Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology

© 2015 Elsevier B.V.. Ca<sup>2+</sup>-ATPases are plasma membrane and intracellular membrane transporters that use the energy of ATP hydrolysis to pump cytosolic Ca<sup>2+</sup> out of the cell (PMCA) or into internal stores. These pumps are the main high-affinity Ca<sup&g...

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Detalles Bibliográficos
Autores: Berrocal, María, Corbacho, Isaac, Vázquez-Hernández, María, Ávila, Jesús, Sepúlveda, M. Rosario, Mata, Ana M.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/139543
Acceso en línea:http://hdl.handle.net/10261/139543
Access Level:acceso abierto
Palabra clave:PMCA
Tau
Calcium
Aging
Alzheimer disease
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spelling Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathologyBerrocal, MaríaCorbacho, IsaacVázquez-Hernández, MaríaÁvila, JesúsSepúlveda, M. RosarioMata, Ana M.PMCATauCalciumAgingAlzheimer disease© 2015 Elsevier B.V.. Ca<sup>2+</sup>-ATPases are plasma membrane and intracellular membrane transporters that use the energy of ATP hydrolysis to pump cytosolic Ca<sup>2+</sup> out of the cell (PMCA) or into internal stores. These pumps are the main high-affinity Ca<sup>2+</sup> systems involved in the maintenance of intracellular free Ca<sup>2+</sup> at the properly low level in eukaryotic cells. The failure of neurons to keep optimal intracellular Ca<sup>2+</sup> concentrations is a common feature of neurodegeneration by aging and aging-linked neuropathologies, such as Alzheimer's disease (AD). This disease is characterized by the accumulation of β-amyloid senile plaques and neurofibrillary tangles of tau, a protein that plays a key role in axonal transport. Here we show a novel inhibition of PMCA activity by tau which is concentration-dependent. The extent of inhibition significantly decreases with aging in mice and control human brain membranes, but inhibition profiles were similar in AD-affected brain membrane preparations, independently of age. No significant changes in PMCA expression and localization with aging or neuropathology were found. These results point out a link between Ca<sup>2+</sup>-transporters, aging and neurodegeneration mediated by tau protein.Ministerio de Economía y Competitividad and Fundación Marcelino Botín (to A.M.M.); Junta de Extremadura and FEDERPeer ReviewedJunta de ExtremaduraEuropean CommissionMinisterio de Economía y Competitividad (España)Fundación BotínConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2016201620152016info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/139543reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1395432026-05-22T06:33:51Z
dc.title.none.fl_str_mv Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology
title Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology
spellingShingle Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology
Berrocal, María
PMCA
Tau
Calcium
Aging
Alzheimer disease
title_short Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology
title_full Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology
title_fullStr Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology
title_full_unstemmed Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology
title_sort Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology
dc.creator.none.fl_str_mv Berrocal, María
Corbacho, Isaac
Vázquez-Hernández, María
Ávila, Jesús
Sepúlveda, M. Rosario
Mata, Ana M.
author Berrocal, María
author_facet Berrocal, María
Corbacho, Isaac
Vázquez-Hernández, María
Ávila, Jesús
Sepúlveda, M. Rosario
Mata, Ana M.
author_role author
author2 Corbacho, Isaac
Vázquez-Hernández, María
Ávila, Jesús
Sepúlveda, M. Rosario
Mata, Ana M.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Junta de Extremadura
European Commission
Ministerio de Economía y Competitividad (España)
Fundación Botín
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv PMCA
Tau
Calcium
Aging
Alzheimer disease
topic PMCA
Tau
Calcium
Aging
Alzheimer disease
description © 2015 Elsevier B.V.. Ca<sup>2+</sup>-ATPases are plasma membrane and intracellular membrane transporters that use the energy of ATP hydrolysis to pump cytosolic Ca<sup>2+</sup> out of the cell (PMCA) or into internal stores. These pumps are the main high-affinity Ca<sup>2+</sup> systems involved in the maintenance of intracellular free Ca<sup>2+</sup> at the properly low level in eukaryotic cells. The failure of neurons to keep optimal intracellular Ca<sup>2+</sup> concentrations is a common feature of neurodegeneration by aging and aging-linked neuropathologies, such as Alzheimer's disease (AD). This disease is characterized by the accumulation of β-amyloid senile plaques and neurofibrillary tangles of tau, a protein that plays a key role in axonal transport. Here we show a novel inhibition of PMCA activity by tau which is concentration-dependent. The extent of inhibition significantly decreases with aging in mice and control human brain membranes, but inhibition profiles were similar in AD-affected brain membrane preparations, independently of age. No significant changes in PMCA expression and localization with aging or neuropathology were found. These results point out a link between Ca<sup>2+</sup>-transporters, aging and neurodegeneration mediated by tau protein.
publishDate 2015
dc.date.none.fl_str_mv 2015
2016
2016
2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/139543
url http://hdl.handle.net/10261/139543
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,812429

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