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Regulation of mitochondrial bioenergetic function by hydrogen sulfide. Part I. Biochemical and physiological mechanisms.
Br J Pharmacol. 2014 Apr; 171(8):2099-122.BJ

Abstract

Until recently, hydrogen sulfide (H2 S) was exclusively viewed a toxic gas and an environmental hazard, with its toxicity primarily attributed to the inhibition of mitochondrial Complex IV, resulting in a shutdown of mitochondrial electron transport and cellular ATP generation. Work over the last decade established multiple biological regulatory roles of H2 S, as an endogenous gaseous transmitter. H2 S is produced by cystathionine γ-lyase (CSE), cystathionine β-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (3-MST). In striking contrast to its inhibitory effect on Complex IV, recent studies showed that at lower concentrations, H2 S serves as a stimulator of electron transport in mammalian cells, by acting as a mitochondrial electron donor. Endogenous H2 S, produced by mitochondrially localized 3-MST, supports basal, physiological cellular bioenergetic functions; the activity of this metabolic support declines with physiological aging. In specialized conditions (calcium overload in vascular smooth muscle, colon cancer cells), CSE and CBS can also associate with the mitochondria; H2 S produced by these enzymes, serves as an endogenous stimulator of cellular bioenergetics. The current article overviews the biochemical mechanisms underlying the stimulatory and inhibitory effects of H2 S on mitochondrial function and cellular bioenergetics and discusses the implication of these processes for normal cellular physiology. The relevance of H2 S biology is also discussed in the context of colonic epithelial cell physiology: colonocytes are exposed to high levels of sulfide produced by enteric bacteria, and serve as a metabolic barrier to limit their entry into the mammalian host, while, at the same time, utilizing it as a metabolic 'fuel'.

Authors+Show Affiliations

Department of Anesthesiology, University of Texas Medical Branch, Galveston, TX, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

23991830

Citation

Szabo, Csaba, et al. "Regulation of Mitochondrial Bioenergetic Function By Hydrogen Sulfide. Part I. Biochemical and Physiological Mechanisms." British Journal of Pharmacology, vol. 171, no. 8, 2014, pp. 2099-122.
Szabo C, Ransy C, Módis K, et al. Regulation of mitochondrial bioenergetic function by hydrogen sulfide. Part I. Biochemical and physiological mechanisms. Br J Pharmacol. 2014;171(8):2099-122.
Szabo, C., Ransy, C., Módis, K., Andriamihaja, M., Murghes, B., Coletta, C., Olah, G., Yanagi, K., & Bouillaud, F. (2014). Regulation of mitochondrial bioenergetic function by hydrogen sulfide. Part I. Biochemical and physiological mechanisms. British Journal of Pharmacology, 171(8), 2099-122. https://doi.org/10.1111/bph.12369
Szabo C, et al. Regulation of Mitochondrial Bioenergetic Function By Hydrogen Sulfide. Part I. Biochemical and Physiological Mechanisms. Br J Pharmacol. 2014;171(8):2099-122. PubMed PMID: 23991830.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Regulation of mitochondrial bioenergetic function by hydrogen sulfide. Part I. Biochemical and physiological mechanisms. AU - Szabo,Csaba, AU - Ransy,Céline, AU - Módis,Katalin, AU - Andriamihaja,Mireille, AU - Murghes,Baptiste, AU - Coletta,Ciro, AU - Olah,Gabor, AU - Yanagi,Kazunori, AU - Bouillaud,Frédéric, PY - 2013/07/06/received PY - 2013/08/08/revised PY - 2013/08/12/accepted PY - 2013/9/3/entrez PY - 2013/9/3/pubmed PY - 2014/12/15/medline KW - 3-mercaptopyruvate sulfurtransferase KW - bioenergetics KW - blood vessels KW - cysteine KW - cytochrome c oxidase KW - free radicals KW - gasotransmitters KW - mitochondrial electron transport KW - nitric oxide KW - superoxide SP - 2099 EP - 122 JF - British journal of pharmacology JO - Br J Pharmacol VL - 171 IS - 8 N2 - Until recently, hydrogen sulfide (H2 S) was exclusively viewed a toxic gas and an environmental hazard, with its toxicity primarily attributed to the inhibition of mitochondrial Complex IV, resulting in a shutdown of mitochondrial electron transport and cellular ATP generation. Work over the last decade established multiple biological regulatory roles of H2 S, as an endogenous gaseous transmitter. H2 S is produced by cystathionine γ-lyase (CSE), cystathionine β-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (3-MST). In striking contrast to its inhibitory effect on Complex IV, recent studies showed that at lower concentrations, H2 S serves as a stimulator of electron transport in mammalian cells, by acting as a mitochondrial electron donor. Endogenous H2 S, produced by mitochondrially localized 3-MST, supports basal, physiological cellular bioenergetic functions; the activity of this metabolic support declines with physiological aging. In specialized conditions (calcium overload in vascular smooth muscle, colon cancer cells), CSE and CBS can also associate with the mitochondria; H2 S produced by these enzymes, serves as an endogenous stimulator of cellular bioenergetics. The current article overviews the biochemical mechanisms underlying the stimulatory and inhibitory effects of H2 S on mitochondrial function and cellular bioenergetics and discusses the implication of these processes for normal cellular physiology. The relevance of H2 S biology is also discussed in the context of colonic epithelial cell physiology: colonocytes are exposed to high levels of sulfide produced by enteric bacteria, and serve as a metabolic barrier to limit their entry into the mammalian host, while, at the same time, utilizing it as a metabolic 'fuel'. SN - 1476-5381 UR - https://www.unboundmedicine.com/medline/citation/23991830/Regulation_of_mitochondrial_bioenergetic_function_by_hydrogen_sulfide__Part_I__Biochemical_and_physiological_mechanisms_ L2 - https://doi.org/10.1111/bph.12369 DB - PRIME DP - Unbound Medicine ER -