BetaII-tubulin and phospho-tau aggregates in alzheimer's disease and pick's disease

The expression of betaI-, betaII- and betaIII-tubulin isotypes was examined by immunohistochemistry in the entorhinal and transentorhinal cortices, hippocampus and dentate gyrus in normal human brains and in cases with Alzheimer's disease (AD), Pick's disease (PiD) and in argyrophilic grai...

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Autores: Puig, Berta, Ferrer, Isidro (Ferrer Abizanda), Ludueña, Richard F., Avila, Jesús
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2005
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/172904
Acceso en línea:https://hdl.handle.net/2445/172904
Access Level:acceso abierto
Palabra clave:Malaltia d'Alzheimer
Patologia
Cervell
Teixit nerviós
Alzheimer's disease
Pathology
Brain
Nerve tissue
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spelling BetaII-tubulin and phospho-tau aggregates in alzheimer's disease and pick's diseasePuig, BertaFerrer, Isidro (Ferrer Abizanda)Ludueña, Richard F.Avila, JesúsMalaltia d'AlzheimerPatologiaCervellTeixit nerviósAlzheimer's diseasePathologyBrainNerve tissueThe expression of betaI-, betaII- and betaIII-tubulin isotypes was examined by immunohistochemistry in the entorhinal and transentorhinal cortices, hippocampus and dentate gyrus in normal human brains and in cases with Alzheimer's disease (AD), Pick's disease (PiD) and in argyrophilic grain disease (AGD). The results showed that betaII-tubulin predominated in the upper layers (mainly layer II) and betaIII-tubulin in the inner layers of the entorhinal and transentorhinal cortices in control brains. betaII-tubulin immunoreactivity was higher than betaIII-tubulin immunoreactivity in granular neurons of the dentate gyrus, whereas pyramidal neurons of the hippocampus proper were stained equally with anti-betaII-tubulin andbetaIII-tubulin antibodies. No preferential layering distribution was observed for betaI-tubulin. Polymerization assays with tubulin peptides following the method of microtubule-associated protein displacement demonstrated that the betaI and betaIII isotypes have a higher binding capacity for tau than does the betaII isotype. Interestingly, about 60% of neurons with neurofibrillary tangles in layer II of the entorhinal and transentorhinal cortices in AD were selectively stained with anti-betaII-tubulin antibodies. Moderate betaII-tubulin immunoreactivity was also observed in Pick bodies in PiD. Taken together, these findings support the view that high betaII-tubulin content is a contributing factor in the formation of abnormal hyper-phosphorylated tau aggregates.IOS Press2005info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/172904Articles publicats en revistes (Patologia i Terapèutica Experimental)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.3233/jad-2005-7303Journal of Alzheimer's Disease, 2005, vol. 7, num. 3, p. 213-220https://doi.org/10.3233/jad-2005-7303(c) Puig, Berta et al., 2005info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1729042026-05-27T06:46:51Z
dc.title.none.fl_str_mv BetaII-tubulin and phospho-tau aggregates in alzheimer's disease and pick's disease
title BetaII-tubulin and phospho-tau aggregates in alzheimer's disease and pick's disease
spellingShingle BetaII-tubulin and phospho-tau aggregates in alzheimer's disease and pick's disease
Puig, Berta
Malaltia d'Alzheimer
Patologia
Cervell
Teixit nerviós
Alzheimer's disease
Pathology
Brain
Nerve tissue
title_short BetaII-tubulin and phospho-tau aggregates in alzheimer's disease and pick's disease
title_full BetaII-tubulin and phospho-tau aggregates in alzheimer's disease and pick's disease
title_fullStr BetaII-tubulin and phospho-tau aggregates in alzheimer's disease and pick's disease
title_full_unstemmed BetaII-tubulin and phospho-tau aggregates in alzheimer's disease and pick's disease
title_sort BetaII-tubulin and phospho-tau aggregates in alzheimer's disease and pick's disease
dc.creator.none.fl_str_mv Puig, Berta
Ferrer, Isidro (Ferrer Abizanda)
Ludueña, Richard F.
Avila, Jesús
author Puig, Berta
author_facet Puig, Berta
Ferrer, Isidro (Ferrer Abizanda)
Ludueña, Richard F.
Avila, Jesús
author_role author
author2 Ferrer, Isidro (Ferrer Abizanda)
Ludueña, Richard F.
Avila, Jesús
author2_role author
author
author
dc.subject.none.fl_str_mv Malaltia d'Alzheimer
Patologia
Cervell
Teixit nerviós
Alzheimer's disease
Pathology
Brain
Nerve tissue
topic Malaltia d'Alzheimer
Patologia
Cervell
Teixit nerviós
Alzheimer's disease
Pathology
Brain
Nerve tissue
description The expression of betaI-, betaII- and betaIII-tubulin isotypes was examined by immunohistochemistry in the entorhinal and transentorhinal cortices, hippocampus and dentate gyrus in normal human brains and in cases with Alzheimer's disease (AD), Pick's disease (PiD) and in argyrophilic grain disease (AGD). The results showed that betaII-tubulin predominated in the upper layers (mainly layer II) and betaIII-tubulin in the inner layers of the entorhinal and transentorhinal cortices in control brains. betaII-tubulin immunoreactivity was higher than betaIII-tubulin immunoreactivity in granular neurons of the dentate gyrus, whereas pyramidal neurons of the hippocampus proper were stained equally with anti-betaII-tubulin andbetaIII-tubulin antibodies. No preferential layering distribution was observed for betaI-tubulin. Polymerization assays with tubulin peptides following the method of microtubule-associated protein displacement demonstrated that the betaI and betaIII isotypes have a higher binding capacity for tau than does the betaII isotype. Interestingly, about 60% of neurons with neurofibrillary tangles in layer II of the entorhinal and transentorhinal cortices in AD were selectively stained with anti-betaII-tubulin antibodies. Moderate betaII-tubulin immunoreactivity was also observed in Pick bodies in PiD. Taken together, these findings support the view that high betaII-tubulin content is a contributing factor in the formation of abnormal hyper-phosphorylated tau aggregates.
publishDate 2005
dc.date.none.fl_str_mv 2005
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/172904
url https://hdl.handle.net/2445/172904
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3233/jad-2005-7303
Journal of Alzheimer's Disease, 2005, vol. 7, num. 3, p. 213-220
https://doi.org/10.3233/jad-2005-7303
dc.rights.none.fl_str_mv (c) Puig, Berta et al., 2005
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Puig, Berta et al., 2005
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv IOS Press
publisher.none.fl_str_mv IOS Press
dc.source.none.fl_str_mv Articles publicats en revistes (Patologia i Terapèutica Experimental)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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