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Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases
Arginase, a binuclear manganese metalloenzyme in the urea, catalyzes the hydrolysis of L-arginine to urea and L-ornithine. Both isoforms, arginase 1 and arginase 2 perform significant roles in the regulation of cellular functions in cardiovascular system, such as senescence, apoptosis, proliferation...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9547100/ https://www.ncbi.nlm.nih.gov/pubmed/36209203 http://dx.doi.org/10.1038/s41420-022-01200-4 |
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author | Li, Zhuozhuo Wang, Liwei Ren, Yuanyuan Huang, Yaoyao Liu, Wenxuan Lv, Ziwei Qian, Lu Yu, Yi Xiong, Yuyan |
author_facet | Li, Zhuozhuo Wang, Liwei Ren, Yuanyuan Huang, Yaoyao Liu, Wenxuan Lv, Ziwei Qian, Lu Yu, Yi Xiong, Yuyan |
author_sort | Li, Zhuozhuo |
collection | PubMed |
description | Arginase, a binuclear manganese metalloenzyme in the urea, catalyzes the hydrolysis of L-arginine to urea and L-ornithine. Both isoforms, arginase 1 and arginase 2 perform significant roles in the regulation of cellular functions in cardiovascular system, such as senescence, apoptosis, proliferation, inflammation, and autophagy, via a variety of mechanisms, including regulating L-arginine metabolism and activating multiple signal pathways. Furthermore, abnormal arginase activity contributes to the initiation and progression of a variety of CVDs. Therefore, targeting arginase may be a novel and promising approach for CVDs treatment. In this review, we give a comprehensive overview of the physiological and biological roles of arginase in a variety of CVDs, revealing the underlying mechanisms of arginase mediating vascular and cardiac function, as well as shedding light on the novel and promising therapeutic approaches for CVDs therapy in individuals. |
format | Online Article Text |
id | pubmed-9547100 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-95471002022-10-10 Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases Li, Zhuozhuo Wang, Liwei Ren, Yuanyuan Huang, Yaoyao Liu, Wenxuan Lv, Ziwei Qian, Lu Yu, Yi Xiong, Yuyan Cell Death Discov Review Article Arginase, a binuclear manganese metalloenzyme in the urea, catalyzes the hydrolysis of L-arginine to urea and L-ornithine. Both isoforms, arginase 1 and arginase 2 perform significant roles in the regulation of cellular functions in cardiovascular system, such as senescence, apoptosis, proliferation, inflammation, and autophagy, via a variety of mechanisms, including regulating L-arginine metabolism and activating multiple signal pathways. Furthermore, abnormal arginase activity contributes to the initiation and progression of a variety of CVDs. Therefore, targeting arginase may be a novel and promising approach for CVDs treatment. In this review, we give a comprehensive overview of the physiological and biological roles of arginase in a variety of CVDs, revealing the underlying mechanisms of arginase mediating vascular and cardiac function, as well as shedding light on the novel and promising therapeutic approaches for CVDs therapy in individuals. Nature Publishing Group UK 2022-10-08 /pmc/articles/PMC9547100/ /pubmed/36209203 http://dx.doi.org/10.1038/s41420-022-01200-4 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Review Article Li, Zhuozhuo Wang, Liwei Ren, Yuanyuan Huang, Yaoyao Liu, Wenxuan Lv, Ziwei Qian, Lu Yu, Yi Xiong, Yuyan Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases |
title | Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases |
title_full | Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases |
title_fullStr | Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases |
title_full_unstemmed | Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases |
title_short | Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases |
title_sort | arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9547100/ https://www.ncbi.nlm.nih.gov/pubmed/36209203 http://dx.doi.org/10.1038/s41420-022-01200-4 |
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