The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump

Autores
de Tezanos Pinto, Felicitas; Corradi, Gerardo Raul; Adamo, Hugo Pedro
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The human gene ATP13A2 has been proposed to code for an ATP powered ion transporter of the P5B subfamily. Mutations of the human gene ATP13A2 were found to underlie an autosomal recessive form of early-onset parkinsonism (PD) with pyramidal degeneration and dementia. The ion transported by the ATP13A2 pump is not known, but several studies have shown that the P5-ATPases influence the homeostasis of intracellular Ca2+, and thus it has been suggested that they transport Ca2+. In order to evaluate this possibility Chinese hamster ovary (CHO) cells stably expressing the human ATP13A2 protein have been obtained and the Ca2+ transport activity of ATP13A2 was assessed by measuring the ATP-dependent uptake of Ca2+ into microsomal vesicles. As a positive control vesicles containing the human plasma membrane Ca2+ pump (PMCA) were used. No significant differences were found between vesicles containing the ATP13A2 protein and the control. Moreover, Ca2+ was unable to induce the formation of the P-ATPase acylphosphate intermediate in vesicles containing the expressed ATP13A2. These results favor the idea that the ATP13A2 does not transport Ca2+.
Fil: de Tezanos Pinto, Felicitas. 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: Corradi, Gerardo Raul. 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: Adamo, Hugo Pedro. 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
Materia
P5B-ATPase
ATP13A2
Ca2+ Transporting
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:11336/147627
Acceder
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network_name_str CONICET Digital (CONICET)
spelling The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pumpde Tezanos Pinto, FelicitasCorradi, Gerardo RaulAdamo, Hugo PedroP5B-ATPaseATP13A2Ca2+ Transportinghttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The human gene ATP13A2 has been proposed to code for an ATP powered ion transporter of the P5B subfamily. Mutations of the human gene ATP13A2 were found to underlie an autosomal recessive form of early-onset parkinsonism (PD) with pyramidal degeneration and dementia. The ion transported by the ATP13A2 pump is not known, but several studies have shown that the P5-ATPases influence the homeostasis of intracellular Ca2+, and thus it has been suggested that they transport Ca2+. In order to evaluate this possibility Chinese hamster ovary (CHO) cells stably expressing the human ATP13A2 protein have been obtained and the Ca2+ transport activity of ATP13A2 was assessed by measuring the ATP-dependent uptake of Ca2+ into microsomal vesicles. As a positive control vesicles containing the human plasma membrane Ca2+ pump (PMCA) were used. No significant differences were found between vesicles containing the ATP13A2 protein and the control. Moreover, Ca2+ was unable to induce the formation of the P-ATPase acylphosphate intermediate in vesicles containing the expressed ATP13A2. These results favor the idea that the ATP13A2 does not transport Ca2+.Fil: de Tezanos Pinto, Felicitas. 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: Corradi, Gerardo Raul. 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: Adamo, Hugo Pedro. 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; ArgentinaDavid Publishing Company2011-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/147627de Tezanos Pinto, Felicitas; Corradi, Gerardo Raul; Adamo, Hugo Pedro; The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump; David Publishing Company; Journal of Life Sciences; 5; 33; 1-2011; 1-101934-7391CONICET DigitalCONICETenginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T09:43:43Zoai:ri.conicet.gov.ar:11336/147627instacron: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:34982025-11-12 09:43:44.104CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump
title The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump
spellingShingle The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump
de Tezanos Pinto, Felicitas
P5B-ATPase
ATP13A2
Ca2+ Transporting
title_short The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump
title_full The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump
title_fullStr The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump
title_full_unstemmed The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump
title_sort The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump
dc.creator.none.fl_str_mv de Tezanos Pinto, Felicitas
Corradi, Gerardo Raul
Adamo, Hugo Pedro
author de Tezanos Pinto, Felicitas
author_facet de Tezanos Pinto, Felicitas
Corradi, Gerardo Raul
Adamo, Hugo Pedro
author_role author
author2 Corradi, Gerardo Raul
Adamo, Hugo Pedro
author2_role author
author
dc.subject.none.fl_str_mv P5B-ATPase
ATP13A2
Ca2+ Transporting
topic P5B-ATPase
ATP13A2
Ca2+ Transporting
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 human gene ATP13A2 has been proposed to code for an ATP powered ion transporter of the P5B subfamily. Mutations of the human gene ATP13A2 were found to underlie an autosomal recessive form of early-onset parkinsonism (PD) with pyramidal degeneration and dementia. The ion transported by the ATP13A2 pump is not known, but several studies have shown that the P5-ATPases influence the homeostasis of intracellular Ca2+, and thus it has been suggested that they transport Ca2+. In order to evaluate this possibility Chinese hamster ovary (CHO) cells stably expressing the human ATP13A2 protein have been obtained and the Ca2+ transport activity of ATP13A2 was assessed by measuring the ATP-dependent uptake of Ca2+ into microsomal vesicles. As a positive control vesicles containing the human plasma membrane Ca2+ pump (PMCA) were used. No significant differences were found between vesicles containing the ATP13A2 protein and the control. Moreover, Ca2+ was unable to induce the formation of the P-ATPase acylphosphate intermediate in vesicles containing the expressed ATP13A2. These results favor the idea that the ATP13A2 does not transport Ca2+.
Fil: de Tezanos Pinto, Felicitas. 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: Corradi, Gerardo Raul. 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: Adamo, Hugo Pedro. 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
description The human gene ATP13A2 has been proposed to code for an ATP powered ion transporter of the P5B subfamily. Mutations of the human gene ATP13A2 were found to underlie an autosomal recessive form of early-onset parkinsonism (PD) with pyramidal degeneration and dementia. The ion transported by the ATP13A2 pump is not known, but several studies have shown that the P5-ATPases influence the homeostasis of intracellular Ca2+, and thus it has been suggested that they transport Ca2+. In order to evaluate this possibility Chinese hamster ovary (CHO) cells stably expressing the human ATP13A2 protein have been obtained and the Ca2+ transport activity of ATP13A2 was assessed by measuring the ATP-dependent uptake of Ca2+ into microsomal vesicles. As a positive control vesicles containing the human plasma membrane Ca2+ pump (PMCA) were used. No significant differences were found between vesicles containing the ATP13A2 protein and the control. Moreover, Ca2+ was unable to induce the formation of the P-ATPase acylphosphate intermediate in vesicles containing the expressed ATP13A2. These results favor the idea that the ATP13A2 does not transport Ca2+.
publishDate 2011
dc.date.none.fl_str_mv 2011-01
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/11336/147627
de Tezanos Pinto, Felicitas; Corradi, Gerardo Raul; Adamo, Hugo Pedro; The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump; David Publishing Company; Journal of Life Sciences; 5; 33; 1-2011; 1-10
1934-7391
CONICET Digital
CONICET
url http://hdl.handle.net/11336/147627
identifier_str_mv de Tezanos Pinto, Felicitas; Corradi, Gerardo Raul; Adamo, Hugo Pedro; The Human P5B-ATPase ATP13A2 is not a Ca2+ Transporting Pump; David Publishing Company; Journal of Life Sciences; 5; 33; 1-2011; 1-10
1934-7391
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv David Publishing Company
publisher.none.fl_str_mv David Publishing Company
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 12.976206

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