Faculty of Chemistry Repository - Cherry
University of Belgrade - Faculty of Chemistry
    • English
    • Српски
    • Српски (Serbia)
  • English 
    • English
    • Serbian (Cyrillic)
    • Serbian (Latin)
  • Login
View Item 
  •   Cherry
  • Hemijski fakultet
  • Publikacije
  • View Item
  •   Cherry
  • Hemijski fakultet
  • Publikacije
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation

Thumbnail
2016
1923.pdf (1.333Mb)
Authors
Wedmann, Rudolf
Onderka, Constantin
Wei, Shengwei
Szijarto, Istvan Andras
Miljković, Jan Lj
Mitrović, Aleksandra D.
Lange, Mike
Savitsky, Sergey
Yadav, Pramod Kumar
Torregrossa, Roberta
Harrer, Ellen G.
Harrer, Thomas
Ishii, Isao
Gollasch, Maik
Wood, Mark E.
Galardon, Erwan
Xian, Ming
Whiteman, Matthew
Banerjee, Ruma
Filipović, Miloš R.
Article (Published version)
Metadata
Show full item record
Abstract
Hydrogen sulfide (H2S) has emerged as a signalling molecule capable of regulating several important physiological functions such as blood pressure, neurotransmission and inflammation. The mechanisms behind these effects are still largely elusive and oxidative posttranslational modification of cysteine residues (protein persulfidation or S-sulfhydration) has been proposed as the main pathway for H2S-induced biological and pharmacological effects. As a signalling mechanism, persulfidation has to be controlled. Using an improved tag-switch assay for persulfide detection we show here that protein persulfide levels are controlled by the thioredoxin system. Recombinant thioredoxin showed an almost 10-fold higher reactivity towards cysteine persulfide than towards cystine and readily cleaved protein persulfides as well. This reaction resulted in H2S release suggesting that thioredoxin could be an important regulator of H2S levels from persulfide pools. Inhibition of the thioredoxin system cau...sed an increase in intracellular persulfides, highlighting thioredoxin as a major protein depersulfidase that controls H2S signalling. Finally, using plasma from HIV-1 patients that have higher circulatory levels of thioredoxin, we could prove depersulfidase role in vivo.

Source:
Chemical Science, 2016, 7, 5, 3414-3426
Publisher:
  • Royal Soc Chemistry, Cambridge
Funding / projects:
  • Medical Research Council [MR/M022706/1]
  • French State in the frame of the Investments for the future Programme IdEx Bordeaux [ANR-10-IDEX-03-02]
  • Deutsche Forschungsgemeinschaft
  • Dr Werner Jackstadt-Stiftung
  • American Heart Association [14POST18760003]
  • Friedrich-Alexander University within the Emerging Field Initiative (MRIC)
  • Brian Ridge Scholarship
  • National Institutes of Health [HL58984, GM112455, NIH R01HL116571]
Note:
  • Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3543

DOI: 10.1039/c5sc04818d

ISSN: 2041-6520

PubMed: 27170841

WoS: 000374859300056

Scopus: 2-s2.0-84966356269
[ Google Scholar ]
117
107
URI
https://cherry.chem.bg.ac.rs/handle/123456789/1925
Collections
  • Publikacije
Institution/Community
Hemijski fakultet
TY  - JOUR
AU  - Wedmann, Rudolf
AU  - Onderka, Constantin
AU  - Wei, Shengwei
AU  - Szijarto, Istvan Andras
AU  - Miljković, Jan Lj
AU  - Mitrović, Aleksandra D.
AU  - Lange, Mike
AU  - Savitsky, Sergey
AU  - Yadav, Pramod Kumar
AU  - Torregrossa, Roberta
AU  - Harrer, Ellen G.
AU  - Harrer, Thomas
AU  - Ishii, Isao
AU  - Gollasch, Maik
AU  - Wood, Mark E.
AU  - Galardon, Erwan
AU  - Xian, Ming
AU  - Whiteman, Matthew
AU  - Banerjee, Ruma
AU  - Filipović, Miloš R.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1925
AB  - Hydrogen sulfide (H2S) has emerged as a signalling molecule capable of regulating several important physiological functions such as blood pressure, neurotransmission and inflammation. The mechanisms behind these effects are still largely elusive and oxidative posttranslational modification of cysteine residues (protein persulfidation or S-sulfhydration) has been proposed as the main pathway for H2S-induced biological and pharmacological effects. As a signalling mechanism, persulfidation has to be controlled. Using an improved tag-switch assay for persulfide detection we show here that protein persulfide levels are controlled by the thioredoxin system. Recombinant thioredoxin showed an almost 10-fold higher reactivity towards cysteine persulfide than towards cystine and readily cleaved protein persulfides as well. This reaction resulted in H2S release suggesting that thioredoxin could be an important regulator of H2S levels from persulfide pools. Inhibition of the thioredoxin system caused an increase in intracellular persulfides, highlighting thioredoxin as a major protein depersulfidase that controls H2S signalling. Finally, using plasma from HIV-1 patients that have higher circulatory levels of thioredoxin, we could prove depersulfidase role in vivo.
PB  - Royal Soc Chemistry, Cambridge
T2  - Chemical Science
T1  - Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation
VL  - 7
IS  - 5
SP  - 3414
EP  - 3426
DO  - 10.1039/c5sc04818d
UR  - Kon_3044
ER  - 
@article{
author = "Wedmann, Rudolf and Onderka, Constantin and Wei, Shengwei and Szijarto, Istvan Andras and Miljković, Jan Lj and Mitrović, Aleksandra D. and Lange, Mike and Savitsky, Sergey and Yadav, Pramod Kumar and Torregrossa, Roberta and Harrer, Ellen G. and Harrer, Thomas and Ishii, Isao and Gollasch, Maik and Wood, Mark E. and Galardon, Erwan and Xian, Ming and Whiteman, Matthew and Banerjee, Ruma and Filipović, Miloš R.",
year = "2016",
abstract = "Hydrogen sulfide (H2S) has emerged as a signalling molecule capable of regulating several important physiological functions such as blood pressure, neurotransmission and inflammation. The mechanisms behind these effects are still largely elusive and oxidative posttranslational modification of cysteine residues (protein persulfidation or S-sulfhydration) has been proposed as the main pathway for H2S-induced biological and pharmacological effects. As a signalling mechanism, persulfidation has to be controlled. Using an improved tag-switch assay for persulfide detection we show here that protein persulfide levels are controlled by the thioredoxin system. Recombinant thioredoxin showed an almost 10-fold higher reactivity towards cysteine persulfide than towards cystine and readily cleaved protein persulfides as well. This reaction resulted in H2S release suggesting that thioredoxin could be an important regulator of H2S levels from persulfide pools. Inhibition of the thioredoxin system caused an increase in intracellular persulfides, highlighting thioredoxin as a major protein depersulfidase that controls H2S signalling. Finally, using plasma from HIV-1 patients that have higher circulatory levels of thioredoxin, we could prove depersulfidase role in vivo.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Chemical Science",
title = "Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation",
volume = "7",
number = "5",
pages = "3414-3426",
doi = "10.1039/c5sc04818d",
url = "Kon_3044"
}
Wedmann, R., Onderka, C., Wei, S., Szijarto, I. A., Miljković, J. L., Mitrović, A. D., Lange, M., Savitsky, S., Yadav, P. K., Torregrossa, R., Harrer, E. G., Harrer, T., Ishii, I., Gollasch, M., Wood, M. E., Galardon, E., Xian, M., Whiteman, M., Banerjee, R.,& Filipović, M. R.. (2016). Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation. in Chemical Science
Royal Soc Chemistry, Cambridge., 7(5), 3414-3426.
https://doi.org/10.1039/c5sc04818d
Kon_3044
Wedmann R, Onderka C, Wei S, Szijarto IA, Miljković JL, Mitrović AD, Lange M, Savitsky S, Yadav PK, Torregrossa R, Harrer EG, Harrer T, Ishii I, Gollasch M, Wood ME, Galardon E, Xian M, Whiteman M, Banerjee R, Filipović MR. Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation. in Chemical Science. 2016;7(5):3414-3426.
doi:10.1039/c5sc04818d
Kon_3044 .
Wedmann, Rudolf, Onderka, Constantin, Wei, Shengwei, Szijarto, Istvan Andras, Miljković, Jan Lj, Mitrović, Aleksandra D., Lange, Mike, Savitsky, Sergey, Yadav, Pramod Kumar, Torregrossa, Roberta, Harrer, Ellen G., Harrer, Thomas, Ishii, Isao, Gollasch, Maik, Wood, Mark E., Galardon, Erwan, Xian, Ming, Whiteman, Matthew, Banerjee, Ruma, Filipović, Miloš R., "Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation" in Chemical Science, 7, no. 5 (2016):3414-3426,
https://doi.org/10.1039/c5sc04818d .,
Kon_3044 .

DSpace software copyright © 2002-2015  DuraSpace
About CHERRY - CHEmistry RepositoRY | Send Feedback

re3dataOpenAIRERCUB
 

 

All of DSpaceInstitutions/communitiesAuthorsTitlesSubjectsThis institutionAuthorsTitlesSubjects

Statistics

View Usage Statistics

DSpace software copyright © 2002-2015  DuraSpace
About CHERRY - CHEmistry RepositoRY | Send Feedback

re3dataOpenAIRERCUB