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Taurine 9 pp 41–51Cite as

Oxidation of Hypotaurine and Cysteine Sulfinic Acid by Peroxidase-generated Reactive Species

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 803))

Abstract

Hypotaurine (HTAU) and cysteine sulfinic acid (CSA) are the metabolic intermediates in the mammalian pathway leading from cysteine to taurine. Strong evidence has been presented that the formation of taurine (TAU) and cysteic acid (CA) is the result of the interaction of both sulfinates with various oxidizing agents that may be present in biological systems. The purpose of the present study is to investigate the oxidation of sulfinates, HTAU and CSA, by peroxidase-generated reactive species. Reactive nitrogen and oxygen species can be produced during the process of nitrite oxidation catalyzed by heme peroxidases, such as horseradish peroxidase (HRP) or myeloperoxidase, in the presence of hydrogen peroxide (H2O2). Nitrite is the major end product of nitric oxide (NO) metabolism. Oxidation of nitrite by such mechanisms could be important at sites of inflammatory processes. The formation of reactive nitrogen species (RNS) via peroxidase-catalyzed oxidation of nitrite could represent an additional mechanism of the formation of taurine. The oxidation of the sulfinates, HTAU and CSA, by HRP/H2O2/nitrite system has been evaluated by monitoring the oxygen consumption and the production of the corresponding sulfonates, TAU and CA. Moreover, the effect of HTAU and CSA, on nitrotyrosine formation by HRP/H2O2/nitrite system has been studied. During the HRP/H2O2-dependent oxidation of tyrosine, tyrosyl radicals are formed. The results provide evidence that sulfinates inhibit nitrotyrosine formation not only by scavenging RNS but also by reducing the peroxidase-generated tyrosyl radical.

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Abbreviations

HRP:

Horseradish peroxidase

HTAU:

Hypotaurine

CSA:

Cysteine sulfinic acid

TAU:

Taurine

CA:

Cysteic acid

Tyr:

Tyrosine

References

  • Aruoma OI, Halliwell B, Hoey BM, Butler J (1988) The antioxidant action of taurine, hypotaurine and their metabolic precursor. Biochem J 256:251–255

    CAS  PubMed Central  PubMed  Google Scholar 

  • Baseggio Conrado A, D’Angelantonio M, Torreggiani A, Pecci L, Fontana M (2014) Reactivity of hypotaurine and cysteine sulfinic acid toward carbonate radical anion and nitrogen dioxide as explored by the peroxidase activity of Cu, Zn-superoxide dismutase and by pulse radiolysis. Free Radic Res 48:1300–1310

    Article  CAS  PubMed  Google Scholar 

  • Beckmann JS, Ye YZ, Anderson PG, Chen J, Accavitti MA, Tarpey MM, White CR (1994) Extensive nitration of protein tyrosines in human atherosclerosis detected by immunohistochemistry. Biol Chem Hoppe Seyler 375:81–88

    Article  CAS  PubMed  Google Scholar 

  • Brennan ML, Wu W, Fu X, Shen Z, Song W, Frost H, Vadseth C, Narine L, Lenkiewicz E, Borchers MT, Lusis AJ, Lee JJ, Lee NA, Abu-Soud HM, Ischiropoulos H, Hazen SL (2002) A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J Biol Chem 277:17415–17427

    Article  CAS  PubMed  Google Scholar 

  • Casella L, Monzani E, Roncone R, Nicolis S, Sala A, De Riso A (2002) Formation of reactive nitrogen species at biologic heme centers: a potential mechanism of nitric oxide-dependent toxicity. Environ Health Perspect 110:709–711

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Ducrocq C, Blanchard B, Pignatelli B, Ohshima H (1999) Peroxynitrite: an endogenous oxidizing and nitrating agent. Cell Mol Life Sci 55:1068–1077

    Article  CAS  PubMed  Google Scholar 

  • Eiserich JP, Baldus S, Brennan ML, Ma W, Zhang C, Tousson A, Castro L, Lusis AJ, Nauseef WM, White CR, Freeman BA (2002) Myeloperoxidase, a leukocyte-derived vascular NO oxidase. Science 296:2391–2394

    Article  CAS  PubMed  Google Scholar 

  • Farrell AJ, Blake DR, Palmer RMJ, Moncada S (1992) Increased concentrations of nitrite in synovial fluid and serum samples suggest increased nitric oxide synthesis in rheumatic diseases. Ann Rheum Dis 51:1219–1222

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Fellman JH, Green TR, Eicher AL (1987) The oxidation of hypotaurine to taurine: bis-aminoethyl-α-disulfone, a metabolic intermediate in mammalian tissue. Adv Exp Med Biol 217:39–48

    Article  CAS  PubMed  Google Scholar 

  • Fontana M, Pecci L, Duprè S, Cavallini D (2004) Antioxidant properties of sulfinates: protective effect of hypotaurine on peroxynitrite-dependent damage. Neurochem Res 29:111–116

    Article  CAS  PubMed  Google Scholar 

  • Fontana M, Amendola D, Orsini E, Boffi A, Pecci L (2005) Oxidation of hypotaurine and cysteine sulphinic acid by peroxynitrite. Biochem J 389:233–240

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Fontana M, Duprè S, Pecci L (2006) The reactivity of hypotaurine and cysteine sulfinic acid with peroxynitrite. Adv Exp Med Biol 583:15–24

    Article  CAS  PubMed  Google Scholar 

  • Fontana M, Giovannitti F, Pecci L (2008) The protective effect of hypotaurine and cysteine sulphinic acid on peroxynitrite-mediated oxidative reactions. Free Radic Res 42:320–330

    Article  CAS  PubMed  Google Scholar 

  • Gaston B, Reilly J, Drazen JM, Fackler J, Ramdey P, Arnelle D, Mullins ME, Sugarbaker DJ, Chee C, Singel DJ, Loscalzo J, Stamler JS (1993) Endogenous nitrogen oxides and bronchodilator S-nitrosothiols in human airways. Proc Natl Acad Sci U S A 90:10957–10961

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Gaut JP, Byun J, Tran HD, Lauber WM, Carroll JA, Hotchkiss RS, Belaaouaj A, Heinecke JW (2002) Myeloperoxidase produces nitrating oxidants in vivo. J Clin Invest 109:1311–1319

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Goldstein S, Czapski G, Lind J, Merényi G (2000) Tyrosine nitration by simultaneous generation of •NO and O2 •– under physiological conditions. How the radicals do the job. J Biol Chem 275:3031–3036

    Article  CAS  PubMed  Google Scholar 

  • Green LC, Wagner DA, Glogowski J, Skipper PL, Wishnok JS, Tannenbaum SR (1982) Analysis of nitrate, nitrite, and [15N] nitrate in biological fluids. Anal Biochem 126:131–138

    Article  CAS  PubMed  Google Scholar 

  • Harman LS, Mottley C, Mason RP (1984) Free radical metabolites of L-cysteine oxidation. J Biol Chem 259:5609–5611

    Google Scholar 

  • Hildebrandt AG, Roots I (1975) Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes. Arch Biochem Biophys 171:385–397

    Article  CAS  Google Scholar 

  • Hirschberger LL, de la Rosa J, Stipanuk MH (1985) Determination of cysteinesulfinate, hypotaurine and taurine in physiological samples by reversed-phase high-performance liquid chromatography. J Chromatogr B 343:303–313

    Article  CAS  Google Scholar 

  • Huxtable RJ (1992) Physiological actions of taurine. Physiol Rev 72:101–163

    CAS  PubMed  Google Scholar 

  • Ischiropoulos H, Zhu L, Chen J, Tsai M, Martin JC, Smith CD, Beckman JS (1992) Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase. Arch Biochem Biophys 298:431–437

    Article  CAS  PubMed  Google Scholar 

  • Leone AM, Francis PL, Rhodes P, Moncada S (1994) A rapid and simple method for the measurement of nitrite and nitrate in plasma by high performance capillary electrophoresis. Biochem Biophys Res Commun 200:951–957

    Article  CAS  PubMed  Google Scholar 

  • Pecci L, Costa M, Montefoschi G, Antonucci A, Cavallini D (1999) Oxidation of hypotaurine to taurine with photochemically generated singlet oxygen: the effect of azide. Biochem Biophys Res Commun 254:661–665

    Article  CAS  PubMed  Google Scholar 

  • Reiter CD, Teng RJ, Beckman JS (2000) Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite. J Biol Chem 275:32460–32466

    Article  CAS  PubMed  Google Scholar 

  • Sampson JB, Ye YZ, Rosen H, Beckman JS (1998) Myeloperoxidase and horseradish peroxidase catalyze tyrosine nitration in proteins from nitrite and hydrogen peroxide. Arch Biochem Biophys 356:207–213

    Article  CAS  PubMed  Google Scholar 

  • Stipanuk MH, Ueki I (2011) Dealing with methionine/homocysteine sulfur: cysteine metabolism to taurine and inorganic sulfur. J Inherit Metab Dis 34:17–32

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Torre D, Ferrario G, Speranza F, Orani A, Fiori GP, Zeroli C (1996) Serum concentrations of nitrite in patients with HIV-1 infection. J Clin Pathol 49:574–576

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Ueda T, Maekawa T, Sadamitsu D, Oshita S, Ogino K, Nakamura K (1995) The determination of nitrite and nitrate in human blood plasma by capillary zone electrophoresis. Electrophoresis 16:1002–1004

    Article  CAS  PubMed  Google Scholar 

  • van der Vliet A, Eiserich JP, Halliwell B, Cross CE (1997) Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. J Biol Chem 272:7617–7625

    Article  PubMed  Google Scholar 

  • Wu W, Chen Y, Hazen SL (1999) Eosinophil peroxidase nitrates protein tyrosyl residues. J Biol Chem 274:25933–25944

    Article  CAS  PubMed  Google Scholar 

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Authors and Affiliations

  1. Dipartimento di Scienze Biochimiche, Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185, Rome, Italy

    Alessia Baseggio Conrado, Laura Pecci, Elisabetta Capuozzo & Mario Fontana

Authors
  1. Alessia Baseggio Conrado
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  2. Laura Pecci
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  3. Elisabetta Capuozzo
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  4. Mario Fontana
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Corresponding author

Correspondence to Mario Fontana .

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Editors and Affiliations

  1. Chair of Immunology, Medical College Jagiellonian University, Krakow, Poland

    Janusz Marcinkiewicz

  2. Department of Pharmacology, College of Medicine University of South Alabama, Mobile, Alabama, USA

    Stephen W. Schaffer

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Baseggio Conrado, A., Pecci, L., Capuozzo, E., Fontana, M. (2015). Oxidation of Hypotaurine and Cysteine Sulfinic Acid by Peroxidase-generated Reactive Species. In: Marcinkiewicz, J., Schaffer, S. (eds) Taurine 9. Advances in Experimental Medicine and Biology, vol 803. Springer, Cham. https://doi.org/10.1007/978-3-319-15126-7_4

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