Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations

Autores
Alleva, Karina Edith; Niemietz, Christa M.; Sutka, Moira Romina; Maurel, Christophe; Parisi, Mario Nestor; Amodeo, Gabriela
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Plasma membrane vesicles isolated by two-phase partitioning from the storage root of Beta vulgaris show atypically high water permeability that is equivalent only to those reported for active aquaporins in tonoplast or animal red cells (Pf5542 lm s21 ). The values were determined from the shrinking kinetics measured by stopped-flow light scattering. This high Pf was only partially inhibited by mercury (HgCl2) but showed low activation energy (Ea) consistent with water permeation through water channels. To study short-term regulation of water transport that could be the result of channel gating, the effects of pH, divalent cations, and protection against dephosphorylation were tested. The high Pf observed at pH 8.3 was dramatically reduced by medium acidification. Moreover, intravesicular acidification (corresponding to the cytoplasmic face of the membrane) shut down the aquaporins. De-phosphorylation was discounted as a regulatory mechanism in this preparation. On the other hand, among divalent cations, only calcium showed a clear effect on aquaporin activity, with two distinct ranges of sensitivity to free Ca21 concentration (pCa 8 and pCa 4). Since the normal cytoplasmic free Ca21 sits between these ranges it allows for the possibility of changes in Ca21 to finely up- or down-regulate water channel activity. The calcium effect is predominantly on the cytoplasmic face, and inhibition corresponds to an increase in the activation energy for water transport. In conclusion, these findings establish both cytoplasmic pH and Ca21 as important regulatory factors involved in aquaporin gating.
Fil: Alleva, Karina Edith. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Niemietz, Christa M.. University of Adelaide; Australia
Fil: Sutka, Moira Romina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Maurel, Christophe. Institut National de la Recherche Agronomique; Francia
Fil: Parisi, Mario Nestor. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Amodeo, Gabriela. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Aquaporin
Water Permeability
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/16650
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/16650
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrationsAlleva, Karina EdithNiemietz, Christa M.Sutka, Moira RominaMaurel, ChristopheParisi, Mario NestorAmodeo, GabrielaAquaporinWater Permeabilityhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Plasma membrane vesicles isolated by two-phase partitioning from the storage root of Beta vulgaris show atypically high water permeability that is equivalent only to those reported for active aquaporins in tonoplast or animal red cells (Pf5542 lm s21 ). The values were determined from the shrinking kinetics measured by stopped-flow light scattering. This high Pf was only partially inhibited by mercury (HgCl2) but showed low activation energy (Ea) consistent with water permeation through water channels. To study short-term regulation of water transport that could be the result of channel gating, the effects of pH, divalent cations, and protection against dephosphorylation were tested. The high Pf observed at pH 8.3 was dramatically reduced by medium acidification. Moreover, intravesicular acidification (corresponding to the cytoplasmic face of the membrane) shut down the aquaporins. De-phosphorylation was discounted as a regulatory mechanism in this preparation. On the other hand, among divalent cations, only calcium showed a clear effect on aquaporin activity, with two distinct ranges of sensitivity to free Ca21 concentration (pCa 8 and pCa 4). Since the normal cytoplasmic free Ca21 sits between these ranges it allows for the possibility of changes in Ca21 to finely up- or down-regulate water channel activity. The calcium effect is predominantly on the cytoplasmic face, and inhibition corresponds to an increase in the activation energy for water transport. In conclusion, these findings establish both cytoplasmic pH and Ca21 as important regulatory factors involved in aquaporin gating.Fil: Alleva, Karina Edith. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Niemietz, Christa M.. University of Adelaide; AustraliaFil: Sutka, Moira Romina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Maurel, Christophe. Institut National de la Recherche Agronomique; FranciaFil: Parisi, Mario Nestor. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Amodeo, Gabriela. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaOxford University Press2006-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/16650Alleva, Karina Edith; Niemietz, Christa M.; Sutka, Moira Romina; Maurel, Christophe; Parisi, Mario Nestor; et al.; Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations; Oxford University Press; Journal Of Experimental Botany; 57; 3; 2-2006; 609-6210022-0957enginfo:eu-repo/semantics/altIdentifier/doi/10.1093/jxb/erj046info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jxb/article-lookup/doi/10.1093/jxb/erj046info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:06:56Zoai:ri.conicet.gov.ar:11336/16650instacron: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:34982025-10-22 12:06:56.553CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations
title Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations
spellingShingle Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations
Alleva, Karina Edith
Aquaporin
Water Permeability
title_short Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations
title_full Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations
title_fullStr Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations
title_full_unstemmed Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations
title_sort Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations
dc.creator.none.fl_str_mv Alleva, Karina Edith
Niemietz, Christa M.
Sutka, Moira Romina
Maurel, Christophe
Parisi, Mario Nestor
Amodeo, Gabriela
author Alleva, Karina Edith
author_facet Alleva, Karina Edith
Niemietz, Christa M.
Sutka, Moira Romina
Maurel, Christophe
Parisi, Mario Nestor
Amodeo, Gabriela
author_role author
author2 Niemietz, Christa M.
Sutka, Moira Romina
Maurel, Christophe
Parisi, Mario Nestor
Amodeo, Gabriela
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Aquaporin
Water Permeability
topic Aquaporin
Water Permeability
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Plasma membrane vesicles isolated by two-phase partitioning from the storage root of Beta vulgaris show atypically high water permeability that is equivalent only to those reported for active aquaporins in tonoplast or animal red cells (Pf5542 lm s21 ). The values were determined from the shrinking kinetics measured by stopped-flow light scattering. This high Pf was only partially inhibited by mercury (HgCl2) but showed low activation energy (Ea) consistent with water permeation through water channels. To study short-term regulation of water transport that could be the result of channel gating, the effects of pH, divalent cations, and protection against dephosphorylation were tested. The high Pf observed at pH 8.3 was dramatically reduced by medium acidification. Moreover, intravesicular acidification (corresponding to the cytoplasmic face of the membrane) shut down the aquaporins. De-phosphorylation was discounted as a regulatory mechanism in this preparation. On the other hand, among divalent cations, only calcium showed a clear effect on aquaporin activity, with two distinct ranges of sensitivity to free Ca21 concentration (pCa 8 and pCa 4). Since the normal cytoplasmic free Ca21 sits between these ranges it allows for the possibility of changes in Ca21 to finely up- or down-regulate water channel activity. The calcium effect is predominantly on the cytoplasmic face, and inhibition corresponds to an increase in the activation energy for water transport. In conclusion, these findings establish both cytoplasmic pH and Ca21 as important regulatory factors involved in aquaporin gating.
Fil: Alleva, Karina Edith. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Niemietz, Christa M.. University of Adelaide; Australia
Fil: Sutka, Moira Romina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Maurel, Christophe. Institut National de la Recherche Agronomique; Francia
Fil: Parisi, Mario Nestor. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Amodeo, Gabriela. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Plasma membrane vesicles isolated by two-phase partitioning from the storage root of Beta vulgaris show atypically high water permeability that is equivalent only to those reported for active aquaporins in tonoplast or animal red cells (Pf5542 lm s21 ). The values were determined from the shrinking kinetics measured by stopped-flow light scattering. This high Pf was only partially inhibited by mercury (HgCl2) but showed low activation energy (Ea) consistent with water permeation through water channels. To study short-term regulation of water transport that could be the result of channel gating, the effects of pH, divalent cations, and protection against dephosphorylation were tested. The high Pf observed at pH 8.3 was dramatically reduced by medium acidification. Moreover, intravesicular acidification (corresponding to the cytoplasmic face of the membrane) shut down the aquaporins. De-phosphorylation was discounted as a regulatory mechanism in this preparation. On the other hand, among divalent cations, only calcium showed a clear effect on aquaporin activity, with two distinct ranges of sensitivity to free Ca21 concentration (pCa 8 and pCa 4). Since the normal cytoplasmic free Ca21 sits between these ranges it allows for the possibility of changes in Ca21 to finely up- or down-regulate water channel activity. The calcium effect is predominantly on the cytoplasmic face, and inhibition corresponds to an increase in the activation energy for water transport. In conclusion, these findings establish both cytoplasmic pH and Ca21 as important regulatory factors involved in aquaporin gating.
publishDate 2006
dc.date.none.fl_str_mv 2006-02
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/11336/16650
Alleva, Karina Edith; Niemietz, Christa M.; Sutka, Moira Romina; Maurel, Christophe; Parisi, Mario Nestor; et al.; Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations; Oxford University Press; Journal Of Experimental Botany; 57; 3; 2-2006; 609-621
0022-0957
url http://hdl.handle.net/11336/16650
identifier_str_mv Alleva, Karina Edith; Niemietz, Christa M.; Sutka, Moira Romina; Maurel, Christophe; Parisi, Mario Nestor; et al.; Plasma membrane of Beta vulgaris storage root shows high water channel activity regulated by cytoplasmic pH and a dual range of calcium concentrations; Oxford University Press; Journal Of Experimental Botany; 57; 3; 2-2006; 609-621
0022-0957
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1093/jxb/erj046
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jxb/article-lookup/doi/10.1093/jxb/erj046
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 Oxford University Press
publisher.none.fl_str_mv Oxford University Press
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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score 12.982451

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