Physical and functional interaction of carbonic anhydrases and nbce1 Na+/HCO3- cotransporter in the heart : The metabolon revisited

Autores
Álvarez, Bernardo Víctor; Aiello, Ernesto Alejandro
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
To allow the control of their intracellular pH (pHi) and bicarbonate (HCO3 - ) levels, cells express HCO3 - transport proteins (NBC) that rapidly and selectively move HCO3 - across the plasma membrane. In the heart electroneutral NBCn1 and electrogenic NBCe1 Na+ /HCO3 - cotransporters facilitate the transmembrane movement of HCO3 - ions into cardiomyocytes, as a response to acid loading. NBCe1 associates with carbonic anhydrases (CA), the enzymes that catalyze the reversible conversion of CO2 to HCO3 - , to form a transport metabolon, a weakly associated complex of sequential metabolic enzymes. NBCe1 physically/functionally interact with the isoforms II, IV, and IX of CA, to increase the HCO3 - flux through cell membranes. NBCe1 and CAs interaction occurs in different cellular compartments in the heart muscle. Physiologically, the NBCe1/CA complex could contribute to the removal of H+ ions accumulated as the result of the contractile activity of the cardiac muscle cell, and this process may occur at the surface sarcolemma (CAII-NBCe1-CAIV complex) or at the ttubule (CAII-NBCe1-CAIX complex) of the cardiomyocyte. Pathologically, upregulation of the NBCe1/CA metabolon system upon ischemic/hypoxic conditions of the heart would favor the hypertrophic growth of the cardiac cells.
Centro de Investigaciones Cardiovasculares
Materia
Ciencias Médicas
NBC/CA complex
Metabolon
Heart
Bicarbonate
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/104654
Acceder
id SEDICI_029c35fc77d1695c8637cdfbd689c5f4
oai_identifier_str oai:sedici.unlp.edu.ar:10915/104654
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Physical and functional interaction of carbonic anhydrases and nbce1 Na+/HCO3- cotransporter in the heart : The metabolon revisitedÁlvarez, Bernardo VíctorAiello, Ernesto AlejandroCiencias MédicasNBC/CA complexMetabolonHeartBicarbonateTo allow the control of their intracellular pH (pHi) and bicarbonate (HCO3 - ) levels, cells express HCO3 - transport proteins (NBC) that rapidly and selectively move HCO3 - across the plasma membrane. In the heart electroneutral NBCn1 and electrogenic NBCe1 Na+ /HCO3 - cotransporters facilitate the transmembrane movement of HCO3 - ions into cardiomyocytes, as a response to acid loading. NBCe1 associates with carbonic anhydrases (CA), the enzymes that catalyze the reversible conversion of CO2 to HCO3 - , to form a transport metabolon, a weakly associated complex of sequential metabolic enzymes. NBCe1 physically/functionally interact with the isoforms II, IV, and IX of CA, to increase the HCO3 - flux through cell membranes. NBCe1 and CAs interaction occurs in different cellular compartments in the heart muscle. Physiologically, the NBCe1/CA complex could contribute to the removal of H+ ions accumulated as the result of the contractile activity of the cardiac muscle cell, and this process may occur at the surface sarcolemma (CAII-NBCe1-CAIV complex) or at the ttubule (CAII-NBCe1-CAIX complex) of the cardiomyocyte. Pathologically, upregulation of the NBCe1/CA metabolon system upon ischemic/hypoxic conditions of the heart would favor the hypertrophic growth of the cardiac cells.Centro de Investigaciones Cardiovasculares2012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf26-36http://sedici.unlp.edu.ar/handle/10915/104654enginfo:eu-repo/semantics/altIdentifier/url/http://hdl.handle.net/11336/60867info:eu-repo/semantics/altIdentifier/issn/1669-5410info:eu-repo/semantics/altIdentifier/hdl/11336/60867info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:22:43Zoai:sedici.unlp.edu.ar:10915/104654Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:22:44.108SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Physical and functional interaction of carbonic anhydrases and nbce1 Na+/HCO3- cotransporter in the heart : The metabolon revisited
title Physical and functional interaction of carbonic anhydrases and nbce1 Na+/HCO3- cotransporter in the heart : The metabolon revisited
spellingShingle Physical and functional interaction of carbonic anhydrases and nbce1 Na+/HCO3- cotransporter in the heart : The metabolon revisited
Álvarez, Bernardo Víctor
Ciencias Médicas
NBC/CA complex
Metabolon
Heart
Bicarbonate
title_short Physical and functional interaction of carbonic anhydrases and nbce1 Na+/HCO3- cotransporter in the heart : The metabolon revisited
title_full Physical and functional interaction of carbonic anhydrases and nbce1 Na+/HCO3- cotransporter in the heart : The metabolon revisited
title_fullStr Physical and functional interaction of carbonic anhydrases and nbce1 Na+/HCO3- cotransporter in the heart : The metabolon revisited
title_full_unstemmed Physical and functional interaction of carbonic anhydrases and nbce1 Na+/HCO3- cotransporter in the heart : The metabolon revisited
title_sort Physical and functional interaction of carbonic anhydrases and nbce1 Na+/HCO3- cotransporter in the heart : The metabolon revisited
dc.creator.none.fl_str_mv Álvarez, Bernardo Víctor
Aiello, Ernesto Alejandro
author Álvarez, Bernardo Víctor
author_facet Álvarez, Bernardo Víctor
Aiello, Ernesto Alejandro
author_role author
author2 Aiello, Ernesto Alejandro
author2_role author
dc.subject.none.fl_str_mv Ciencias Médicas
NBC/CA complex
Metabolon
Heart
Bicarbonate
topic Ciencias Médicas
NBC/CA complex
Metabolon
Heart
Bicarbonate
dc.description.none.fl_txt_mv To allow the control of their intracellular pH (pHi) and bicarbonate (HCO3 - ) levels, cells express HCO3 - transport proteins (NBC) that rapidly and selectively move HCO3 - across the plasma membrane. In the heart electroneutral NBCn1 and electrogenic NBCe1 Na+ /HCO3 - cotransporters facilitate the transmembrane movement of HCO3 - ions into cardiomyocytes, as a response to acid loading. NBCe1 associates with carbonic anhydrases (CA), the enzymes that catalyze the reversible conversion of CO2 to HCO3 - , to form a transport metabolon, a weakly associated complex of sequential metabolic enzymes. NBCe1 physically/functionally interact with the isoforms II, IV, and IX of CA, to increase the HCO3 - flux through cell membranes. NBCe1 and CAs interaction occurs in different cellular compartments in the heart muscle. Physiologically, the NBCe1/CA complex could contribute to the removal of H+ ions accumulated as the result of the contractile activity of the cardiac muscle cell, and this process may occur at the surface sarcolemma (CAII-NBCe1-CAIV complex) or at the ttubule (CAII-NBCe1-CAIX complex) of the cardiomyocyte. Pathologically, upregulation of the NBCe1/CA metabolon system upon ischemic/hypoxic conditions of the heart would favor the hypertrophic growth of the cardiac cells.
Centro de Investigaciones Cardiovasculares
description To allow the control of their intracellular pH (pHi) and bicarbonate (HCO3 - ) levels, cells express HCO3 - transport proteins (NBC) that rapidly and selectively move HCO3 - across the plasma membrane. In the heart electroneutral NBCn1 and electrogenic NBCe1 Na+ /HCO3 - cotransporters facilitate the transmembrane movement of HCO3 - ions into cardiomyocytes, as a response to acid loading. NBCe1 associates with carbonic anhydrases (CA), the enzymes that catalyze the reversible conversion of CO2 to HCO3 - , to form a transport metabolon, a weakly associated complex of sequential metabolic enzymes. NBCe1 physically/functionally interact with the isoforms II, IV, and IX of CA, to increase the HCO3 - flux through cell membranes. NBCe1 and CAs interaction occurs in different cellular compartments in the heart muscle. Physiologically, the NBCe1/CA complex could contribute to the removal of H+ ions accumulated as the result of the contractile activity of the cardiac muscle cell, and this process may occur at the surface sarcolemma (CAII-NBCe1-CAIV complex) or at the ttubule (CAII-NBCe1-CAIX complex) of the cardiomyocyte. Pathologically, upregulation of the NBCe1/CA metabolon system upon ischemic/hypoxic conditions of the heart would favor the hypertrophic growth of the cardiac cells.
publishDate 2012
dc.date.none.fl_str_mv 2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/104654
url http://sedici.unlp.edu.ar/handle/10915/104654
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://hdl.handle.net/11336/60867
info:eu-repo/semantics/altIdentifier/issn/1669-5410
info:eu-repo/semantics/altIdentifier/hdl/11336/60867
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
26-36
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.070432

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