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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...

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Autores principales: Ju, Yun-Jin, Lee, Hye-Won, Choi, Ji-Woong, Choi, Min-Sik
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
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.
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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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