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Signaling molecules: hydrogen sulfide and polysulfide.
Antioxid Redox Signal. 2015 Feb 10; 22(5):362-76.AR

Abstract

SIGNIFICANCE

Hydrogen sulfide (H2S) has been recognized as a signaling molecule as well as a cytoprotectant. It modulates neurotransmission, regulates vascular tone, and protects various tissues and organs, including neurons, the heart, and kidneys, from oxidative stress and ischemia-reperfusion injury. H2S is produced from l-cysteine by cystathionine β-synthase (CBS), cystathionine γ-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase.

RECENT ADVANCES

In addition to these enzymes, we recently identified a novel pathway to produce H2S from d-cysteine, which involves d-amino acid oxidase (DAO) along with 3MST. These enzymes are localized in the cytoplasm, mitochondria, and peroxisomes. However, some enzymes translocate to organelles under specific conditions. Moreover, H2S-derived potential signaling molecules such as polysulfides and HSNO have been identified.

CRITICAL ISSUES

The physiological stimulations, which trigger the production of H2S and its derivatives and maintain their local levels, remain unclear.

FUTURE DIRECTIONS

Understanding the regulation of the H2S production and H2S-derived signaling molecules and the specific stimuli that induce their release will provide new insights into the biology of H2S and therapeutic development in diseases involving these substances.

Authors+Show Affiliations

National Institute of Neuroscience , National Center of Neurology and Psychiatry, Kodaira, Tokyo, Japan .

Pub Type(s)

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

Language

eng

PubMed ID

24800864

Citation

Kimura, Hideo. "Signaling Molecules: Hydrogen Sulfide and Polysulfide." Antioxidants & Redox Signaling, vol. 22, no. 5, 2015, pp. 362-76.
Kimura H. Signaling molecules: hydrogen sulfide and polysulfide. Antioxid Redox Signal. 2015;22(5):362-76.
Kimura, H. (2015). Signaling molecules: hydrogen sulfide and polysulfide. Antioxidants & Redox Signaling, 22(5), 362-76. https://doi.org/10.1089/ars.2014.5869
Kimura H. Signaling Molecules: Hydrogen Sulfide and Polysulfide. Antioxid Redox Signal. 2015 Feb 10;22(5):362-76. PubMed PMID: 24800864.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Signaling molecules: hydrogen sulfide and polysulfide. A1 - Kimura,Hideo, Y1 - 2014/06/25/ PY - 2014/5/8/entrez PY - 2014/5/8/pubmed PY - 2015/11/18/medline SP - 362 EP - 76 JF - Antioxidants & redox signaling JO - Antioxid Redox Signal VL - 22 IS - 5 N2 - SIGNIFICANCE: Hydrogen sulfide (H2S) has been recognized as a signaling molecule as well as a cytoprotectant. It modulates neurotransmission, regulates vascular tone, and protects various tissues and organs, including neurons, the heart, and kidneys, from oxidative stress and ischemia-reperfusion injury. H2S is produced from l-cysteine by cystathionine β-synthase (CBS), cystathionine γ-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase. RECENT ADVANCES: In addition to these enzymes, we recently identified a novel pathway to produce H2S from d-cysteine, which involves d-amino acid oxidase (DAO) along with 3MST. These enzymes are localized in the cytoplasm, mitochondria, and peroxisomes. However, some enzymes translocate to organelles under specific conditions. Moreover, H2S-derived potential signaling molecules such as polysulfides and HSNO have been identified. CRITICAL ISSUES: The physiological stimulations, which trigger the production of H2S and its derivatives and maintain their local levels, remain unclear. FUTURE DIRECTIONS: Understanding the regulation of the H2S production and H2S-derived signaling molecules and the specific stimuli that induce their release will provide new insights into the biology of H2S and therapeutic development in diseases involving these substances. SN - 1557-7716 UR - https://www.unboundmedicine.com/medline/citation/24800864/Signaling_molecules:_hydrogen_sulfide_and_polysulfide_ L2 - https://www.liebertpub.com/doi/10.1089/ars.2014.5869?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -