메뉴 건너뛰기




Volumn 58, Issue 2, 2002, Pages 127-135

Hypochlorous acid-induced oxidative damage of human red blood cells: Effects of tert-butyl hydroperoxide and nitrite on the HOCl reaction with erythrocytes

Author keywords

Erythrocyte; Haemolysis; Hypochlorite; Nitrite; Oxidative stress

Indexed keywords

ACTIVATION ENERGY; BIOLOGICAL MEMBRANES; BLOOD; COLLOIDS; ENZYMES; INORGANIC ACIDS; OSMOSIS; OXIDATION;

EID: 0036888624     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1567-5394(01)00126-8     Document Type: Article
Times cited : (32)

References (34)
  • 2
    • 0031916191 scopus 로고    scopus 로고
    • Hypochlorous acid inhibits Ca(2+)-ATPase from skeletal muscle sarcoplasmic reticulum
    • Favero T.G., Colter D., Hooper P.F., Abramson J.J. Hypochlorous acid inhibits Ca(2+)-ATPase from skeletal muscle sarcoplasmic reticulum. J. Appl. Physiol. 84:1998;425-430.
    • (1998) J. Appl. Physiol. , vol.84 , pp. 425-430
    • Favero, T.G.1    Colter, D.2    Hooper, P.F.3    Abramson, J.J.4
  • 3
    • 0027359174 scopus 로고
    • Potential roles of hypochlorous acid and N-chloroamines in collagen breakdown by phagocytic cells in synovitis
    • Davies J.M., Horwitz D.A., Davies K.J. Potential roles of hypochlorous acid and N-chloroamines in collagen breakdown by phagocytic cells in synovitis. Free Radical Biol. Med. 15:1993;434-637.
    • (1993) Free Radical Biol. Med. , vol.15 , pp. 434-637
    • Davies, J.M.1    Horwitz, D.A.2    Davies, K.J.3
  • 4
    • 0001883969 scopus 로고
    • Phagocytic cells: Products of oxygen metabolism
    • J.I. Gallin, I.M. Goldstein, & R. Snyderman. New York: Raven Press
    • Klebanoff S.J. Phagocytic cells: products of oxygen metabolism. Gallin J.I., Goldstein I.M., Snyderman R. Inflammation: Basic principles and Clinical Correlates. 1988;391-443 Raven Press, New York.
    • (1988) Inflammation: Basic principles and Clinical Correlates , pp. 391-443
    • Klebanoff, S.J.1
  • 5
    • 0025980710 scopus 로고
    • Oxidative damage to fibronectin: I. The effects of the neutrophil myeloperoxidase system and HOCl
    • Vissers M.C.M., Winterbourn C.C. Oxidative damage to fibronectin: I. The effects of the neutrophil myeloperoxidase system and HOCl. Arch. Biochem. Biophys. 285:1991;53-59.
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 53-59
    • Vissers, M.C.M.1    Winterbourn, C.C.2
  • 6
    • 0032525801 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to proteins: Formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation
    • Hawkins C.L., Davies M.J. Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. Biochem. J. 332:1998;617-625.
    • (1998) Biochem. J. , vol.332 , pp. 617-625
    • Hawkins, C.L.1    Davies, M.J.2
  • 7
    • 0031350219 scopus 로고    scopus 로고
    • Modification of red cell membrane lipids by hypochlorous acid and haemolysis by preformed lipid chlorohydrins
    • Carr A.C., Vissers M.C.M., Domigan N.M., Winterbourn C.C. Modification of red cell membrane lipids by hypochlorous acid and haemolysis by preformed lipid chlorohydrins. Redox Rep. 3:1997;263-271.
    • (1997) Redox Rep. , vol.3 , pp. 263-271
    • Carr, A.C.1    Vissers, M.C.M.2    Domigan, N.M.3    Winterbourn, C.C.4
  • 8
    • 0028940342 scopus 로고
    • Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid
    • Vissers M.C.M., Winterbourn C.C. Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid. Biochem. J. 307:1995;57-62.
    • (1995) Biochem. J. , vol.307 , pp. 57-62
    • Vissers, M.C.M.1    Winterbourn, C.C.2
  • 9
    • 0030928562 scopus 로고    scopus 로고
    • Characterisation of the oxidation products of the reaction between reduced glutathione and hypochlorous acid
    • Winterbourn C.C., Brennan S.O. Characterisation of the oxidation products of the reaction between reduced glutathione and hypochlorous acid. Biochem. J. 326:1997;87-92.
    • (1997) Biochem. J. , vol.326 , pp. 87-92
    • Winterbourn, C.C.1    Brennan, S.O.2
  • 12
    • 0032519779 scopus 로고    scopus 로고
    • Comparison of human red cell lysis by hypochlorous and hypobromous acids: Insights into the mechanism of lysis
    • Vissers M.C.M., Carr A.C., Chapman A.L.P. Comparison of human red cell lysis by hypochlorous and hypobromous acids: insights into the mechanism of lysis. Biochem. J. 330:1998;131-138.
    • (1998) Biochem. J. , vol.330 , pp. 131-138
    • Vissers, M.C.M.1    Carr, A.C.2    Chapman, A.L.P.3
  • 14
    • 0029554597 scopus 로고
    • The production of nitrating species by the reaction between nitrite and hypochlorous acid
    • Kono Y. The production of nitrating species by the reaction between nitrite and hypochlorous acid. Biochem. Mol. Biol. Int. 36:1995;275-283.
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , pp. 275-283
    • Kono, Y.1
  • 15
    • 0032742579 scopus 로고    scopus 로고
    • Loss of GSH and thiol enzymes in endothelial cells exposed to sublethal concentrations of hypochlorous acid
    • Pullar J.M., Winterbourn C.C., Vissers M.C.M. Loss of GSH and thiol enzymes in endothelial cells exposed to sublethal concentrations of hypochlorous acid. Am. J. Physiol. 277:1999;H1505-H1512.
    • (1999) Am. J. Physiol. , vol.277
    • Pullar, J.M.1    Winterbourn, C.C.2    Vissers, M.C.M.3
  • 16
    • 8544251150 scopus 로고    scopus 로고
    • The acid ionization constant of HOCl from 5° to 35°
    • Morris J.C. The acid ionization constant of HOCl from 5° to 35° J. Phys. Chem. 70:1996;3798-3805.
    • (1996) J. Phys. Chem. , vol.70 , pp. 3798-3805
    • Morris, J.C.1
  • 17
    • 0014974075 scopus 로고
    • The autoxidation of human red cell lipids induced by hydrogen peroxide
    • Stocks J., Dormandy T.L. The autoxidation of human red cell lipids induced by hydrogen peroxide. Br. J. Haematol. 20:1971;95-111.
    • (1971) Br. J. Haematol. , vol.20 , pp. 95-111
    • Stocks, J.1    Dormandy, T.L.2
  • 18
    • 0025145949 scopus 로고
    • Oxidative reaction of hemoglobin
    • Winterborn C.C. Oxidative reaction of hemoglobin. Methods Enzymol. 186:1990;265-272.
    • (1990) Methods Enzymol. , vol.186 , pp. 265-272
    • Winterborn, C.C.1
  • 20
    • 0028872559 scopus 로고
    • Thiol groups in proteins as endogenous reductants to determine glutathione-protein mixed disulphides in biological systems
    • Rossi R., Cardaioli E., Scaloni A., Amiconi G., Di Simplico P. Thiol groups in proteins as endogenous reductants to determine glutathione-protein mixed disulphides in biological systems. Biochim. Biophys. Acta. 1243:1995;230-238.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 230-238
    • Rossi, R.1    Cardaioli, E.2    Scaloni, A.3    Amiconi, G.4    Di Simplico, P.5
  • 22
    • 0018689246 scopus 로고
    • A sensitive fluorimetric microassay for the determination of glutathione peroxidase activity. Application to human blood platelets
    • Martinez J.I., Launay J.M., Dreux C. A sensitive fluorimetric microassay for the determination of glutathione peroxidase activity. Application to human blood platelets. Anal. Biochem. 98:1979;154-159.
    • (1979) Anal. Biochem. , vol.98 , pp. 154-159
    • Martinez, J.I.1    Launay, J.M.2    Dreux, C.3
  • 23
    • 0030941614 scopus 로고    scopus 로고
    • Effect of postirradiation treatment on the radiation-induced haemolysis of human erythrocytes
    • Soszynski M., Bartosz G. Effect of postirradiation treatment on the radiation-induced haemolysis of human erythrocytes. Int. J. Radiat. Biol. 71:1997;337-343.
    • (1997) Int. J. Radiat. Biol. , vol.71 , pp. 337-343
    • Soszynski, M.1    Bartosz, G.2
  • 24
    • 0346613555 scopus 로고    scopus 로고
    • Reaction of HOCl with amino acids and peptides: EPR evidence for rapid rearrangement and fragmentation reactions of nitrogen-centred radicals
    • Hawkins C.L., Davies M.J. Reaction of HOCl with amino acids and peptides: EPR evidence for rapid rearrangement and fragmentation reactions of nitrogen-centred radicals. J. Chem. Soc., Perkin Trans. 2:1998;1937-1945.
    • (1998) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1937-1945
    • Hawkins, C.L.1    Davies, M.J.2
  • 25
    • 0001198324 scopus 로고    scopus 로고
    • Hypochlorous acid as reactive oxygen species
    • Schaur J.R., Jerlich A., Stelmaszynska T. Hypochlorous acid as reactive oxygen species. Curr. Top. Biophys. 22(Suppl. B):1998;176-185.
    • (1998) Curr. Top. Biophys. , vol.22 , Issue.SUPPL. B , pp. 176-185
    • Schaur, J.R.1    Jerlich, A.2    Stelmaszynska, T.3
  • 27
    • 0025787444 scopus 로고
    • Differential scanning calorimetric study of carboxypeptidase B, procarboxypeptidase B and its globular activation domain
    • Conejero-Lara F., Sanchez-Ruiz J.M., Mateo P.L., Burgos F.J., Vendrell J., Aviles F.X. Differential scanning calorimetric study of carboxypeptidase B, procarboxypeptidase B and its globular activation domain. Eur. J. Biochem. 200:1991;663-670.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 663-670
    • Conejero-Lara, F.1    Sanchez-Ruiz, J.M.2    Mateo, P.L.3    Burgos, F.J.4    Vendrell, J.5    Aviles, F.X.6
  • 28
    • 33845549925 scopus 로고
    • Lipid chain length and temperature dependence of ethanol-phosphatidylcholine interactions
    • Rowe E. Lipid chain length and temperature dependence of ethanol-phosphatidylcholine interactions. Biochemistry. 22:1983;3329-3335.
    • (1983) Biochemistry , vol.22 , pp. 3329-3335
    • Rowe, E.1
  • 29
    • 2242486963 scopus 로고
    • Structure and functions of erythrocyte membranes
    • (in Russian)
    • Chernitskii E.A., Vorobei A.V. Structure and functions of erythrocyte membranes. Nauka Tekh. (Minsk). 1981;. (in Russian).
    • (1981) Nauka Tekh. (Minsk)
    • Chernitskii, E.A.1    Vorobei, A.V.2
  • 30
    • 0022408597 scopus 로고
    • Membrane acetylcholinesterases: Purification, molecular properties and interactions with amphiphilic environments
    • Ott P. Membrane acetylcholinesterases: purification, molecular properties and interactions with amphiphilic environments. Biochim. Biophys. Acta. 882:1985;375-392.
    • (1985) Biochim. Biophys. Acta , vol.882 , pp. 375-392
    • Ott, P.1
  • 31
    • 0031401811 scopus 로고    scopus 로고
    • Effect of malathione on kinetic parameters of acetylcholinesterase (EC 3.1.1.7) in vitro
    • Kamal M.A. Effect of malathione on kinetic parameters of acetylcholinesterase (EC 3.1.1.7) in vitro. Biochem. Mol. Biol. Int. 43:1997;89-97.
    • (1997) Biochem. Mol. Biol. Int. , vol.43 , pp. 89-97
    • Kamal, M.A.1
  • 32
    • 0031571108 scopus 로고    scopus 로고
    • Oxidative modification and nitration of human low-density lipoproteins by the reaction of hypochlorous acid with nitrite
    • Panasenko O.M., Briviba K., Klotz L.-O., Sies H. Oxidative modification and nitration of human low-density lipoproteins by the reaction of hypochlorous acid with nitrite. Arch. Biochem. Biophys. 343:1997;254-259.
    • (1997) Arch. Biochem. Biophys. , vol.343 , pp. 254-259
    • Panasenko, O.M.1    Briviba, K.2    Klotz, L.-O.3    Sies, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.