022-2631CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s00232-005-0739-6info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00232-005-0739-6info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:55:50Zoai:ri.conicet.gov.ar:11336/151033instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:55:50.689CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes |
title |
Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes |
spellingShingle |
Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes Kotsias, Basilio Aristides CELL COMMUNICATION CFTR CHANNEL GATING CHLORIDE CHANNELS CONNEXINS GAP JUNCTIONS XENOPUS OOCYTES |
title_short |
Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes |
title_full |
Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes |
title_fullStr |
Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes |
title_full_unstemmed |
Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes |
title_sort |
Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes |
dc.creator.none.fl_str_mv |
Kotsias, Basilio Aristides Peracchia, C. |
author |
Kotsias, Basilio Aristides |
author_facet |
Kotsias, Basilio Aristides Peracchia, C. |
author_role |
author |
author2 |
Peracchia, C. |
author2_role |
author |
dc.subject.none.fl_str_mv |
CELL COMMUNICATION CFTR CHANNEL GATING CHLORIDE CHANNELS CONNEXINS GAP JUNCTIONS XENOPUS OOCYTES |
topic |
CELL COMMUNICATION CFTR CHANNEL GATING CHLORIDE CHANNELS CONNEXINS GAP JUNCTIONS XENOPUS OOCYTES |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride (Cl−) channel known to influence the function of other channels, including connexin channels. To further study potential functional interactions between CFTR and gap junction channels, we have co-expressed CFTR and connexin45 (Cx45) in Xenopus oocytes and monitored junctional conductance and voltage sensitivity by dual voltage clamp electrophysiology. In single oocytes expressing CFTR, an increase in cAMP caused by forskolin application induced a Cl− current and increased membrane conductance; application of diphenylamine carboxylic acid (CFTR blocker) readily blocked the Cl− current. With co-expression of CFTR and Cx45, application of forskolin to paired oocytes induced a typical outward current and increased junctional conductance (Gj). In addition, the presence of CFTR reduced the transjunctional voltage sensitivity of Cx45 channels without affecting the kinetics of junctional current inactivation. The drop in voltage sensitivity was further enhanced by forskolin application. The data indicate that CFTR influences cell-to-cell coupling mediated by Cx45 channels. Fil: Kotsias, Basilio Aristides. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Médicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Médicas; Argentina Fil: Peracchia, C.. University of Rochester School of Medicine; Estados Unidos |
description |
The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride (Cl−) channel known to influence the function of other channels, including connexin channels. To further study potential functional interactions between CFTR and gap junction channels, we have co-expressed CFTR and connexin45 (Cx45) in Xenopus oocytes and monitored junctional conductance and voltage sensitivity by dual voltage clamp electrophysiology. In single oocytes expressing CFTR, an increase in cAMP caused by forskolin application induced a Cl− current and increased membrane conductance; application of diphenylamine carboxylic acid (CFTR blocker) readily blocked the Cl− current. With co-expression of CFTR and Cx45, application of forskolin to paired oocytes induced a typical outward current and increased junctional conductance (Gj). In addition, the presence of CFTR reduced the transjunctional voltage sensitivity of Cx45 channels without affecting the kinetics of junctional current inactivation. The drop in voltage sensitivity was further enhanced by forskolin application. The data indicate that CFTR influences cell-to-cell coupling mediated by Cx45 channels. |
publishDate |
2005 |
dc.date.none.fl_str_mv |
2005-12 |
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 |
http://hdl.handle.net/11336/151033 Kotsias, Basilio Aristides; Peracchia, C.; Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes; Springer; Journal of Membrane Biology; 203; 3; 12-2005; 143-150 0022-2631 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/151033 |
identifier_str_mv |
Kotsias, Basilio Aristides; Peracchia, C.; Functional interaction between CFTR and Cx45 gap junction channels expressed in oocytes; Springer; Journal of Membrane Biology; 203; 3; 12-2005; 143-150 0022-2631 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1007/s00232-005-0739-6 info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00232-005-0739-6 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Springer |
publisher.none.fl_str_mv |
Springer |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.070432 |