ER Dysfunction and Protein Folding Stress in ALS
Amyotrophic lateral sclerosis (ALS) is the most frequent paralytic disease in adults. Most ALS cases are considered sporadic with no clear genetic component. The disruption of protein homeostasis due to chronic stress responses at the endoplasmic reticulum (ER) and the accumulation of abnormal prote...
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| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2013-01-01
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| Series: | International Journal of Cell Biology |
| Online Access: | http://dx.doi.org/10.1155/2013/674751 |
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| _version_ | 1832549542279512064 |
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| author | Soledad Matus Vicente Valenzuela Danilo B. Medinas Claudio Hetz |
| author_facet | Soledad Matus Vicente Valenzuela Danilo B. Medinas Claudio Hetz |
| author_sort | Soledad Matus |
| collection | DOAJ |
| description | Amyotrophic lateral sclerosis (ALS) is the most frequent paralytic disease in adults. Most ALS cases are considered sporadic with no clear genetic component. The disruption of protein homeostasis due to chronic stress responses at the endoplasmic reticulum (ER) and the accumulation of abnormal protein inclusions are extensively described in ALS mouse models and patient-derived tissue. Recent studies using pharmacological and genetic manipulation of the unfolded protein response (UPR), an adaptive reaction against ER stress, have demonstrated a complex involvement of the pathway in experimental models of ALS. In addition, quantitative changes in ER stress-responsive chaperones in body fluids have been proposed as possible biomarkers to monitor the disease progression. Here we review most recent advances attributing a causal role of ER stress in ALS. |
| format | Article |
| id | doaj-art-cc604072232247c4b94c189e25c55fdf |
| institution | Kabale University |
| issn | 1687-8876 1687-8884 |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | International Journal of Cell Biology |
| spelling | doaj-art-cc604072232247c4b94c189e25c55fdf2025-02-03T06:11:02ZengWileyInternational Journal of Cell Biology1687-88761687-88842013-01-01201310.1155/2013/674751674751ER Dysfunction and Protein Folding Stress in ALSSoledad Matus0Vicente Valenzuela1Danilo B. Medinas2Claudio Hetz3Neurounion Biomedical Foundation, Santiago, ChileBiomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, ChileBiomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, ChileBiomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, ChileAmyotrophic lateral sclerosis (ALS) is the most frequent paralytic disease in adults. Most ALS cases are considered sporadic with no clear genetic component. The disruption of protein homeostasis due to chronic stress responses at the endoplasmic reticulum (ER) and the accumulation of abnormal protein inclusions are extensively described in ALS mouse models and patient-derived tissue. Recent studies using pharmacological and genetic manipulation of the unfolded protein response (UPR), an adaptive reaction against ER stress, have demonstrated a complex involvement of the pathway in experimental models of ALS. In addition, quantitative changes in ER stress-responsive chaperones in body fluids have been proposed as possible biomarkers to monitor the disease progression. Here we review most recent advances attributing a causal role of ER stress in ALS.http://dx.doi.org/10.1155/2013/674751 |
| spellingShingle | Soledad Matus Vicente Valenzuela Danilo B. Medinas Claudio Hetz ER Dysfunction and Protein Folding Stress in ALS International Journal of Cell Biology |
| title | ER Dysfunction and Protein Folding Stress in ALS |
| title_full | ER Dysfunction and Protein Folding Stress in ALS |
| title_fullStr | ER Dysfunction and Protein Folding Stress in ALS |
| title_full_unstemmed | ER Dysfunction and Protein Folding Stress in ALS |
| title_short | ER Dysfunction and Protein Folding Stress in ALS |
| title_sort | er dysfunction and protein folding stress in als |
| url | http://dx.doi.org/10.1155/2013/674751 |
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