Role of reactive nitrogen species in blood platelet functions

References

• Patel RP, McAndrew J, Sellak H, White CR, Jo H, Freeman BA, Darley-Usmar VM. Biological aspects of reactive nitrogen species. Biochim Biophys Acta 1999; 1411: 385–400
   PubMed Web of Science ®Google Scholar
• Ischiropoulos H, Gow A. Pathophysiological functions of nitric oxide-mediated protein modifications. Toxicology 2005; 208: 299–303
   PubMed Web of Science ®Google Scholar
• Hedin HLM, Fowler CJ. Further studies of the effects of diamide and hydrogen peroxide on calcium signaling in the human platelet. Methods Find Exp Clin Pharmacol 1999; 21: 321–325
   PubMedGoogle Scholar
• Iuliano L, Pedersen JZ, Pratico D, Rotilio G, Violi F. Role of hydroxyl radicals in the activation of human platelets. Eur J Biochem 1994; 15: 695–704
   Google Scholar
• Pignatelli P, Pulcinelli FM, Lenti L, Gazzaniga PP, Violi F. Hydrogen peroxide is involved in collagen  – induced platelet activation. Blood 1998; 91: 484–490
   PubMed Web of Science ®Google Scholar
• Schoene NW, Guidry CA. Genistein inhibits reactive oxygen species (ROS) production, shape change, and aggregation in rat platelets. Nutr Res 2000; 20: 47–57
   Web of Science ®Google Scholar
• Krotz F, Sohn HY, Pohl U. Reactive oxygen species, players in the platelet game. Arterioscler Thromb Vasc Biol 2004; 24: 1988–1996
   PubMed Web of Science ®Google Scholar
• Iuliano L, Colavita AR, Leo R, Practico D, Violi F. Oxygen free radicals and platelet activation. Free Rad Biol Med 1997; 22: 999–1006
   PubMed Web of Science ®Google Scholar
• Maresca M, Colao C, Leoncini G. Generation of hydrogen peroxide in resting and activated platelets. Cell Biochem Funct 1992; 10: 79–82
   PubMed Web of Science ®Google Scholar
• Salvemini D, Botting R. Modulation of platelet function by free radicals and free radicals scavengers. TIPS 1993; 14: 36–42
   PubMed Web of Science ®Google Scholar
• Del Principe D, Menichelli A, De Matteis W, Di Corpo ML, Di Giulio S, Finazzi-Agro AF. Hydrogen peroxide has a role in the aggregation of human platelets. FEBS 1985; 1: 142–149
   Google Scholar
• Del Principe D, Menichelli A, De Matteis W, Di Giulio S, Giordani M, Savini I, Finazzi Agro AF. Hydrogen peroxide is an intermediate in the platelet activation cascade triggered by collagen, but not by thrombin. Thromb Res 1991; 62: 365–371
   PubMed Web of Science ®Google Scholar
• Ambrosio G, Golino P, Pascucci I, Rosolowsky M, Campbell WB, DeClerck F, Tritto I, Chiariello M. Modulation of platelet function by reactive oxygen metabolites. Am J Physiol 1994; 267: 308–318
   Google Scholar
• Komiya T, Higurasahi K, Iizuka K, Mizuno Y. A novel free radical scavenger, nicaraven, inhibits human platelet aggregation in vitro. Clin Neuropharmacol 1999; 22: 11–14
   PubMed Web of Science ®Google Scholar
• Hernandez-Hernandez A, Anchez-Yague J, Martin-Valmaseda EM, Llianillo M. Oxidative inactivation of human and sheep platelet membrane-associated phosphotyrosine phosphatase activity. Free Rad Biol Med 1999; 26: 1218–1230
   PubMed Web of Science ®Google Scholar
• Irani K, Pham Y, Coleman LD, Roos Ch, Cooke GE, Miodovnik A, Karim N, Wilhide CC, Bray PF, Goldschmidt-Clemont PJ. Priming of platelet αIIbβ3 by oxidants is associated with tyrosine phosphorylation of β3. Arterioscler Thromb Vasc Biol 1998; 18: 1698–1706
   PubMed Web of Science ®Google Scholar
• Nagai K, Inazu T, Yamamura H. P72syk is activated by vanadate plus H2O2 in porcine platelets and phosphorylates GTPase activating protein on tyrosine residue(s). J Biochem 1994; 116: 1176–1181
   PubMed Web of Science ®Google Scholar
• Wachowicz B, Olas B, Zbikowska HM, Buczynski A. Generation of reactive oxygen species in blood platelets. Platelets 2002; 13: 175–182
   PubMed Web of Science ®Google Scholar
• Jahn B, Hansch GM. Oxygen radical generation in human platelets: Depence of 12-lipoxygenase activity and on the glutathione cycle. Int Arch Allergy Appl Immunol 1990; 93: 73–79
   PubMedGoogle Scholar
• Gopalakrishna R, Jaken S. Protein kinase C signaling and oxidative stress. Free Radic Biol Med 2000; 28: 1349–1361
   PubMed Web of Science ®Google Scholar
• Forde RC, Fitzgerald DJ. Reactive oxygen species and platelet activation in reperfusion injury. Circulation 1997; 95: 787–789
   PubMed Web of Science ®Google Scholar
• Begonja AJ, Gambaryan S, Geiger J, Aktas B, Pozgajova M, Nieswandt B, Walter U. Platelet NAD(P)H oxidase-generated ROS production regulates {alpha}IIb{beta}3 integrin activation independent of the NO/cGMP pathway. Blood 2005; 106: 2757–2760
   PubMed Web of Science ®Google Scholar
• Miller DM, Grover TA, Nayini N, Aust SD. Xantine-oxidase- and iron-dependent lipid peroxidation. Arch Biochem Biophys 1993; 301: 1–7
   PubMed Web of Science ®Google Scholar
• Muruganandam A, Mutus B. Isolation of nitric oxide synthase from human platelets. Biochimica et Biophysica Acta 1994; 1200: 1–6
   PubMed Web of Science ®Google Scholar
• Sase K, Michel T. Expression of constitutive endothelial nitric oxide synthase in human blood platelets. Life Sci 1995; 57: 2049–2055
   PubMed Web of Science ®Google Scholar
• Mehta JL, Chen LY, Kone CB, Mehta P, Turner P. Identification of constitutive and inducible forms of nitric oxide synthase in human platelets. J Lab Clin Med 1995; 125: 87–96
   Web of Science ®Google Scholar
• Freedman JE, Loscalzo J, Barnard MR, Alpert C, Keaney JF, Michelson AD. Nitric oxide released from activated platelets inhibits platelet recruitment. J Clin Invest 1977; 100: 350–356
   Google Scholar
• Leoncini G, Pascale R, Signorello MG. Modulation of L-arginine transport and nitric oxide production by gabexate mesylate. Biochem Pharmacol 2002; 64: 277–283
   PubMed Web of Science ®Google Scholar
• Leoncini G, Bruzzese D, Signorello MG. The L-arginine/NO pathway in the early phases of platelet stimulation by collagen. Biochem Pharmacol 2005; 69: 289–296
   PubMed Web of Science ®Google Scholar
• Signorello MG, Pascale R, Leoncini G. Transport of L-arginine and nitric oxide formation in human platelets. Eur J Biochem 2003; 270: 2005–2012
   PubMedGoogle Scholar
• Zhou MH, Leist M, Ulrich U. Selective nitration of prostacyclin synthase and defective vasorelaxation in atherosclerotic bovine coronary arteries. Am J Path 1999; 154: 1359–1365
   PubMed Web of Science ®Google Scholar
• Malinski T, Radomski MW, Taha Z, Moncada S. Direct electrochemical measurement of nitric oxide released from human platelets. Biochem Biophys Res Commun 1993; 194: 960–965
   PubMed Web of Science ®Google Scholar
• Radomski MW, Zakar T, Salas E. Nitric oxide in platelets. Met Enzymol 1996; 269: 88–107
   PubMed Web of Science ®Google Scholar
• Bartosz G. Peroxynitrite: Mediator of the toxic action of nitric oxide. Acta Biochim Pol 1996; 43: 645–659
   PubMed Web of Science ®Google Scholar
• Soszynski M, Bartosz G. Effect of peroxynitrite on erythrocytes. Biochim Biophys Acta 1996; 1291: 107–114
   PubMed Web of Science ®Google Scholar
• Radi R. Nitric oxide, oxidations, and protein tyrosine nitration. PNAS 2004; 101: 4003–4008
   PubMed Web of Science ®Google Scholar
• Moro MA, Darley-Usmar VM, Goodwin DA, Read NG, Zamora-Pino R, Feelisch M, Radomski MW, Moncada S. Paradoxical fate and biological action of peroxynitrite on human platelets. Proc Natl Acad Sci 1994; 91: 6702–6706
   PubMed Web of Science ®Google Scholar
• Radomski MW, Palmer RMJ, Moncada S. An L-arginine/nitric oxide pathway present in human platelets regulates aggregation. Proc Natl Acad Sci 1990; 87: 5193–5197
   PubMed Web of Science ®Google Scholar
• Saluk-Juszczak J, Olas B, Nowak P, Kolodziejczyk J, Wachowicz B, Zgirski A. The effect of lipopolysaccharide from Proteus mirabilis on the level of the stable end metabolic products of nitric oxide in blood platelets. Curr Microbiol 2007; 54: 27–30
   PubMed Web of Science ®Google Scholar
• Picunio S, Simoni M, Doni MG. Platelet activation and modulation of the induction of nitric oxide synthase in the conscious rat. Life Sci 1999; 65: 1463–1475
   PubMed Web of Science ®Google Scholar
• Olszaniecki R, Gebska A, Kozlovski VI, Gryglewski RJ. Flavonoids and nitric oxide synthase. J Physiol Pharmacol 2002; 53: 571–584
   PubMed Web of Science ®Google Scholar
• Berkels R, Bertsch A, Zuther T, Dhein S, Stockklauser K, Rosen P, Rosen R. Evidence for a NO synthase in porcine platelets which is stimulated during activation/aggregation. Eur J Haematol 1997; 58: 307–313
   PubMed Web of Science ®Google Scholar
• Wallerath T, Gath I, Aulitzky WE, Pollock JS, Kleinert H, Forsermann U. Identification of the NO synthase isoforms expressed in human neutrophil granulocytes, megakoaryocytes and platelets. Thromb Haemost 1997; 77: 163–167
   PubMed Web of Science ®Google Scholar
• Matsubara K, Hayashi N, Jing T, Titani K. Regulation of endothelial nitric oxide synthase by protein kinase C. J Biochem 2003; 133: 773–781
   PubMed Web of Science ®Google Scholar
• Hirata K, Kuroda R, Sakoda T, Katay AM, Inoue N, Suematsu M, Kawashima S, Yokoyama M. Inhibition of endothelial nitric oxide synthase activity by protein kinase. C Hypertension 1995; 25: 180–185
   PubMed Web of Science ®Google Scholar
• Munzel T, Feil R, Mulsch A, Lohmann SM, Hofmann F, Walter U. Physiology and pathophysiology of vascular signaling controlled by guanosine 3’5’-cycilmonophosphate-dependent protein kinase. Circulation 2003; 108: 2172–2183
   PubMed Web of Science ®Google Scholar
• Lohmann SM, Walter U. Tracking functions of cGMP-dependent protein kinase (cGK). Front Biosc 2005; 10: 1313–1328
   PubMed Web of Science ®Google Scholar
• Grossmann R, Sokolova O, Schnurr A, Porsche C, Obergfell A, Lengenfelder B, Walter U, Figenthaler M. Variable extent of clopidogrel responsiveness in patients after coronary stending. Thromb Haemost 2004; 92: 1201–1206
   PubMed Web of Science ®Google Scholar
• Marcondes S, Cardoso MHM, Morganti RP, Thomazzi SM, Lilla S, Murad F, De Nucci G, Antunes E. Cyclic GMP-independent mechanisms contribute to the inhibition of platelet adhesion by nitric oxide donor: A role for α–actinin nitration. PNAS 2006; 103: 3434–3439
   PubMed Web of Science ®Google Scholar
• Marjanovic JA, Li Z, Stojanovic A, Du X. Stimulatory roles of nitric-oxide synthase 3 and guanylyl cyclase in platelet activation. J Biol Chem 2005; 280: 37430–37438
   PubMed Web of Science ®Google Scholar
• Begonja AJ, Teichmann L, Geiger J, Gambaryan S, Walter U. Platelet regulation by NO/cGMP signaling and NAD(P)H oxidase-generated ROS. Blood Cells, Molecules and Diseases 2006; 36: 166–170
   PubMed Web of Science ®Google Scholar
• Chakrabarti S, Clutton P, Verhese S, Cox D, Mascelli MA, Freedman JE. Glycoprotein IIb/IIIa inhibition enhances platelet nitric oxide release. Thromb Res 2004; 113: 225–233
   PubMed Web of Science ®Google Scholar
• Bermejo E, Saenz DA, Alberto F, Rosenstein RE, Bari SE, Lazzari MA. Effect of nitroxyl on human platelets function. Thromb Haemost 2005; 94: 578–584
   PubMed Web of Science ®Google Scholar
• Beckman JS, Koppenol WH. Nitric oxide, superoxide, and peroxynitrite: The good the bad, and ugly. Am J Physiol 1996; 271: 6C1424–37
   Google Scholar
• Beckman JS, Beckman TW, Chen J, Marshal PA, Freeman BA. Apperent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide. Proc Nat Acad Sci USA 1990; 87: 1620–1624
   PubMed Web of Science ®Google Scholar
• Huie RE, Padmaja S. The reaction of NO with superoxide. Free Rad Res Commun 1993; 18: 195–199
   PubMed Web of Science ®Google Scholar
• Pryor WA, Squadrito GL. The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide. Am J Physiol 1995; 268: L699–722
   PubMed Web of Science ®Google Scholar
• Lufrano M, Balazy M. Interactions of peroxynitrite and other nitrating substances with human platelets: The role of glutathione and peroxynitrite permeability. Biochem Pharmacol 2003; 65: 515–523
   PubMed Web of Science ®Google Scholar
• Gaston B. Nitric oxide and thiol groups. BBA 1999; 1411: 323–333
   PubMed Web of Science ®Google Scholar
• Crane MS, Ollosson R, Moore KP, Rossi AG, Megson IL. Novel role for low molecular weight plasma thiols in nitric oxide-mediated control of platelet function. J Biol Chem 2002; 277: 46858–46863
   PubMed Web of Science ®Google Scholar
• Inayama T, Oka J, Kashiba M, Saito M, Higuchi M, Umegaki K, Yamamoto Y, Matsuda M. Moderate physical exercise induces the oxidation of human blood protein thiols. Life Sci 2002; 70: 2039–2046
   PubMed Web of Science ®Google Scholar
• Kato Y, Kawakishi S, Aoki T, Itakura K, Osawa T. Oxidative modification of tryptophan residues exposed to peroxynitrite. Biochim Biophys Res Commun 1997; 234: 82–84
   PubMed Web of Science ®Google Scholar
• Ischiropoulos H, Al-Mehdi AB. Peroxynitrite-mediated oxidative protein modifications. FEBS Lett 1995; 364: 279–282
   PubMed Web of Science ®Google Scholar
• Mondoro TH, Shafer BC, Vostal JG. Peroxynitrite-induced tyrosine nitration and phosphorylation in human platelets. Free Rad Biol Med 1997; 22: 1055–1063
   PubMed Web of Science ®Google Scholar
• Ducrocq C, Blanchard B, Pignatelli B, Oshima H. Peroxynitrite: An endogenous oxidizing and nitrating agent. Cell Mol Life Sci 1999; 55: 1068–1077
   PubMed Web of Science ®Google Scholar
• Sneddon JM, Vane JR. Endothelium-derived relaxing factor reduces platelet adhesion to bovine endothelial cells. Proc Natl Acad Sci USA 1988; 85: 2800–2804
   PubMed Web of Science ®Google Scholar
• Yin K, Lai PS, Rodriguez A, Spur BW, Wong PY. Antithrombotic effects of peroxynitrite: Inhibition and reversal of aggregation in human platelets. Prostaglandins 1995; 50: 169–178
   PubMed Web of Science ®Google Scholar
• Brown AS, Moro MA, Masse JM, Cramer EM, Radomski M, Darley-Usmar V. Nitric oxide-dependent and independent effects on human platelets treated with peroxynitrite. Cardiovasc Res 1998; 40: 380–388
   PubMed Web of Science ®Google Scholar
• Maalej N, Albrecht R, Loscalzo J, Folts JD. The potent platelet inhibitory effects of S-nitrosed albumin coating of artificial surfaces. J Am Coll Cardiol 1996; 33: 1408–1414
   Google Scholar
• Nowak P, Wachowicz B. Studies on pig blood platelet responses to peroxynitrite action. Platelets 2001; 12: 376–381
   PubMed Web of Science ®Google Scholar
• Nowak P, Wachowicz B. Peroxynitrite-mediated modification of fibrinogen affects platelet aggregation and adhesion. Platelets 2002; 13: 293–299
   PubMed Web of Science ®Google Scholar
• Nowak P, Wachowicz B. The effects of peroxynitrite on pig platelet lipid peroxidation and the secretory process induced by thrombin. Cytobios 2001; 106: 179–187
   PubMedGoogle Scholar
• Naseem KM, Low SY, Sabetkar M, Bradley NJ, Khan J, Jacobs M, Bruckdorfer KR. The nitration of platelet cytosolic proteins during agonist-induced activation of platelets. FEBS Lett 2000; 473: 119–122
   PubMed Web of Science ®Google Scholar
• Bruckdorfer KR. The nitration of proteins in platelets. Life Sci 2001; 324: 611–615
   Web of Science ®Google Scholar
• Olas B, Nowak P, Ponczek M, Wachowicz B. Natural phenolic compound  — resveratrol may reduce carbonylation of proteins induced by peroxynitrite in blood platelets. General Physiol Biophys 2006; 25: 215–222
   PubMed Web of Science ®Google Scholar
• Olas B, Nowak P, Kołodziejczyk J, Wachowicz B. The effects of antioxidants on peroxynitrite-induced changes in platelet proteins. Thromb Res 2004; 113: 399–406
   PubMed Web of Science ®Google Scholar
• Sabetkar M, Low SY, Naseem KM, Bruckdorfer KR. The nitration of proteins in platelets: Significance in platelet function. Free Rad Biol Med 2002; 33: 728–736
   PubMed Web of Science ®Google Scholar
• Nowak P, Olas B, Bald E, Glowacki R, Wachowicz B. Peroxynitrite-induced changes of thiol groups in human blood platelets. Platelets 2003; 14: 375–379
   PubMed Web of Science ®Google Scholar
• Quijano C, Alvarez B, Gatti RM, Augusto O, Radi R. Pathways of peroxynitrite oxidation of thiol groups. Biochem J 1997; 322: 167–173
   PubMed Web of Science ®Google Scholar
• Minetti M, Mallozzi C, Di Stasi AMM. Peroxynitrite activates kinases of the src family and upregulates tyrosine phosphorylation signalling. Free Rad Biol Med 2002; 33: 744–754
   PubMed Web of Science ®Google Scholar
• Hart JJ, Welch RM, Norvell WA, Kochian LV. Measurement of thiol-containing amino acids and phytochelatin (PC2) via capillary electrophoresis with laser-induced fluorescence detection. Electrophoresis 2002; 23: 81–87
   PubMed Web of Science ®Google Scholar
• Kappusamy P, Li H, Ilangovan G, Cardounel AJ, Zweier JL, Yamada K, Krishna MC, Mitchell JB. Noninvasive imaging of tumor redox status and its modification by tissue glutathione levels. Cancer Res 2002; 62: 307–312
   PubMed Web of Science ®Google Scholar
• Schafer FQ, Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Rad Biol Med 2001; 30: 1191–1212
   PubMed Web of Science ®Google Scholar
• Essex DW, Li M. Redox control of platelet aggregation. Biochemistry 2003; 42: 129–136
   PubMed Web of Science ®Google Scholar
• Hansen JM, Choe HS, Carney EW, Harris C. Differential antioxidant enzyme activities and glutathione content between rat and rabbit conceptuses. Free Rad Biol Med 2001; 30: 1078–1088
   PubMed Web of Science ®Google Scholar
• Martin C, Martinez R, Navarro R, Ruiz-Sanz JI, Lacort M, Ruiz-Larrea MB. Tert-Butyl hydroperoxide-induced lipid signalling in hepatocytes: Involvement of glutathione and free radicals. Biochem Pharmacol 2001; 62: 705–712
   PubMed Web of Science ®Google Scholar
• Mayer B, Schrammel A, Klatt P, Koesling D, Schmidt K. Peroxynitrite-induced accumulation of cyclic GMP in endothelial cells and stimulated soluble guanylyl cyclase. Dependence on glutathione and possible role of S-nitrosylation. J Biol Chem 1995; 270: 17355–17360
   PubMed Web of Science ®Google Scholar
• Scorza G, Minetti M. One-electron oxidation pathway of thiols by peroxynitrite in biological fluids: Bicarbonate and ascorbate promote the formation of albumin disulphide dimmers in human blood plasma. Biochem J 1998; 329: 405–413
   PubMed Web of Science ®Google Scholar
• Dalle-Donne I, Rossi R, Giustarini D, Gagliano N, Lusini L, Milzani A, Di Simplicio P, Colombo R. Actin carbonylation: From a simple marker of protein oxidation to relevant signs of severe functional impairement. Free Rad Biol Med 2001; 31: 1075–1083
   PubMed Web of Science ®Google Scholar
• Dalle-Donne I, Rossi R, Giustarini D, Milzani A, Colombo R. Protein carbonyl groups as biomarkers of oxidative stress. Clinica Chimica Acta 2003; 329: 23–38
   PubMed Web of Science ®Google Scholar
• Dalle-Donne I, Giustarini D, Colombo R, Rossi R, Milzani A. Protein carbonylation in human diseases. Trends in Molceular Medicine 2003; 9: 169–176
   PubMed Web of Science ®Google Scholar
• Ischiropoulos H. Biological tyrosine nitration: A pathophysiological function of nitric oxide. Arch Biochem Biophys 1998; 356: 1–11
   PubMed Web of Science ®Google Scholar
• Reiter CD, Teng RJ, Beckman JS. Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite. J Biol Chem 2000; 259: 32460–32466
   Web of Science ®Google Scholar
• Boulos C, Jiang H, Balazy M. Diffusion of peroxynitrite into the human platelet inhibits cyclooxygenase via nitration of tyrosine residues. J Pharmacol Exp Ther 2000; 293: 222–229
   PubMed Web of Science ®Google Scholar
• Jiang H, Balazy M. Detection of 3-nitrotyrosine in human platelets exposed to peroxynitrite by a new gas chromatography/mass spectrometry assay. Nitric Oxide 1998; 2: 350–359
   PubMed Web of Science ®Google Scholar
• Butt E, Abel K, Krieger M, Palm D, Hoppe V, Walter U. cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact platelets. J Biol Chem 1994; 269: 14509–14517
   PubMed Web of Science ®Google Scholar
• Ischiropoulos H. Biological selectivity and functional aspects of protein tyrosine nitration. Biochem Biophys Res Commun 2003; 305: 776–783
   PubMed Web of Science ®Google Scholar
• Low SY, Sabetkar M, Bruckdorfer KR, Naseem KM. The role of protein nitration in the inhibition of platelet activation by peroxynitrite. FEBS Lett 2002; 511: 59–64
   PubMed Web of Science ®Google Scholar
• Khan J, Brennan DM, Bradley N, Gao B, Brukdorfer R, Jacobs M. 3-Nitrotyrosine in the proteins of human plasma determined by an Elisa method. Biochem J 1998; 330: 795–801
   PubMed Web of Science ®Google Scholar
• Kalyanaraman B. Nitrated lipids: A class of cell-signaling molecules. PNAS 2004; 101: 11527–11528
   PubMed Web of Science ®Google Scholar
• Coles B, Bloodsworth A, Eiserich JP, Lewis MJ, McLoughlin RM, Giddings JC, Lewis MJ, Haslam RJ, Freedman BA, O’Donnelll VB. Nitrolinoleate inhibits platelet activation by attenuating calcium mobilization and inducing phosphorylation of vasodilator-stimulated phosphoprotein through elevation of cAMP. J Biol Chem 2002; 277: 5832–5840
   PubMed Web of Science ®Google Scholar
• Klotz LO, Sies H. Defenses against peroxynitrite: Selenocompounds and flavonoids. Toxicol Lett 2003; 140: 125–132
   PubMed Web of Science ®Google Scholar
• Arteel GE, Briviba K, Sies H. Protection against peroxynitrite. FEBS Lett 1999; 445: 226–230
   PubMed Web of Science ®Google Scholar
• Sies H. Ebselen, a selenoorganic compound as glutathione peroxidase mimic. Free Rad Biol Med 1993; 14: 313–323
   PubMed Web of Science ®Google Scholar
• Fiala ES, Sodum RS, Bhattacharaya M, Li H. (−)-Epigallocatechin gallate, a polyphenolic tea antioxidant, inhibits peroxynitrite-mediated formation of 8-oxodeoxyguanosine and 3-nitrotyrosine. Experientia 1996; 52: 922–926
   PubMedGoogle Scholar
• Pannala AS, Rice-Evans CA, Halliwell B, Singh S. Inhibition of peroxynitrite-mediated tyrosine nitration by catechin polyphenols. Biochem Biophys Res Commun 1997; 232: 164–168
   PubMed Web of Science ®Google Scholar
• Wippel R, Rehn M, Gorren ACF, Schmidt K, Mayer B. Interference of the polyphenol epicatechin with the biological chemistry of nitric oxide- and peroxynitrite-mediated reactions. Biochem Pharmacol 2004; 67: 1285–1295
   PubMed Web of Science ®Google Scholar
• Schroeder P, Zhang H, Klotz LO, Kalyanaraman B, Sies H. (−)-Epicatechin inhibits nitration and dimerization of tyrosine in hydrophilic as well as hydrophobic environments. Biochem Biophys Res Commun 2001; 289: 1334–1338
   PubMed Web of Science ®Google Scholar
• van Acker SA, Tromp MN, Haenen GR, van der Vijgh WJ, Bast A. Flavonoids as scavengers of nitric oxide radical. Biochem Biophys Res Commun 1995; 214: 755–759
   PubMed Web of Science ®Google Scholar
• Robak J, Gryglewski RJ. Flavonoids are scavengers of superoxide anions. Biochem Pharmacol 1988; 37: 837–841
   PubMed Web of Science ®Google Scholar
• Kostyuk VA, Kraemer T, Sies H, Schewe T. Myeloperoxidase/nitrite-mediated lipid peroxidation of low-density lipoprotein as modulated by flavonoids. FEBS Lett 2003; 537: 146–150
   PubMed Web of Science ®Google Scholar
• Olas B, Wachowicz B, Saluk-Juszczak J, Zielinski T, Kaca W, Buczynski A. Antioxidant activity of resveratrol in endotoxin  – stimulated blood platelets. Cell Biol Toxicol 2001; 17: 117–125
   PubMed Web of Science ®Google Scholar
• Olas B, Nowak P, Wachowicz B. Resveratrol protects against peroxynitrite  – induced thiol oxidation in blood platelets. CMBL 2004; 9: 577–587
   Google Scholar
• Bartesaghi S, Trujillo M, Denicola A, Folkes L, Wardman P, Radi R. Reactions of desferrioxamine with peroxynitrite-derived carbonate and nitrogen dioxide radicals. Free Rad Biol Med 2004; 36: 471–483
   PubMed Web of Science ®Google Scholar
• Fremont L, Belguendouz L, Delpal S. Antioxidant activity of resveratrol and alcohol-free wine polyphenols related to LDL oxidation and polyunsaturated fatty acids. Life Sci 1999; 64: 2511–2521
   PubMed Web of Science ®Google Scholar
• Olas B, Wachowicz B. Resveratrol, a phenolic antioxidant with effects on blood platelet functions. Platelets 2005; 16: 251–260
   PubMed Web of Science ®Google Scholar
• Olas B, Zbikowska HM, Wachowicz B, Krajewski T, Buczynski A, Magnuszewska A. Inhibitory effect of resveratrol on free radical generation in blood platelets. Acta Biochim Polon 1999; 46: 961–966
   PubMed Web of Science ®Google Scholar
• Olas B, Wachowicz B. Resveratrol and vitamin c as antioxidants in blood platelets. Thromb Res 2002; 106: 143–148
   PubMed Web of Science ®Google Scholar
• Olas B, Wachowicz B, Saluk-Juszczak J, Zielinski T. Effect of resveratrol, a natural polyphenolic compound, on platelet activation induced by endotoxin or thrombin. Thromb Res 2002; 107: 141–145
   PubMed Web of Science ®Google Scholar
• Zbikowska HM, Olas B, Wachowicz B, Krajewski T. Response of blood platelets to resveratrol. Platelets 1999; 10: 247–252
   PubMed Web of Science ®Google Scholar
• Arts MJTJ, Haenen GRMM, Wilms LC, Beetstra SAJN, Heijnen CGM, Voss HP, Bast A. Interactions between flavonoids and proteins: Effect on the total antioxidant capacity. J Agric Food Chem 2002; 50: 1184–1187
   PubMed Web of Science ®Google Scholar
• Kim AR, Park MJ, Lee MK, Sung SH, Park EJ, Kim J, Kim SY, Oh TH, Markelonis J, Kim YC. Flavonoids of Inula Britanica protect cultured cortical cells from cecrotic cell death induced by glutamate. Free Rad Biol Med 2002; 32: 596–604
   PubMed Web of Science ®Google Scholar
• Stojanovic S, Sprintz H, Brede O. Efficiency and mechanism of the antioxidant action of trans-resveratrol and its analogues in the radical liposome oxidation. Archiv Biochem Biophys 2001; 391: 79–89
   PubMed Web of Science ®Google Scholar
• Zhao CY, Shi YM, Yao SD, Jia ZJ, Fan BT, Wang WF, Lin WZ, Lin NY, Zheng RL. Scavenging effects of natural phenols on oxidizing intermediates of peroxynitrite. Pharmazie 2003; 58: 742–749
   PubMed Web of Science ®Google Scholar
• Bulger EM, Maier RV. Antioxidants in critical illness. Arch Surg 2001; 136: 1201–7
   PubMedGoogle Scholar
• Pippard MJ, Weatherall RV. Deferiprone for thalassaemia. Lancet 2000; 35: 1444–1445
   Google Scholar
• Practico D, Pasin M, Barry OP, Ghiselli A, Sabatino G, Iuliano L, Fitzgerald GA, Violi F. Iron-dependent human platelet activation and hydroxyl radical formation: Involvement of protein kinase C. Circulation 1999; 99: 118–124
   Web of Science ®Google Scholar
• Waring WS, Webb DJ, Maxwell RJ. Systemic uric acid administration increases serum antioxidant capacity in healthy volunteers. J Cardiovasc Pharmacol 2003; 38: 365–371
   Web of Science ®Google Scholar