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

Elisabetta Capuozzo (Lead / Corresponding author), Alessandra Giorgi, Sonia Canterini, Alessia Baseggio Conrado, Pina Giarrusso, Maria Eugenia Schininà, Mario Fontana

    Research output: Chapter in Book/Report/Conference proceedingConference contribution

    4 Citations (Scopus)
    172 Downloads (Pure)

    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.

    Original languageEnglish
    Title of host publicationTaurine 10
    EditorsDong-Hee Lee, Stephen W. Schaffer, Eunkyue Park, Ha Won Kim
    Place of PublicationDordrecht
    PublisherSpringer
    Pages563-571
    Number of pages9
    Volume975
    ISBN (Electronic)9789402410792
    ISBN (Print)9789402410778
    DOIs
    Publication statusPublished - 2017
    Event20th International Taurine Meeting: “Taurine and Brain Health” - Plaza Hotel, Seoul, Korea, Republic of
    Duration: 23 May 201627 May 2016
    http://taurine2016.org/register/2016_met/main.html

    Publication series

    Name Advances in Experimental Medicine and Biology
    PublisherSpringer
    Volume975
    ISSN (Print)0065-2598
    ISSN (Electronic)2214-8019

    Conference

    Conference20th International Taurine Meeting
    Abbreviated titleINTAM20
    CountryKorea, Republic of
    CitySeoul
    Period23/05/1627/05/16
    Internet address

    Keywords

    • Human neutrophils
    • Thiotaurine
    • Sulfhydration
    • Hydrogen sulfide
    • Inflammation

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  • Cite this

    Capuozzo, E., Giorgi, A., Canterini, S., Baseggio Conrado, A., Giarrusso, P., Schininà, M. E., & Fontana, M. (2017). A Proteomic Approach to Study the Effect of Thiotaurine on Human Neutrophil Activation. In D-H. Lee, S. W. Schaffer, E. Park, & H. W. Kim (Eds.), Taurine 10 (Vol. 975, pp. 563-571). ( Advances in Experimental Medicine and Biology ; Vol. 975). Springer . https://doi.org/10.1007/978-94-024-1079-2_44