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Antioxidant effects of sulfane sulfur


Authors: R. Hyšpler 1,2;  A. Tichá 1,2;  Z. Zadák 2
Authors‘ workplace: Ústav klinické biochemie a diagnostiky, Fakultní nemocnice Hradec Králové 1;  Centrum pro vývoj a výzkum, Fakultní nemocnice Hradec Králové 2
Published in: Klin. Biochem. Metab., 30, 2022, No. 3, p. 79-82

Overview

Sulfane sulfur is a reactive, divalent sulfur atom bonded to another sulfur. It modifies cysteine residues in proteins and thus changes enzyme activities. Also, it may be bound to glutathione and this greatly increases its antioxidative properties. Analytical methods used for the determination of sulfane sulfur are discussed and our developed method using an extractive alkylation technique is mentioned. The sulfane sulfur donor compounds are described and categorized. The potential use and future perspectives of this monoelemental antioxidant are summarised and discussed.

Keywords:

antioxidant – sulfane sulfur – sulfate sulfur donor compounds


Sources

1. Abdolrasulnia, R., Wood, J. L. Transfer of persulfide sulfur from thiocystine to rhodanese. Biochim. Biophys. Acta, 1979, 567, 135-143.

2. Sorbo, B. Enzymic transfer of sulfur from mercaptopyruvate to sulfate or sulfinates. Biochim. Biophys., 1957, 24, 324-329.

3. Ogasawara, Y., Isoda, S., Tanabe, S. Tissue and subcelullar distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat. Biol. Pharm. Bull., 1994, 17, 1535-1542.

4. Kotke, S., Ogasawara, Y. Sulfur Atom in its Bound State Is a Unique Element Involved in Physiological Functions in Mammals. Molecules, 2016, 21, E1753.

5. Koj, A., Frendo, J. The aktivity of cysteine desulphhydrase and rhodanase in animal tissues. Acta Biochim. Pol., 1962, 9, 373-379.

6. Toohey, J. Sulfur singaling: is the agent sulfide or sulfane? Anal. Biochem., 2011, 413, 1-7.

7. Iciek, M., Wlodek, L. Biosynthesis and biological properties of compounds containing highly reactive, reduced sulfane sulfur. Pol. J Pharmacol., 2001, 53, 215-225.

8. Sawa, T., Ono, K., Tsutsuki, H., et al. Reactive cysteine persulphides: occurrence, biosynthesis, antioxidant aktivity, methodologies, and bacterial persulphide signalling. Adv. Microb. Physiol., 2018, 72, 1-28.

9. Parker-Cote, J., Rizer, J., Vakkalanka, J., et al. Challenges in the diagnosis of acute cyanide poisoning. Clin. Toxicol., 2018, 56, 609-617.

10. Everett, S., Folkes, L., Wardman, P., et al. Freeradical repair by a novel perthiol: reversible hydrogen transfer and perthiyl radical formation. Free Radic. Res., 1994, 20, 387-400.

11. Yang, G., Wu, L., Wang, R. Pro-apoptotic effect of endogenous H2S on human aorta smooth muscle cells. FASEB J, 2006, 20, 553-555.

12. Baskar, R., Bian, J. Hydrogen sulfide gas has cell growth regulatory role. Eur. J Pharmacol., 2011, 656, 5-9.

13. Katsouda, A., Bibli, S., Pyriouchou, A., et al. Regulation and role of endogenously produced hydrogen sulphide in angiogenesis. Pharmacol. Res., 2016, 113, 175-185.

14. Zhang, H., Liu, S., Tang, X., et al. H2S Attenuates LPS-induced acute lung injury by reducing oxidative/ nitrative stress and inflammation. Cell Physiol. Biochem., 2016, 40, 1603-1612.

15. Drapala, A., Koszelewski, D., Tomasova, L., et al. Parenteral Na2S, a fast-releasing H2S donor, but not GYY4137, a slow-releasing H2S donor, lowers blood pressure in rats. Acta Biochim. Pol., 2017, 64, 561-566.

16. Feliers, D., Lee, H., Kasinath, B. Hydrogen sulfide in renal physiology and disease. Antioxid. Redox. Signal, 2016, 25, 720-731.

17. Beltowski, J., Wojcicka, G., Jamroz-Wisniewska, A. Hydrogen sulfide in the regulation of insulin secretion and insulin sensitivity: Implications for the pathogenesis and treatment of diabetes mellitus. Biochem. Pharmacol., 2018, 149, 60-76.

18. Toohey, J. Sulfur signaling: is the agent sulphide or sulfane? Anal. Biochem., 2011, 413, 1-7.

19. Akaike, T., Ida, T., Wei, F., et al. Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. Nat. Commun., 2017, 8, 1177.

20. Ogasawara, Y., Ishii, K., Togawa, T., et al. Determination of bound sulfur in serum by gas dialysis/ high-performance liquid chromatography. Anal. Biochem., 1993, 215, 73-81.

21. Ran, M., Wang, T., Shao, M., et al. Sensitive method for reliable quantification of sulfane sulfur in biological samples. Anal. Chem., 2019, 91, 11981-11986.

22. Hyšpler, R., Tichá, A., Indrová, M., Zadák, Z., Hyšplerová, L., Gasparič, J., Churáček, J. A simple, optimized method for the determination of sulphide in whole blood by GC-MS as a marker of bowel fermentation processes. J Chromatography B, 2002, 770, 255-259.

23. Janáky, R., Varga, V., Hermann, A., Saransaari, P., Oja, S. Mechanisms of L-cysteine neurotoxicity. Neurochem. Res., 2000, 25, 1397-1405.

24. Patriarca, S., Furfaro, A., Domenicotti, C., Odetti, P., Cottalasso, D., Marinari, U., Pronzato, M., Traverso, N. Supplementation with N-acetylcysteine and taurine failed to restore glutathione content in oxidative stress. Biochim. Biophys. Acta, 2005, 1741, 48-54.

25. Jurkowska, H., Wróbel, M. N-acetyl-L-cysteine as a source of sulfane sulfur in astrocytoma and astrocyte cultures: correlations with cell proliferation. Amino Acids, 2008, 34, 231-237.

26. Ezerina, D., Takano, Y., Hanaoka, K., Urano, Y., Dick, T. N-Acetyl cysteine functions as a fast-acting antioxidant by triggering intracellular H2S and sulfane sulfur production. Cell. Chem. Biol., 2018, 25, 447-459. e4.

27. Citi, V., Martelli, A., Testai, L., Marino, A., Breschi, M., Calderone, V. Hydrogen sulphide releasing capacity of natural isothiocyanates: is it a reliable explanation for the multiple biological effects of Brassicaceae? Planta Med., 2014, 80, 610-613.

28. Jurkowska, H., Wróbel, M. Inhibition of human neuroblastoma cell proliferation by N-acetyl-L-cysteine as a result of increased sulfane sulfur level. Anticancer Res., 2018, 38, 5109-5113.

29. Bilska, A., Dudek, M., Iciek, M., Kwiecień, I., Sokolowska-Jezewicz, M., Filipek, B., Wlodek, L. Biological actions of lipoic acid associated with sulfane sulfur metabolism. Pharmacol. Rep., 2008, 60, 225-232.

30. Dudek, M., Bilska-Wilkosz, A., Knutelska, J., Mogiiski, S., Bednarski, M., Zygmunt, M., Iciek, M., Sapa, J., Bugajski, D., Filipek, B., Wlodek, L. Are anti-inflammatory properties of lipoic acid associated with the formation of hydrogen sulfide? Pharmacol. Rep., 2013, 65, 1018-1024.

31. Iciek, M., Bilska, A., Ksiazek, L., Srebro, Z., Wlodek, L. Allyl disulfide as donor and cyanide as acceptor of sulfane sulfur in the mouse tissues. Pharmacol. Rep., 2005, 57, 212-218.

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