Taurine 11 pp 755-771 | Cite as

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

  • Alessia Baseggio Conrado
  • Elisabetta Capuozzo
  • Luciana Mosca
  • Antonio Francioso
  • Mario FontanaEmail author
Conference paper
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 1155)


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.


Thiotaurine Hypotaurine Sulfane sulfur H2S donor H2S signaling Reactive sulfur species Hydrogen sulfide Antioxidant Inflammation Neutrophils 





Cysteine aminotransferase


Cystathionine β-synthase


Cysteine dioxygenase




Cysteine sulfinate decarboxylase


Cystathionine γ-lyase


Glyceraldehyde 3-phosphate dehydrogenase




Glutathione persulfide


Hydrogen sulfide


Hydrogen persulfide




Mercaptopyruvate sulfurtransferase




Pyridoxal 5′-phosphate


Phorbol 12-myristate 13-acetate


Reactive oxygen species


Thiolate anion


















Zero-valent sulfur




Thiosulfonate group




Elemental sulfur









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


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Copyright information

© Springer Nature Singapore Pte Ltd. 2019

Authors and Affiliations

  • Alessia Baseggio Conrado
    • 1
    • 2
  • Elisabetta Capuozzo
    • 1
  • Luciana Mosca
    • 1
  • Antonio Francioso
    • 1
    • 3
  • Mario Fontana
    • 1
    Email author
  1. 1.Department of Biochemical SciencesSapienza University of RomeRomeItaly
  2. 2.Photobiology UnitUniversity of Dundee, Ninewells Hospital & Medical SchoolDundeeUK
  3. 3.Department of Bioorganic ChemistryLeibniz Institute of Plant BiochemistryHalleGermany

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