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.
Similar content being viewed by others
References
Mansoor MA, Svardal AM, Ueland PM (1992) Determination of the in vivo redox status of cysteine, cysteinylglycine, homocysteine, and glutathione in human plasma. Anal Biochem 200:18–29
Ramakrishnan S, Sulochana KN, Lakshmi S, Selvi R, Angayarkanni K (2006) Biochemistry of homocysteine in health and diseases. Indian J Biochem Biophys 43:275–283
Perła-Kajan J, Twardowski T, Jakubowski H (2007) Mechanisms of homocysteine toxicity in humans. Amino Acids 32:561–572
Zou CG, Banerjee R (2005) Homocysteine and redox signaling. Antioxid Redox Signal 7:47–59
Medina M, Urdiales JL, Amores-Sanchez MI (2001) Roles of homocysteine in cell metabolism: old and new functions. Eur J Biochem 268:3871–3882
Olsen KR (2009) Is hydrogen sulfide a circulating “gasotransmitter” in vertebrate blood? BBA 1787:856–863
Zhao W, Zhang J, Lu Y, Wang R (2001) The vasorelaxant effect of H(2)S as a novel endogenous gaseous K(ATP) channel opener. EMBO J 20:6008–6016
Deplanecke B, Gaskins HR (2003) Hydrogen sulphide induces serum-independent cell cycle entry in nontransformed rat intestinal epithelial cells. FASEB J 17:1310–1312
Wachowicz B (1984) Adenine nucleotides in thrombocytes of birds. Cell Biochem Funct 2:167–170
Kang SS, Wong PW, Malinow MR (1992) Hyperhomocyst(e)inemia as a risk factor for occlusive vascular disease. Annu Rev Nutr 12:279–289
Lentz SR, Haynes WG (2004) Homocysteine: it is a clinically important cardiovascular risk factor? Clev Clin J Med 71:729–734
Olas B, Kedzierska M, Wachowicz B (2008) Comparative studies on homocysteine and its metabolite-homocysteine thiolactone action in blood platelets in vitro. Platelets 19:520–527
Sibrian-Vazquez M, Escobedo JO, Lim S, Samoei GK, Strongin RM (2010) Homocystamides promote free-radical and oxidative damage to proteins. Proc Natl Acad Sci USA 107:551–554
Malinowska J, Babicz K, Olas B, Stochmal S, Oleszek W (2012) Aronia melanocarpa extract suppresses biotoxicity of homocysteine and its metabolite on hemostatic activity of fibrinogen and plasma. Nutrition 28:793–798
Chelchowska M, Ambroszkiewicz J, Klemarczyk W, Gajewska J, Oltarzewski M, Laskowska-Klita T (2010) Influence of vegetarian diet on serum values of homocysteine and total antioxidant status in children. Pol Merkur Lekarski 29:177–180
Glowacki R, Jakubowski H (2004) Cross-talk between Cys34 and lysine residues in human serum albumin revealed by N-homocysteinylation. J Biol Chem 279:10846–10871
Leoncini G, Bruzzese D, Signorello MG (2007) A role for PLCγ2 in platelet activation by homocysteine. J Cell Biochem 100:1255–1265
Leoncini G, Bruzzese D, Signorello MG (2006) Activation of p38MAPKinase/cPLA2 pathway in homocysteine treated platelets. J Thromb Haemost 4:209–216
Christian F, Albu E, Zamosteanu N, Jaba IM, Silion M, Jerca L, Gheorghita N, Mungui OC (2010) Hyperhomocysteinemia’s effect on antioxidant capacity in rats. Cent Eur J Med 5:620–626
McCully K, Ragsdale B (1970) Production of arteriosclerosis by homocysteinemia. Am J Pathol 61:1–8
Stamler J, Osborne J, Jaraki O, Rabbani LE, Mullins M, Single D, Loscalzo J et al (1993) Adverse vascular effects of homocysteine are modulated by endothelium-derived relaxing factor and related oxides of nitrogen. J Clin Invest 91:308–318
Schafer FQ, Beuttner GR (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30:1191–1212
Sun WH, Liu F, Chen Y, Zhu YC (2012) Hydrogen sulfide decreases the levels of ROS by inhibiting mitochondrial complex IV and increasing SOD activities in cardiomyocytes under ischemia/reperfusion. Biochem Biohys Res Commun 421:164–169
Morel A, Malinowska J, Olas B (2012) Antioxidative properties of hydrogen sulfide may involve in its antiadhesive action on blood platelets. Clin Biochem 45:1678–1682
Yan SK, Chang T, Wang H, Wu L, Wang R, Meng QH (2006) Effects of hydrogen sulfide on homocysteine-induced oxidative stress in vascular smooth muscle cell. Biochem Biophys Res Commun 351:485–491
Chang L, Geng B, Yu F, Zhao J, Jiang H, Du J, Tang C (2008) Hydrogen sulfide inhibits myocardial injury induced by homocysteine in rats. Amino Acids 34:573–585
Predmore BL, Lefer DJ, Gojon G (2012) Hydrogen sulfide in biochemistry and medicine. Antioxid Redox Signal 17:119–140
Geng B, Chang L, Pan C, Qi Y, Zhao J, Pang Y, Du J, Tang C (2004) Endogenous hydrogen sulfide regulation of myocardial injury induced by isoproterenol. Biochem Biophys Res Commun 318:756–763
Chai W, Wang Y, Lin JY, Sun XD, Yao LN, Yang YH, Zhao H, Jiang W, Gao CJ, Ding Q (2012) Exogenous hydrogen sulphide protects against traumatic hemorrhagic shock via attenuation of oxidative stress. J Surg 176:210–219
Kimura Y, Kimura H (2004) Hydrogen sulfide protects neurons from oxidative stress. FASEB J 18:1165–1167
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.
Conflict of interest
None to declare.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
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
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11010-015-2364-8