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dc.contributor.authorSánchez-Varo, Raquel María 
dc.contributor.authorCriado-Álamo, Elena
dc.contributor.authorFernández-Valenzuela, Juan José
dc.contributor.authorMercado-Sáenz, Silvia 
dc.contributor.authorLópez-Villodres, Juan Antonio 
dc.contributor.authorEscamilla-Sánchez, Alejandro 
dc.contributor.authorRodríguez-Pérez, Luis Manuel 
dc.contributor.authorArranz-Salas, Isabel María 
dc.contributor.authorOrtega-Jiménez, Concepción 
dc.contributor.authorAlba-Tercedor, Carmen
dc.contributor.authorGutiérrez-Pérez, Antonia 
dc.date.accessioned2022-09-20T07:16:24Z
dc.date.available2022-09-20T07:16:24Z
dc.date.created2022-09-19
dc.date.issued2022-09
dc.identifier.urihttps://hdl.handle.net/10630/25037
dc.description.abstractAlzheimer's disease (AD) constitutes the most prevalent form of dementia. There is no cure so there is an urgent need of novel therapeutic targets and treatments. The main histopathological hallmarks of AD brains are extracellular plaques formed by the beta-amyloid (Abeta) peptide, and intraneuronal neurofibrillary tangles composed of hyperphosphorylated tau (phospho-tau). In fact, AD is considered a neurodegenerative proteinopathy. The coexistence of these protein aggregates leads to synaptic damage, neuronal loss and cognitive decline in patients. The dysfunction of intracellular proteolytic systems (autophagy-lysosomal and ubiquitin-proteasome) has been postulated as a pathological mechanism contributing to the cerebral accumulation of these toxic proteins. Our aim is to verify the involvement of these pathways in the hippocampus of two different transgenic mice of AD to understand the differential impact of Abeta and phospho-tau accumulation on the pathological progression. Cerebral sections from APP/PS1 and ThyTau22 models (2 to 18 months) were analyzed. WT animals were used as controls. Immunohistochemical stainings were performed to evaluate amyloid deposition, phospho-tau accumulation, autophagic/lysosomal markers and ubiquitin at different pathological stages. In the amyloidogenic model we found a pathological accumulation of autophagic vesicles, lysosomes and ubiquitin in periplaque dystrophic neurites. In ThyTau22 model, only abnormal accumulation of ubiquitin was detected. These results demonstrate significant alterations of the proteolytic pathways in both models of proteinopathy even though they were differentially affected. Preclinical studies in transgenic models able to reproduce the pathogenic mechanisms of patients will allow the identification of novel therapeutic targets and to test effective treatments. Compounds able to reduce the burden of toxic proteins might be an alternative pharmacological approach to AD and other tauopathies.es_ES
dc.description.sponsorshipSupported by CTS-429 (Biology and Histology), and Instituto de Salud Carlos III (ISCiii) of Spain, co-financed by FEDER funds from European Union through grant PI21/00915 (to AG). Universidad de Málaga. Campus de Excelencia Internacional Andalucía Tech.es_ES
dc.language.isoenges_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.subjectAlzheimer, Enfermedad dees_ES
dc.subject.otherAlzheimeres_ES
dc.subject.otherModelos animaleses_ES
dc.subject.otherProteostasises_ES
dc.subject.otherBeta-amiloidees_ES
dc.subject.otherTaues_ES
dc.titleProtein homeostasis as a therapeutical target for Alzheimer’s disease: analysis in the hippocampus of transgenic mouse modelses_ES
dc.typeinfo:eu-repo/semantics/conferenceObjectes_ES
dc.centroFacultad de Medicinaes_ES
dc.relation.eventtitleXXI Congreso de la Sociedad Española de Histología e Ingeniería Tisular (SEHIT 2022)es_ES
dc.relation.eventplaceGranada, Españaes_ES
dc.relation.eventdate7 de septiembrees_ES


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