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Production of Hydrogen Sulfide from D-Cysteine and Its Therapeutic Potential

Accumulating evidence shows that H(2)S has physiological functions in various tissues and organs. It includes regulation of neuronal activity, vascular tension, a release of insulin, and protection of the heart, kidney, and brain from ischemic insult. H(2)S is produced by enzymes from l-cysteine; cy...

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Detalles Bibliográficos
Autores principales: Shibuya, Norihiro, Kimura, Hideo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3712494/
https://www.ncbi.nlm.nih.gov/pubmed/23882260
http://dx.doi.org/10.3389/fendo.2013.00087
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author Shibuya, Norihiro
Kimura, Hideo
author_facet Shibuya, Norihiro
Kimura, Hideo
author_sort Shibuya, Norihiro
collection PubMed
description Accumulating evidence shows that H(2)S has physiological functions in various tissues and organs. It includes regulation of neuronal activity, vascular tension, a release of insulin, and protection of the heart, kidney, and brain from ischemic insult. H(2)S is produced by enzymes from l-cysteine; cystathionine β-synthase, cystathionine γ-lyase, and 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase. We recently discovered an additional pathway for the production of H(2)S from d-cysteine. d-Amino acid oxidase provides 3-mercaptopyruvate for 3MST to produce H(2)S. d-Cysteine protects cerebellar neurons from oxidative stress and attenuates ischemia-reperfusion injury caused in the kidney more effectively than l-cysteine. This review focuses on a novel pathway for the production of H(2)S and its therapeutic application especially to the renal diseases.
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spelling pubmed-37124942013-07-23 Production of Hydrogen Sulfide from D-Cysteine and Its Therapeutic Potential Shibuya, Norihiro Kimura, Hideo Front Endocrinol (Lausanne) Endocrinology Accumulating evidence shows that H(2)S has physiological functions in various tissues and organs. It includes regulation of neuronal activity, vascular tension, a release of insulin, and protection of the heart, kidney, and brain from ischemic insult. H(2)S is produced by enzymes from l-cysteine; cystathionine β-synthase, cystathionine γ-lyase, and 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase. We recently discovered an additional pathway for the production of H(2)S from d-cysteine. d-Amino acid oxidase provides 3-mercaptopyruvate for 3MST to produce H(2)S. d-Cysteine protects cerebellar neurons from oxidative stress and attenuates ischemia-reperfusion injury caused in the kidney more effectively than l-cysteine. This review focuses on a novel pathway for the production of H(2)S and its therapeutic application especially to the renal diseases. Frontiers Media S.A. 2013-07-16 /pmc/articles/PMC3712494/ /pubmed/23882260 http://dx.doi.org/10.3389/fendo.2013.00087 Text en Copyright © 2013 Shibuya and Kimura. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.
spellingShingle Endocrinology
Shibuya, Norihiro
Kimura, Hideo
Production of Hydrogen Sulfide from D-Cysteine and Its Therapeutic Potential
title Production of Hydrogen Sulfide from D-Cysteine and Its Therapeutic Potential
title_full Production of Hydrogen Sulfide from D-Cysteine and Its Therapeutic Potential
title_fullStr Production of Hydrogen Sulfide from D-Cysteine and Its Therapeutic Potential
title_full_unstemmed Production of Hydrogen Sulfide from D-Cysteine and Its Therapeutic Potential
title_short Production of Hydrogen Sulfide from D-Cysteine and Its Therapeutic Potential
title_sort production of hydrogen sulfide from d-cysteine and its therapeutic potential
topic Endocrinology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3712494/
https://www.ncbi.nlm.nih.gov/pubmed/23882260
http://dx.doi.org/10.3389/fendo.2013.00087
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