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Título: | Amyloid Generation and Dysfunctional Immunoproteasome Activation with Disease Progression in Animal Model of Familial Alzheimer¿s Disease |
Autor: | Aso, E.; Lomoio, S.; López-González, I.; Joda, L.; Carmona, M.; Fernández-Yagüe, N.; Jiménez-Moreno, José Antonio; Juvés, S.; Pujol, A.; Pamplona, R.; Portero-Otín, M.; Martín, María Virginia; Díaz, M.; Ferrer, I. | Palabras clave: | Centro Oceanográfico de Canarias Desconocido |
Fecha de publicación: | 2012 | Citación: | Brain Pathology, 22 (5). 2012: 636-653 | Resumen: | Double-transgenic amyloid precursor protein/presenilin 1 (APP/PS1) mice express a chimeric mouse/human APP bearing the Swedish mutation (Mo/HuAPP695swe) and a mutant human PS1-dE9 both causative of familial Alzheimer's disease (FAD). Transgenic mice show impaired memory and learning performance from the age of 6 months onwards. Double-transgenic APP/PS1 mice express altered APP and PS1 mRNAs and proteins, reduced β-secretase 1 (BACE1) mRNA and normal BACE1 protein, all of which suggest a particular mechanism of amyloidogenesis when compared with sporadic AD. The first β-amyloid plaques in APP/PS1 mice appear at 3 months, and they increase in number and distribution with disease progression in parallel with increased levels of brain soluble β-amyloid 1–42 and 1–40, but also with reduced 1–42/1–40 ratio with age. Amyloid deposition in plaques is accompanied by altered mitochondria and increased oxidative damage, post-translational modifications and accumulation of altered proteins at the dystrophic neurites surrounding plaques. Degradation pathways are also modified with disease progression including activation of the immunoproteasome together with variable alterations of the different protease activities of the ubiquitin-proteasome system. Present observations show modifications in the production of β-amyloid and activation and malfunction of the subcellular degradation pathways that have general implications in the pathogenesis of AD and more particularly in specificities of FAD amyloidogenesis. | URI: | http://hdl.handle.net/10261/327523 | DOI: | 10.1111/j.1750-3639.2011.00560.x | ISSN: | 1750-3639 |
Aparece en las colecciones: | (IEO) Artículos |
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