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Nuclear SOD1 in Growth Control, Oxidative Stress Response, Amyotrophic Lateral Sclerosis, and Cancer

SOD1 is the major superoxide dismutase responsible for catalyzing dismutation of superoxide to hydrogen peroxide and molecular oxygen. It is well known as an essential antioxidant enzyme for maintaining cellular redox homeostasis. SOD1 dysregulation has been associated with many diseases, including...

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Detalles Bibliográficos
Autores principales: Xu, Joyce, Su, Xiaoyang, Burley, Stephen K., Zheng, X. F. Steven
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8869091/
https://www.ncbi.nlm.nih.gov/pubmed/35204309
http://dx.doi.org/10.3390/antiox11020427
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author Xu, Joyce
Su, Xiaoyang
Burley, Stephen K.
Zheng, X. F. Steven
author_facet Xu, Joyce
Su, Xiaoyang
Burley, Stephen K.
Zheng, X. F. Steven
author_sort Xu, Joyce
collection PubMed
description SOD1 is the major superoxide dismutase responsible for catalyzing dismutation of superoxide to hydrogen peroxide and molecular oxygen. It is well known as an essential antioxidant enzyme for maintaining cellular redox homeostasis. SOD1 dysregulation has been associated with many diseases, including amyotrophic lateral sclerosis (ALS), cancer, accelerated aging, and age-related diseases. Recent studies also revealed that SOD1 can serve as a regulatory protein in cell signaling, transcription, and ribosome biogenesis. Notably, SOD1 is localized in the nucleus under both normal and pathological conditions, contributing to oxidative stress response and growth control. Moreover, increasing evidence points to the importance of nuclear SOD1 in the pathogenesis of ALS and cancer.
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spelling pubmed-88690912022-02-25 Nuclear SOD1 in Growth Control, Oxidative Stress Response, Amyotrophic Lateral Sclerosis, and Cancer Xu, Joyce Su, Xiaoyang Burley, Stephen K. Zheng, X. F. Steven Antioxidants (Basel) Review SOD1 is the major superoxide dismutase responsible for catalyzing dismutation of superoxide to hydrogen peroxide and molecular oxygen. It is well known as an essential antioxidant enzyme for maintaining cellular redox homeostasis. SOD1 dysregulation has been associated with many diseases, including amyotrophic lateral sclerosis (ALS), cancer, accelerated aging, and age-related diseases. Recent studies also revealed that SOD1 can serve as a regulatory protein in cell signaling, transcription, and ribosome biogenesis. Notably, SOD1 is localized in the nucleus under both normal and pathological conditions, contributing to oxidative stress response and growth control. Moreover, increasing evidence points to the importance of nuclear SOD1 in the pathogenesis of ALS and cancer. MDPI 2022-02-21 /pmc/articles/PMC8869091/ /pubmed/35204309 http://dx.doi.org/10.3390/antiox11020427 Text en © 2022 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
Xu, Joyce
Su, Xiaoyang
Burley, Stephen K.
Zheng, X. F. Steven
Nuclear SOD1 in Growth Control, Oxidative Stress Response, Amyotrophic Lateral Sclerosis, and Cancer
title Nuclear SOD1 in Growth Control, Oxidative Stress Response, Amyotrophic Lateral Sclerosis, and Cancer
title_full Nuclear SOD1 in Growth Control, Oxidative Stress Response, Amyotrophic Lateral Sclerosis, and Cancer
title_fullStr Nuclear SOD1 in Growth Control, Oxidative Stress Response, Amyotrophic Lateral Sclerosis, and Cancer
title_full_unstemmed Nuclear SOD1 in Growth Control, Oxidative Stress Response, Amyotrophic Lateral Sclerosis, and Cancer
title_short Nuclear SOD1 in Growth Control, Oxidative Stress Response, Amyotrophic Lateral Sclerosis, and Cancer
title_sort nuclear sod1 in growth control, oxidative stress response, amyotrophic lateral sclerosis, and cancer
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8869091/
https://www.ncbi.nlm.nih.gov/pubmed/35204309
http://dx.doi.org/10.3390/antiox11020427
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