Cathepsin D in a murine model of frontotemporal dementia with parkinsonism-linked to chromosome 17
Entity
UAM. Departamento de Anatomía, Histología y NeurocienciaPublisher
IOS PressDate
2015-01-01Citation
10.3233/JAD-140456
Journal of Alzheimer's Disease 45.1 (2015): 1-14
ISSN
1387-2877DOI
10.3233/JAD-140456Funded by
This study was funded by grant from the Spanish Ministry of Health (SAF 2011-24841)Project
Gobierno de España. SAF 2011-24841Editor's Version
http://dx.doi.org/10.3233/JAD-140456Subjects
Cathepsin D; FTDP-17; Lysosomal system; Mutated tau; MedicinaNote
The final of publication is available at: http://dx.doi.org/10.3233/JAD-140456Abstract
Tauopathies, such as Alzheimer’s disease (AD) and Frontotemporal dementia with Parkinsonism linked to chromosome 17 (FTDP-17), are characterized by tau accumulation. This accumulation could result from alterations in tau degradation by either the ubiquitin-proteasome system or the autophagy–lysosomal pathway. To analyze a possible alteration of the autophagy–lysosomal pathway in transgenic mice expressing human tau with three FTDP-17 missense mutations (TauVLW mice), we studied the lysosomal enzyme Cathepsin D. The hippocampi of TauVLW mice, where the human mutant tau accumulates, showed both increased Cathepsin D and partial colocalization of Cathepsin D with human mutant tau. At the ultrastructural level, some multivesicular bodies showed human mutant tau-immunopositive vesicles. This finding could provide insights into the molecular mechanisms of tau degradation in human tauopathies
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Google Scholar:Fernández-Montoya, Julia
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Pérez, Mar
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