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Hydrogen sulfide decreases the plasma lipid peroxidation induced by homocysteine and its thiolactone

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Abstract

Hydrogen sulfide (H2S) has been investigated widely in recent years. H2S plays a variety of roles in different biological systems, including cardiovascular system. It is the final product of amino acids metabolism, which contains sulfur—cysteine and homocysteine (Hcy). In human plasma, there are several various forms of homocysteine: free Hcy, protein-bound Hcy (S-linked, and N-linked), and homocysteine thiolactone (HTL). Our previous works have shown that both Hcy in the reduced form and its thiolactone may modify fibrinolysis, coagulation process, and biological activity of blood platelets. Moreover, we have observed that HTL, like its precursor—Hcy stimulated the generation of superoxide anion radicals (O −•2 ) in blood platelets. The aim of our study in vitro was to establish the influence of sodium hydrosulfide (NaHS, as a fast-releasing H2S donor; at tested concentrations: 10–1000 µM) on the plasma lipid peroxidation induced by the reduced Hcy (at final concentrations of 0.01–1 mM) and HTL (at final concentrations of 0.1–1 µM). Our results indicate that 10 and 100 µM NaHS decreased the lipid peroxidation in plasma treated with 1 mM Hcy or 1 µM HTL (when NaHS and Hcy/HTL were added to plasma together). The protective effect of 10 and 100 µM NaHS against the lipid peroxidation in plasma preincubated with 1 mM Hcy or 1 µM HTL was also observed. Considering the data presented in this study, we suggest that the lipid peroxidation (induced by different forms of homocysteine) may be reduced by hydrogen sulfide.

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Acknowledgments

This work was supported by grant 506/1136 from University of Lodz. Special thanks goes to P. Brodek, A. Krysztofiak, K. Makaruk, and J. Tadeusiewicz (Department of General Biochemistry, University of Lodz) for skilled technical assistance.

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Correspondence to Beata Olas.

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Olas, B., Kontek, B. Hydrogen sulfide decreases the plasma lipid peroxidation induced by homocysteine and its thiolactone. Mol Cell Biochem 404, 39–43 (2015). https://doi.org/10.1007/s11010-015-2364-8

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