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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/102752

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network_name_str CONICET Digital (CONICET)
spelling 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
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info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-018-29885-7
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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/
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application/pdf
application/pdf
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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)
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