Autophagy and misfolded proteins in neurodegeneration
The accumulation of misfolded proteins in insoluble aggregates within the neuronal cytoplasm is one of the common pathological hallmarks of most adult-onset human neurodegenerative diseases. The clearance of these misfolded proteins may represent a promising therapeutic strategy in these diseases. T...
| Main Authors: | , , , |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
Academic Press
2012
|
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3463804/ |
| id |
pubmed-3463804 |
|---|---|
| recordtype |
oai_dc |
| spelling |
pubmed-34638042012-11-01 Autophagy and misfolded proteins in neurodegeneration Metcalf, Daniel J. García-Arencibia, Moisés Hochfeld, Warren E. Rubinsztein, David C. Review The accumulation of misfolded proteins in insoluble aggregates within the neuronal cytoplasm is one of the common pathological hallmarks of most adult-onset human neurodegenerative diseases. The clearance of these misfolded proteins may represent a promising therapeutic strategy in these diseases. The two main routes for intracellular protein degradation are the ubiquitin–proteasome and the autophagy–lysosome pathways. In this review, we will focus on the autophagic pathway, by providing some examples of how impairment at different steps in this degradation pathway is related to different neurodegenerative diseases. We will also consider that upregulating autophagy may be useful in the treatment of some of these diseases. Finally, we discuss how antioxidants, which have been considered to be beneficial in neurodegenerative diseases, can block autophagy, thus potentially compromising their therapeutic potential. Academic Press 2012-11 /pmc/articles/PMC3463804/ /pubmed/21095248 http://dx.doi.org/10.1016/j.expneurol.2010.11.003 Text en © 2012 Elsevier Inc. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Metcalf, Daniel J. García-Arencibia, Moisés Hochfeld, Warren E. Rubinsztein, David C. |
| spellingShingle |
Metcalf, Daniel J. García-Arencibia, Moisés Hochfeld, Warren E. Rubinsztein, David C. Autophagy and misfolded proteins in neurodegeneration |
| author_facet |
Metcalf, Daniel J. García-Arencibia, Moisés Hochfeld, Warren E. Rubinsztein, David C. |
| author_sort |
Metcalf, Daniel J. |
| title |
Autophagy and misfolded proteins in neurodegeneration |
| title_short |
Autophagy and misfolded proteins in neurodegeneration |
| title_full |
Autophagy and misfolded proteins in neurodegeneration |
| title_fullStr |
Autophagy and misfolded proteins in neurodegeneration |
| title_full_unstemmed |
Autophagy and misfolded proteins in neurodegeneration |
| title_sort |
autophagy and misfolded proteins in neurodegeneration |
| description |
The accumulation of misfolded proteins in insoluble aggregates within the neuronal cytoplasm is one of the common pathological hallmarks of most adult-onset human neurodegenerative diseases. The clearance of these misfolded proteins may represent a promising therapeutic strategy in these diseases. The two main routes for intracellular protein degradation are the ubiquitin–proteasome and the autophagy–lysosome pathways. In this review, we will focus on the autophagic pathway, by providing some examples of how impairment at different steps in this degradation pathway is related to different neurodegenerative diseases. We will also consider that upregulating autophagy may be useful in the treatment of some of these diseases. Finally, we discuss how antioxidants, which have been considered to be beneficial in neurodegenerative diseases, can block autophagy, thus potentially compromising their therapeutic potential. |
| publisher |
Academic Press |
| publishDate |
2012 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3463804/ |
| _version_ |
1611913576223604736 |