Mitochondrial Dysfunction and Oxidative and Endoplasmic Reticulum Stress in Argyrophilic Grain Disease

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dc.contributor.authorIlieva, Ekaterina V.
dc.contributor.authorKichev, Anton Vladimirov
dc.contributor.authorNaudí i Farré, Alba
dc.contributor.authorFerrer, Isidre
dc.contributor.authorPamplona Gras, Reinald
dc.contributor.authorPortero Otín, Manuel
dc.date.accessioned2016-11-24T11:06:53Z
dc.date.embargoEndDate2025-01-01
dc.date.issued2011
dc.description.abstractArgyrophilic grain disease (AGD) is characterized by the accumulation of hyperphosphorylated 4R tau in dendritic varicosities (i.e."grains") in neurons and pretangles in certain areas of the cerebral cortex and other brain regions. We investigated oxidative and endoplasmic reticulum (ER) stress and dysregulation of mitochondrialbiogenesis as potential mechanisms involved in the AGD pathogenesis. Samples from AGD patients (n = 8) and nonpathologic, age-matched controls (n = 5) were compared using biochemical and immunohistochemical techniques with a panel of antibodies to markers of ER stress responses, stress chaperones, oxidative stress and associated cellular responses, respiratory chain complexes, mitochondrial regulators, and modulators of mitochondrial biogenesis. Because AGD is often associated with other tauopathies, mainly Alzheimer disease (AD), results were also compared with those of a group of similar Braak AD stage cases without grains (n = 5). In both AD and AGD cases, we found activation of key molecules that are involved in the unfolded protein response and lead to elevated ER chaperone levels, increased oxidative stress damage, mainly related to lipoxidation and targeting glycolytic enzymes. Altered expression of components of the respiratory chain markers modulating mitochondrial biogenesis were selectively affected in AGD. The findings suggest that, despite the common pathogenic trends in AD and AGD, there is molecular specificity for AGD.ca_ES
dc.description.sponsorshipThe authors thank the tissue donors and their families and Dr Jesus Requena (Universidad de Santiago de Compostela, Spain) for providing the GSA and AASA standards.ca_ES
dc.identifier.doihttps://doi.org/10.1097/NEN.0b013e31820f8765
dc.identifier.idgrec017000
dc.identifier.issn0022-3069
dc.identifier.urihttp://hdl.handle.net/10459.1/58645
dc.language.isoengca_ES
dc.publisherOxford University Pressca_ES
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.1097/NEN.0b013e31820f8765ca_ES
dc.relation.ispartofJournal of Neuropathology and Experimental Neurology, 2011, vol. 70, núm. 4, p. 253-263ca_ES
dc.rights(c) American Association of Neuropathologists, Inc., 2011ca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccessca_ES
dc.subjectEndoplasmic reticulum stressca_ES
dc.subjectMitochondrial dysfunctionca_ES
dc.subjectNeurodegenerationca_ES
dc.subjectOxidative stressca_ES
dc.subjectProteomicsca_ES
dc.subjectUnfolded protein responseca_ES
dc.subjectArgyrophilic grain diseaseca_ES
dc.titleMitochondrial Dysfunction and Oxidative and Endoplasmic Reticulum Stress in Argyrophilic Grain Diseaseca_ES
dc.typearticleca_ES
dc.type.versionpublishedVersionca_ES
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