期刊
PROGRESS IN NEUROBIOLOGY
卷 105, 期 -, 页码 49-59出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pneurobio.2013.03.001
关键词
Tau; Alzheimer's disease; Degradation; Aggregation; Ubiquitin; Proteasome; Autophagy
资金
- Basic Science Research Program
- National Research Foundation of Korea (NRF) Collaborative Research Program
- Ministry of Education, Science and Technology [2012-0003217, 2012-0009484, 2012R1A6A3A01039788]
- Korea-UK Collaborative Alzheimer's Disease Research Project, Ministry of Health & Welfare, Republic of Korea [A111227]
- Wellcome Trust
- Wellcome Trust/MRC Strategic Grant on Alzheimer's disease
- Tau Consortium
- Biomedical Research Unit in Dementia at Addenbrooke's Hospital
- Korea Health Promotion Institute [A111227] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2012R1A6A3A01039788] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- MRC [MC_G1000734] Funding Source: UKRI
- Medical Research Council [MC_G1000734] Funding Source: researchfish
The ubiquitin-proteasome system (UPS) and the autophagy-lysosome system are two major protein quality control mechanisms in eukaryotic cells. While the UPS has been considered for decades as the critical regulator in the degradation of various aggregate-prone proteins, autophagy has more recently been shown to be an important pathway implicated in neuronal health and disease. The two hallmark lesions of Alzheimer's disease (AD) are extracellular beta-amyloid plaques and intracellular tau tangles. It has been suggested that tau accumulation is pathologically more relevant to the development of neurodegeneration and cognitive decline in AD patients than beta-amyloid plaques. Here, we review the UPS and autophagy-mediated tau clearance mechanisms and outline the biochemical connections between these two processes. In addition, we discuss pharmacological methods that target these degradation systems for the treatment and prevention of AD. (C) 2013 Elsevier Ltd. All rights reserved.
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