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A Proteomic Approach to Study the Effect of Thiotaurine on Human Neutrophil Activation

  • Conference paper
Taurine 10

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 975))

Abstract

Thiotaurine, a thiosulfonate related to taurine and hypotaurine, is formed by a metabolic process from cystine and generated by a transulfuration reaction between hypotaurine and thiocysteine. Thiotaurine can produce hydrogen sulfide (H2S) from its sulfane sulfur moiety. H2S is a gaseous signaling molecule which can have regulatory roles in inflammatory process. In addition, sulfane sulfur displays the capacity to reversibly bind to other sulfur atoms. Thiotaurine inhibits PMA-induced activation of human neutrophils, and hinders neutrophil spontaneous apoptosis. Here, we present the results of a proteomic approach to study the possible effects of thiotaurine at protein expression level. Proteome analysis of human neutrophils has been performed comparing protein extracts of resting or PMA-activated neutrophils in presence or in absence of thiotaurine. In particular, PMA-stimulated neutrophils showed high level of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) expression compared to the level of the same glycolytic enzyme in the resting neutrophils. Conversely, decreased expression of GAPDH has been observed when human neutrophils were incubated with 1 mM thiotaurine before activation with PMA. This result, confirmed by Western blot analysis, suggests again that thiotaurine shows a bioactive role in the mechanisms underlying the inflammatory process, influencing the energy metabolism of activated leukocytes and raises the possibility that thiotaurine, acting as a sulfur donor, could modulate neutrophil activation via persulfidation of target proteins, such as GAPDH.

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Abbreviations

GAPDH:

Glyceraldehyde 3-phosphate dehydrogenase

TTAU:

Thiotaurine

PMA:

Phorbol 12-myristate 13-acetate PMNs, human neutrophils

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Authors and Affiliations

  1. Dipartimento di Scienze Biochimiche, Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185, Rome, Italy

    Elisabetta Capuozzo, Alessandra Giorgi, Alessia Baseggio Conrado, Maria Eugenia Schininà & Mario Fontana

  2. Dipartimento di Psicologia, sezione di Neuroscienze, Centro di Ricerche in Neurobiologia “Daniel Bovet”, Sapienza Università di Roma, Piazzale Aldo Moro, Rome, Italy

    Sonia Canterini

  3. Photobiology Unit, University of Dundee, Ninewells Hospital and Medical School, Dundee, DD1 9SY, UK

    Alessia Baseggio Conrado

  4. Dipartimento di Scienze Cardiovascolari, Respiratorie, Nefrologiche, Anestesiologiche e Geriatriche, Sapienza Università di Roma, Piazzale Aldo Moro, Rome, Italy

    Pina Giarrusso

Authors
  1. Elisabetta Capuozzo
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  2. Alessandra Giorgi
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  3. Sonia Canterini
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  4. Alessia Baseggio Conrado
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  5. Pina Giarrusso
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  6. Maria Eugenia Schininà
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  7. Mario Fontana
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Corresponding author

Correspondence to Elisabetta Capuozzo .

Editor information

Editors and Affiliations

  1. Department of Life Sciences, University of Seoul, Seoul, South Korea

    Dong-Hee Lee  & Ha Won Kim  & 

  2. College of Medicine, University of South Alabama, Mobile, Alabama, USA

    Stephen W. Schaffer

  3. Department of Developmental Neurobiology, NY State Institute for Basic Research in Developmental Disabilities, New York, USA

    Eunkyue Park

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Capuozzo, E. et al. (2017). A Proteomic Approach to Study the Effect of Thiotaurine on Human Neutrophil Activation. In: Lee, DH., Schaffer, S.W., Park, E., Kim, H.W. (eds) Taurine 10. Advances in Experimental Medicine and Biology, vol 975. Springer, Dordrecht. https://doi.org/10.1007/978-94-024-1079-2_44

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