Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1
- Autores
- Marginedas Freixa, Irene; Alvarez, Cora Lilia; Moras, Martina; Leal Denis, Maria Florencia; Hattab, Claude; Halle, François; Bihel, Frédéric; Mouro Chanteloup, Isabelle; Lefevre, Sophie Denise; Le Van Kim, Caroline; Schwarzbaum, Pablo Julio; Ostuni, Mariano
- Año de publicación
- 2018
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- We previously demonstrated that the translocase protein TSPO2 together with the voltage-dependentanion channel (VDAC) and adenine nucleotide transporter (ANT) were involved in a membrane transportcomplex in human red blood cells (RBCs). Because VDAC was proposed as a channel mediating ATPrelease in RBCs, we used TSPO ligands together with VDAC and ANT inhibitors to test this hypothesis.ATP release was activated by TSPO ligands, and blocked by inhibitors of VDAC and ANT, while it wasinsensitive to pannexin-1 blockers. TSPO ligand increased extracellular ATP (ATPe) concentration by 24?59% over the basal values, displaying an acute increase in [ATPe] to a maximal value, which remainedconstant thereafter. ATPe kinetics were compatible with VDAC mediating a fast but transient ATPefflux. ATP release was strongly inhibited by PKC and PKA inhibitors as well as by depleting intracellularcAMP or extracellular Ca2+, suggesting a mechanism involving protein kinases. TSPO ligands favouredVDAC polymerization yielding significantly higher densities of oligomeric bands than in unstimulatedcells. Polymerization was partially inhibited by decreasing Ca2+ and cAMP contents. The present resultsshow that TSPO ligands induce polymerization of VDAC, coupled to activation of ATP release by asupramolecular complex involving VDAC, TSPO2 and ANT.
Fil: Marginedas Freixa, Irene. Université Paris Diderot - Paris 7; Francia. Institut National de la Transfusion Sanguine; . Université de la Réunion; Francia. Université des Antilles; Francia
Fil: Alvarez, Cora Lilia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Moras, Martina. Institut National de la Transfusion Sanguine; . Université des Antilles; Francia. Université Paris Diderot - Paris 7; Francia. Université de la Réunion; Francia
Fil: Leal Denis, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica. Cátedra de Química Analítica; Argentina
Fil: Hattab, Claude. Université de la Réunion; Francia. Université Paris Diderot - Paris 7; Francia. Université des Antilles; Francia. Institut National de la Transfusion Sanguine;
Fil: Halle, François. University of Strasbourg; Francia
Fil: Bihel, Frédéric. Université de Strasbourg; Francia
Fil: Mouro Chanteloup, Isabelle. Université des Antilles; Francia. Institut National de la Transfusion Sanguine; . Université de la Réunion; Francia. Université Paris Diderot - Paris 7; Francia
Fil: Lefevre, Sophie Denise. Université Paris Diderot - Paris 7; Francia. Université des Antilles; Francia. Université de la Réunion; Francia. Institut National de la Transfusion Sanguine;
Fil: Le Van Kim, Caroline. Université des Antilles; Francia. Université de la Réunion; Francia. Institut National de la Transfusion Sanguine; . Université Paris Diderot - Paris 7; Francia
Fil: Schwarzbaum, Pablo Julio. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Ostuni, Mariano. Université Paris Diderot - Paris 7; Francia. Université de la Réunion; Francia. Université des Antilles; Francia. Institut National de la Transfusion Sanguine; - Materia
-
EXTRACELLULAR ATP
NUCLEOTIDASES
VDAC
PANNEXIN 1 - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/102752
Ver los metadatos del registro completo
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Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1Marginedas Freixa, IreneAlvarez, Cora LiliaMoras, MartinaLeal Denis, Maria FlorenciaHattab, ClaudeHalle, FrançoisBihel, FrédéricMouro Chanteloup, IsabelleLefevre, Sophie DeniseLe Van Kim, CarolineSchwarzbaum, Pablo JulioOstuni, MarianoEXTRACELLULAR ATPNUCLEOTIDASESVDACPANNEXIN 1https://purl.org/becyt/ford/3.5https://purl.org/becyt/ford/3We previously demonstrated that the translocase protein TSPO2 together with the voltage-dependentanion channel (VDAC) and adenine nucleotide transporter (ANT) were involved in a membrane transportcomplex in human red blood cells (RBCs). Because VDAC was proposed as a channel mediating ATPrelease in RBCs, we used TSPO ligands together with VDAC and ANT inhibitors to test this hypothesis.ATP release was activated by TSPO ligands, and blocked by inhibitors of VDAC and ANT, while it wasinsensitive to pannexin-1 blockers. TSPO ligand increased extracellular ATP (ATPe) concentration by 24?59% over the basal values, displaying an acute increase in [ATPe] to a maximal value, which remainedconstant thereafter. ATPe kinetics were compatible with VDAC mediating a fast but transient ATPefflux. ATP release was strongly inhibited by PKC and PKA inhibitors as well as by depleting intracellularcAMP or extracellular Ca2+, suggesting a mechanism involving protein kinases. TSPO ligands favouredVDAC polymerization yielding significantly higher densities of oligomeric bands than in unstimulatedcells. Polymerization was partially inhibited by decreasing Ca2+ and cAMP contents. The present resultsshow that TSPO ligands induce polymerization of VDAC, coupled to activation of ATP release by asupramolecular complex involving VDAC, TSPO2 and ANT.Fil: Marginedas Freixa, Irene. Université Paris Diderot - Paris 7; Francia. Institut National de la Transfusion Sanguine; . Université de la Réunion; Francia. Université des Antilles; FranciaFil: Alvarez, Cora Lilia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Moras, Martina. Institut National de la Transfusion Sanguine; . Université des Antilles; Francia. Université Paris Diderot - Paris 7; Francia. Université de la Réunion; FranciaFil: Leal Denis, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica. Cátedra de Química Analítica; ArgentinaFil: Hattab, Claude. Université de la Réunion; Francia. Université Paris Diderot - Paris 7; Francia. Université des Antilles; Francia. Institut National de la Transfusion Sanguine; Fil: Halle, François. University of Strasbourg; FranciaFil: Bihel, Frédéric. Université de Strasbourg; FranciaFil: Mouro Chanteloup, Isabelle. Université des Antilles; Francia. Institut National de la Transfusion Sanguine; . Université de la Réunion; Francia. Université Paris Diderot - Paris 7; FranciaFil: Lefevre, Sophie Denise. Université Paris Diderot - Paris 7; Francia. Université des Antilles; Francia. Université de la Réunion; Francia. Institut National de la Transfusion Sanguine; Fil: Le Van Kim, Caroline. Université des Antilles; Francia. Université de la Réunion; Francia. Institut National de la Transfusion Sanguine; . Université Paris Diderot - Paris 7; FranciaFil: Schwarzbaum, Pablo Julio. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Ostuni, Mariano. Université Paris Diderot - Paris 7; Francia. Université de la Réunion; Francia. Université des Antilles; Francia. Institut National de la Transfusion Sanguine; Springer Nature2018-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/102752Marginedas Freixa, Irene; Alvarez, Cora Lilia; Moras, Martina; Leal Denis, Maria Florencia; Hattab, Claude; et al.; Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1; Springer Nature; Scientific Reports; 8; 1; 12-2018; 1-132045-2322CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/s41598-018-29885-7info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-018-29885-7info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:10:17Zoai:ri.conicet.gov.ar:11336/102752instacron: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 10:10:18.288CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1 |
title |
Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1 |
spellingShingle |
Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1 Marginedas Freixa, Irene EXTRACELLULAR ATP NUCLEOTIDASES VDAC PANNEXIN 1 |
title_short |
Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1 |
title_full |
Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1 |
title_fullStr |
Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1 |
title_full_unstemmed |
Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1 |
title_sort |
Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1 |
dc.creator.none.fl_str_mv |
Marginedas Freixa, Irene Alvarez, Cora Lilia Moras, Martina Leal Denis, Maria Florencia Hattab, Claude Halle, François Bihel, Frédéric Mouro Chanteloup, Isabelle Lefevre, Sophie Denise Le Van Kim, Caroline Schwarzbaum, Pablo Julio Ostuni, Mariano |
author |
Marginedas Freixa, Irene |
author_facet |
Marginedas Freixa, Irene Alvarez, Cora Lilia Moras, Martina Leal Denis, Maria Florencia Hattab, Claude Halle, François Bihel, Frédéric Mouro Chanteloup, Isabelle Lefevre, Sophie Denise Le Van Kim, Caroline Schwarzbaum, Pablo Julio Ostuni, Mariano |
author_role |
author |
author2 |
Alvarez, Cora Lilia Moras, Martina Leal Denis, Maria Florencia Hattab, Claude Halle, François Bihel, Frédéric Mouro Chanteloup, Isabelle Lefevre, Sophie Denise Le Van Kim, Caroline Schwarzbaum, Pablo Julio Ostuni, Mariano |
author2_role |
author author author author author author author author author author author |
dc.subject.none.fl_str_mv |
EXTRACELLULAR ATP NUCLEOTIDASES VDAC PANNEXIN 1 |
topic |
EXTRACELLULAR ATP NUCLEOTIDASES VDAC PANNEXIN 1 |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/3.5 https://purl.org/becyt/ford/3 |
dc.description.none.fl_txt_mv |
We previously demonstrated that the translocase protein TSPO2 together with the voltage-dependentanion channel (VDAC) and adenine nucleotide transporter (ANT) were involved in a membrane transportcomplex in human red blood cells (RBCs). Because VDAC was proposed as a channel mediating ATPrelease in RBCs, we used TSPO ligands together with VDAC and ANT inhibitors to test this hypothesis.ATP release was activated by TSPO ligands, and blocked by inhibitors of VDAC and ANT, while it wasinsensitive to pannexin-1 blockers. TSPO ligand increased extracellular ATP (ATPe) concentration by 24?59% over the basal values, displaying an acute increase in [ATPe] to a maximal value, which remainedconstant thereafter. ATPe kinetics were compatible with VDAC mediating a fast but transient ATPefflux. ATP release was strongly inhibited by PKC and PKA inhibitors as well as by depleting intracellularcAMP or extracellular Ca2+, suggesting a mechanism involving protein kinases. TSPO ligands favouredVDAC polymerization yielding significantly higher densities of oligomeric bands than in unstimulatedcells. Polymerization was partially inhibited by decreasing Ca2+ and cAMP contents. The present resultsshow that TSPO ligands induce polymerization of VDAC, coupled to activation of ATP release by asupramolecular complex involving VDAC, TSPO2 and ANT. Fil: Marginedas Freixa, Irene. Université Paris Diderot - Paris 7; Francia. Institut National de la Transfusion Sanguine; . Université de la Réunion; Francia. Université des Antilles; Francia Fil: Alvarez, Cora Lilia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina Fil: Moras, Martina. Institut National de la Transfusion Sanguine; . Université des Antilles; Francia. Université Paris Diderot - Paris 7; Francia. Université de la Réunion; Francia Fil: Leal Denis, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica. Cátedra de Química Analítica; Argentina Fil: Hattab, Claude. Université de la Réunion; Francia. Université Paris Diderot - Paris 7; Francia. Université des Antilles; Francia. Institut National de la Transfusion Sanguine; Fil: Halle, François. University of Strasbourg; Francia Fil: Bihel, Frédéric. Université de Strasbourg; Francia Fil: Mouro Chanteloup, Isabelle. Université des Antilles; Francia. Institut National de la Transfusion Sanguine; . Université de la Réunion; Francia. Université Paris Diderot - Paris 7; Francia Fil: Lefevre, Sophie Denise. Université Paris Diderot - Paris 7; Francia. Université des Antilles; Francia. Université de la Réunion; Francia. Institut National de la Transfusion Sanguine; Fil: Le Van Kim, Caroline. Université des Antilles; Francia. Université de la Réunion; Francia. Institut National de la Transfusion Sanguine; . Université Paris Diderot - Paris 7; Francia Fil: Schwarzbaum, Pablo Julio. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina Fil: Ostuni, Mariano. Université Paris Diderot - Paris 7; Francia. Université de la Réunion; Francia. Université des Antilles; Francia. Institut National de la Transfusion Sanguine; |
description |
We previously demonstrated that the translocase protein TSPO2 together with the voltage-dependentanion channel (VDAC) and adenine nucleotide transporter (ANT) were involved in a membrane transportcomplex in human red blood cells (RBCs). Because VDAC was proposed as a channel mediating ATPrelease in RBCs, we used TSPO ligands together with VDAC and ANT inhibitors to test this hypothesis.ATP release was activated by TSPO ligands, and blocked by inhibitors of VDAC and ANT, while it wasinsensitive to pannexin-1 blockers. TSPO ligand increased extracellular ATP (ATPe) concentration by 24?59% over the basal values, displaying an acute increase in [ATPe] to a maximal value, which remainedconstant thereafter. ATPe kinetics were compatible with VDAC mediating a fast but transient ATPefflux. ATP release was strongly inhibited by PKC and PKA inhibitors as well as by depleting intracellularcAMP or extracellular Ca2+, suggesting a mechanism involving protein kinases. TSPO ligands favouredVDAC polymerization yielding significantly higher densities of oligomeric bands than in unstimulatedcells. Polymerization was partially inhibited by decreasing Ca2+ and cAMP contents. The present resultsshow that TSPO ligands induce polymerization of VDAC, coupled to activation of ATP release by asupramolecular complex involving VDAC, TSPO2 and ANT. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-12 |
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/11336/102752 Marginedas Freixa, Irene; Alvarez, Cora Lilia; Moras, Martina; Leal Denis, Maria Florencia; Hattab, Claude; et al.; Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1; Springer Nature; Scientific Reports; 8; 1; 12-2018; 1-13 2045-2322 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/102752 |
identifier_str_mv |
Marginedas Freixa, Irene; Alvarez, Cora Lilia; Moras, Martina; Leal Denis, Maria Florencia; Hattab, Claude; et al.; Human erythrocytes release ATP by a novel pathway involving VDAC oligomerization independent of pannexin-1; Springer Nature; Scientific Reports; 8; 1; 12-2018; 1-13 2045-2322 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/s41598-018-29885-7 info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-018-29885-7 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Springer Nature |
publisher.none.fl_str_mv |
Springer Nature |
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) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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1844613990723878912 |
score |
13.070432 |