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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)

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.

Keywords

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

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

Notes

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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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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