The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Polysulfides Link H 2 S to Protein Thiol Oxidation
Open accessAbstract
AIMS: Hydrogen sulfide (H2S) is suggested to act as a gaseous signaling molecule in a variety of physiological processes. Its molecular mechanism of action was proposed to involve protein S-sulfhydration, that is, conversion of cysteinyl thiolates (Cys-S(-)) to persulfides (Cys-S-S(-)). A central and unresolved question is how H2S-that is, a molecule with sulfur in its lowest possible oxidation state (-2)-can lead to oxidative thiol modifications. RESULTS: Using the lipid phosphatase PTEN as a model protein, we find that the "H2S donor" sodium hydrosulfide (NaHS) leads to very rapid reversible oxidation of the enzyme in vitro. We identify polysulfides formed in NaHS solutions as the oxidizing species, and present evidence that sulfane sulfur is added to the active site cysteine. Polysulfide-mediated oxidation of PTEN was induced by all "H2S donors" tested, including sodium sulfide (Na2S), gaseous H2S, and morpholin-4-ium 4-methoxyphenyl(morpholino) phosphinodithioate (GYY4137). Moreover, we show that polysulfides formed in H2S solutions readily modify PTEN inside intact cells. INNOVATION: Our results shed light on the previously unresolved question of how H2S leads to protein thiol oxidation, and suggest that polysulfides formed in solutions of H2S mediate this process. CONCLUSION: This study suggests that the effects that have been attributed to H2S in previous reports may in fact have been mediated by polysulfides. It also supports the notion that sulfane sulfur rather than sulfide is the actual in vivo agent of H2S signaling.
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Cites
NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638
Physiological Implications of Hydrogen Sulfide: A Whiff Exploration That Blossomed
Wang, R. (2012) · Physiological Reviews · doi:10.1152/physrev.00017.2011 · Cited by 1,939
H 2 S Signals Through Protein S-Sulfhydration
Mustafa, A. K., Gadalla, M. M., Sen, N., Kim, S., Mu, W., Gazi, S. K., Barrow, R. K., Yang, G., Wang, R., & Snyder, S. H. (2009) · Science Signaling · doi:10.1126/scisignal.2000464 · Cited by 1,231
Reversible Inactivation of the Tumor Suppressor PTEN by H2O2
Lee, S.-R., Yang, K.-S., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,057
Hanson, G. T., Aggeler, R., Oglesbee, D., Cannon, M., Capaldi, R. A., Tsien, R. Y., & Remington, S. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312846200 · Cited by 988
3-Mercaptopyruvate Sulfurtransferase Produces Hydrogen Sulfide and Bound Sulfane Sulfur in the Brain
Shibuya, N., Tanaka, M., Yoshida, M., Ogasawara, Y., Togawa, T., Ishii, K., & Kimura, H. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2253 · Cited by 919
Real-time imaging of the intracellular glutathione redox potential
Gutscher, M., Pauleau, A.-L., Marty, L., Brach, T., Wabnitz, G. H., Samstag, Y., Meyer, A. J., & Dick, T. P. (2008) · Nature Methods · doi:10.1038/nmeth.1212 · Cited by 894
Self-citationHydrogen sulfide is an endogenous stimulator of angiogenesis
Papapetropoulos, A., Pyriochou, A., Altaany, Z., Yang, G., Marazioti, A., Zhou, Z., Jeschke, M. G., Branski, L. K., Herndon, D. N., Wang, R., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908047106 · Cited by 862
H2S signalling through protein sulfhydration and beyond
Paul, B. D., & Snyder, S. H. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3391 · Cited by 853
Li, L., Whiteman, M., Guan, Y. Y., Neo, K. L., Cheng, Y., Lee, S. W., Zhao, Y., Baskar, R., Tan, C.-H., & Moore, P. K. (2008) · Circulation · doi:10.1161/circulationaha.107.753467 · Cited by 839
Cited by
Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520
Chemical Biology of H2S Signaling through Persulfidation
Filipovic, M. R., Zivanovic, J., Alvarez, B., & Banerjee, R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00205 · Cited by 1,046
Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling
Ida, T., Sawa, T., Ihara, H., Tsuchiya, Y., Watanabe, Y., Kumagai, Y., Suematsu, M., Motohashi, H., Fujii, S., Matsunaga, T., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321232111 · Cited by 934
Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways
Mishanina, T. V., Libiad, M., & Banerjee, R. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1834 · Cited by 615
Physiological roles of hydrogen sulfide in mammalian cells, tissues, and organs
Cirino, G., Szabo, C., & Papapetropoulos, A. (2023) · Physiological Reviews · doi:10.1152/physrev.00028.2021 · Cited by 553
Metadata
- Authors
- Greiner, R., Pálinkás, Z., Bäsell, K., Becher, D., Antelmann, H., Nagy, P., & Dick, T. P.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2013-11-20
- Volume
- 19
- Issue
- 15
- Pages
- 1749-1765
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2067469839
- Cited by
- 468
- References
- 44
- FWCI
- 18.36
- Type
- journal article
- Language
- en
- Open access
- green
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