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Thiotaurine: From Chemical and Biological Properties to Role in H2S Signaling

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Taurine 11

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 1155))

Abstract

In the last decade thiotaurine, 2-aminoethane thiosulfonate, has been investigated as an inflammatory modulating agent as a result of its ability to release hydrogen sulfide (H2S) known to play regulatory roles in inflammation. Thiotaurine can be included in the “taurine family” due to structural similarity to taurine and hypotaurine, and is characterized by the presence of a sulfane sulfur moiety. Thiotaurine can be produced by different pathways, such as the spontaneous transsulfuration between thiocysteine – a persulfide analogue of cysteine – and hypotaurine as well as in vivo from cystine. Moreover, the enzymatic oxidation of cysteamine to hypotaurine and thiotaurine in the presence of inorganic sulfur can occur in animal tissues and last but not least thiotaurine can be generated by the transfer of sulfur from mercaptopyruvate to hypotaurine catalyzed by a sulfurtransferase. Thiotaurine is an effective antioxidant agent as demonstrated by its ability to counteract the damage caused by pro-oxidants in the rat. Recently, we observed the influence of thiotaurine on human neutrophils functional responses. In particular, thiotaurine has been found to prevent human neutrophil spontaneous apoptosis suggesting an alternative or additional role to its antioxidant activity. It is likely that the sulfane sulfur of thiotaurine may modulate neutrophil activation via persulfidation of target proteins. In conclusion, thiotaurine can represent a biologically relevant sulfur donor acting as a biological intermediate in the transport, storage and release of sulfide.

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Abbreviations

APAP:

Acetaminophen

CAT:

Cysteine aminotransferase

CBS:

Cystathionine β-synthase

CDO:

Cysteine dioxygenase

CN−:

Cyanide

CSAD:

Cysteine sulfinate decarboxylase

CSE:

Cystathionine γ-lyase

GAPDH:

Glyceraldehyde 3-phosphate dehydrogenase

GSH:

Glutathione

GSSH:

Glutathione persulfide

H2S:

Hydrogen sulfide

HSSH:

Hydrogen persulfide

MDA:

Malondialdehyde

MST:

Mercaptopyruvate sulfurtransferase

NAC:

N-acetylcysteine

PLP:

Pyridoxal 5′-phosphate

PMA:

Phorbol 12-myristate 13-acetate

ROS:

Reactive oxygen species

RS−:

Thiolate anion

RSH:

Thiol

RSO2H:

Sulfinate/Hypotaurine

RSO2SH:

Thiosulfonate/Thiotaurine

RSO3H:

Sulfonate/Taurine

RSOH:

Sulfenate

RSSH:

Persulfide/Thiocysteine

RSSnSR:

Polysulfide

RSSR:

Disulfide

S0:

Zero-valent sulfur

S2−:

Sulfide

−S2O2−:

Thiosulfonate group

S2O32−:

Thiosulfate

S8:

Elemental sulfur

SCN−:

Thiocyanate

SO32−:

Sulfite

STZ:

Streptozotocin

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Acknowledgement

The authors are grateful to Dr. Alessandro Chinazzi (Department of Biochemical Sciences – Sapienza University of Rome) for the technical assistance.

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Authors and Affiliations

  1. Department of Biochemical Sciences, Sapienza University of Rome, Rome, Italy

    Alessia Baseggio Conrado, Elisabetta Capuozzo, Luciana Mosca, Antonio Francioso & Mario Fontana

  2. Photobiology Unit, University of Dundee, Ninewells Hospital & Medical School, Dundee, UK

    Alessia Baseggio Conrado

  3. Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, Halle, Germany

    Antonio Francioso

Authors
  1. Alessia Baseggio Conrado
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  2. Elisabetta Capuozzo
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  3. Luciana Mosca
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  4. Antonio Francioso
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  5. Mario Fontana
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Corresponding author

Correspondence to Mario Fontana .

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Editors and Affiliations

  1. College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, Shenyang, Liaoning, China

    Jianmin Hu

  2. Department of Occupational and Environmental Health, Dalian Medicine University, Dalian, Liaoning, China

    Fengyuan Piao

  3. Department of Pharmacology, College of Medicine, University of South Alabama, Mobile, AL, USA

    Stephen W. Schaffer

  4. Department of Biology, Center for Developmental Neuroscience, College of Staten Island, Staten Island, NY, USA

    Abdeslem El Idrissi

  5. Department of Biomedical Science, Charles E. Schmidt College of Medicine, Florida Atlantic University, Boca Raton, FL, USA

    Jang-Yen Wu

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This work is dedicated to the memory of Professor Doriano Cavallini and Professor Carlo De Marco

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Baseggio Conrado, A., Capuozzo, E., Mosca, L., Francioso, A., Fontana, M. (2019). Thiotaurine: From Chemical and Biological Properties to Role in H2S Signaling. In: Hu, J., Piao, F., Schaffer, S., El Idrissi, A., Wu, JY. (eds) Taurine 11. Advances in Experimental Medicine and Biology, vol 1155. Springer, Singapore. https://doi.org/10.1007/978-981-13-8023-5_66

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