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The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases
Abnormal and excessive nitrosative stress contributes to neurodegenerative disease associated with the production of pathological levels of misfolded proteins. The accumulated findings strongly suggest that excessive NO production can induce and deepen these pathological processes, particularly by t...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8304259/ https://www.ncbi.nlm.nih.gov/pubmed/34357077 http://dx.doi.org/10.3390/life11070705 |
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author | Ju, Yun-Jin Lee, Hye-Won Choi, Ji-Woong Choi, Min-Sik |
author_facet | Ju, Yun-Jin Lee, Hye-Won Choi, Ji-Woong Choi, Min-Sik |
author_sort | Ju, Yun-Jin |
collection | PubMed |
description | Abnormal and excessive nitrosative stress contributes to neurodegenerative disease associated with the production of pathological levels of misfolded proteins. The accumulated findings strongly suggest that excessive NO production can induce and deepen these pathological processes, particularly by the S-nitrosylation of target proteins. Therefore, the relationship between S-nitrosylated proteins and the accumulation of misfolded proteins was reviewed. We particularly focused on the S-nitrosylation of E3-ubiquitin-protein ligase, parkin, and endoplasmic reticulum chaperone, PDI, which contribute to the accumulation of misfolded proteins. In addition to the target proteins being S-nitrosylated, NOS, which produces NO, and GSNOR, which inhibits S-nitrosylation, were also suggested as potential therapeutic targets for protein misfolding-associated diseases. |
format | Online Article Text |
id | pubmed-8304259 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-83042592021-07-25 The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases Ju, Yun-Jin Lee, Hye-Won Choi, Ji-Woong Choi, Min-Sik Life (Basel) Review Abnormal and excessive nitrosative stress contributes to neurodegenerative disease associated with the production of pathological levels of misfolded proteins. The accumulated findings strongly suggest that excessive NO production can induce and deepen these pathological processes, particularly by the S-nitrosylation of target proteins. Therefore, the relationship between S-nitrosylated proteins and the accumulation of misfolded proteins was reviewed. We particularly focused on the S-nitrosylation of E3-ubiquitin-protein ligase, parkin, and endoplasmic reticulum chaperone, PDI, which contribute to the accumulation of misfolded proteins. In addition to the target proteins being S-nitrosylated, NOS, which produces NO, and GSNOR, which inhibits S-nitrosylation, were also suggested as potential therapeutic targets for protein misfolding-associated diseases. MDPI 2021-07-17 /pmc/articles/PMC8304259/ /pubmed/34357077 http://dx.doi.org/10.3390/life11070705 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Ju, Yun-Jin Lee, Hye-Won Choi, Ji-Woong Choi, Min-Sik The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases |
title | The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases |
title_full | The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases |
title_fullStr | The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases |
title_full_unstemmed | The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases |
title_short | The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases |
title_sort | role of protein s-nitrosylation in protein misfolding-associated diseases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8304259/ https://www.ncbi.nlm.nih.gov/pubmed/34357077 http://dx.doi.org/10.3390/life11070705 |
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