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The physiological role of hydrogen sulfide and beyond.
Nitric Oxide. 2014 Sep 15; 41:4-10.NO

Abstract

Hydrogen sulfide (H2S) has been considered to be a physiological mediator since the identification of endogenous sulfides in the mammalian brain. H2S is produced from L-cysteine by enzymes such as cystathionine β-synthase (CBS), cystathionine γ-lyase (CSE), 3-mercaptopyruvate sulfurtransferase (3MST), and cysteine aminotransferase (CAT). CSE and CAT are regulated by Ca(2+). At steady-state low intracellular concentrations of Ca(2+), CSE and the 3MST/CAT pathway produce H2S. However, after intracellular concentrations of Ca(2+) increase in stimulated cells, the production of H2S by these enzymes decreases. We recently identified a fourth pathway, by which H2S is produced from D-cysteine by the enzymes D-amino acid oxidase (DAO) and 3MST. This pathway is mainly localized in the cerebellum and the kidney. The production of H2S from D-cysteine is 80 times more efficient than that from L-cysteine in the kidney, and the administration of D-cysteine to mice ameliorates renal ischemia-reperfusion injury more effectively than L-cysteine. These results suggest that D-cysteine might be used to treat renal diseases or even increase the success of kidney transplantation. We found that H2S-derived polysulfides exist in the brain and activate transient receptor potential ankyrin-1 (TRPA1) channels 300 times more potently than H2S. Although TRPA1 channels mediate sensory transduction and respond to a variety of stimuli, including cold temperature, pungent compounds and environmental irritants, their endogenous ligand(s) has not been identified. The sulfane sulfur of polysulfides is a reactive electrophile that is readily transferred to a nucleophilic protein thiolate to generate the protein persulfide or bound sulfane sulfur by sulfhydration (as referred to as sulfuration). The bound sulfane sulfur-producing activity of polysulfides is much greater than that of H2S. This review focuses on the physiological roles of H2S and H2S-derived polysulfides as signaling molecules.

Authors+Show Affiliations

National Institute of Neuroscience, National Center of Neurology and Psychiatry, Kodaira, Tokyo 187-8502, Japan. Electronic address: kimura@ncnp.go.jp.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

24491257

Citation

Kimura, Hideo. "The Physiological Role of Hydrogen Sulfide and Beyond." Nitric Oxide : Biology and Chemistry, vol. 41, 2014, pp. 4-10.
Kimura H. The physiological role of hydrogen sulfide and beyond. Nitric Oxide. 2014;41:4-10.
Kimura, H. (2014). The physiological role of hydrogen sulfide and beyond. Nitric Oxide : Biology and Chemistry, 41, 4-10. https://doi.org/10.1016/j.niox.2014.01.002
Kimura H. The Physiological Role of Hydrogen Sulfide and Beyond. Nitric Oxide. 2014 Sep 15;41:4-10. PubMed PMID: 24491257.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The physiological role of hydrogen sulfide and beyond. A1 - Kimura,Hideo, Y1 - 2014/02/01/ PY - 2013/11/29/received PY - 2014/01/20/revised PY - 2014/01/22/accepted PY - 2014/2/5/entrez PY - 2014/2/5/pubmed PY - 2015/6/2/medline KW - Bound sulfane sulfur KW - H(2)S KW - Polysulfides KW - Sulfhydration KW - Sulfuration KW - TRP channels SP - 4 EP - 10 JF - Nitric oxide : biology and chemistry JO - Nitric Oxide VL - 41 N2 - Hydrogen sulfide (H2S) has been considered to be a physiological mediator since the identification of endogenous sulfides in the mammalian brain. H2S is produced from L-cysteine by enzymes such as cystathionine β-synthase (CBS), cystathionine γ-lyase (CSE), 3-mercaptopyruvate sulfurtransferase (3MST), and cysteine aminotransferase (CAT). CSE and CAT are regulated by Ca(2+). At steady-state low intracellular concentrations of Ca(2+), CSE and the 3MST/CAT pathway produce H2S. However, after intracellular concentrations of Ca(2+) increase in stimulated cells, the production of H2S by these enzymes decreases. We recently identified a fourth pathway, by which H2S is produced from D-cysteine by the enzymes D-amino acid oxidase (DAO) and 3MST. This pathway is mainly localized in the cerebellum and the kidney. The production of H2S from D-cysteine is 80 times more efficient than that from L-cysteine in the kidney, and the administration of D-cysteine to mice ameliorates renal ischemia-reperfusion injury more effectively than L-cysteine. These results suggest that D-cysteine might be used to treat renal diseases or even increase the success of kidney transplantation. We found that H2S-derived polysulfides exist in the brain and activate transient receptor potential ankyrin-1 (TRPA1) channels 300 times more potently than H2S. Although TRPA1 channels mediate sensory transduction and respond to a variety of stimuli, including cold temperature, pungent compounds and environmental irritants, their endogenous ligand(s) has not been identified. The sulfane sulfur of polysulfides is a reactive electrophile that is readily transferred to a nucleophilic protein thiolate to generate the protein persulfide or bound sulfane sulfur by sulfhydration (as referred to as sulfuration). The bound sulfane sulfur-producing activity of polysulfides is much greater than that of H2S. This review focuses on the physiological roles of H2S and H2S-derived polysulfides as signaling molecules. SN - 1089-8611 UR - https://www.unboundmedicine.com/medline/citation/24491257/The_physiological_role_of_hydrogen_sulfide_and_beyond_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1089-8603(14)00003-2 DB - PRIME DP - Unbound Medicine ER -