메뉴 건너뛰기




Volumn 12, Issue 11, 2010, Pages 1235-1246

Irreversible inactivation of glutathione peroxidase 1 and reversible inactivation of peroxiredoxin ii by H2O2 in red blood cells

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; CYSTEINE SULFINIC ACID; DEHYDROALANINE; GLUTATHIONE PEROXIDASE 1; HEMOGLOBIN; HYDROGEN PEROXIDE; OXIDOREDUCTASE; PEROXIREDOXIN 2; SELENOCYSTEINE; SULFIREDOXIN; UNCLASSIFIED DRUG;

EID: 77951813369     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2009.2701     Document Type: Article
Times cited : (115)

References (48)
  • 2
    • 0016769483 scopus 로고
    • Purification and properties of human erythrocyte glutathione peroxidase
    • Awasthi YC, Beutler E, and Srivastava SK. Purification and properties of human erythrocyte glutathione peroxidase. J Biol Chem 250: 5144-5149, 1975.
    • (1975) J Biol Chem , vol.250 , pp. 5144-5149
    • Awasthi, Y.C.1    Beutler, E.2    Srivastava, S.K.3
  • 3
    • 0019192485 scopus 로고
    • Aging of the erythrocyte. VII. on the possible causes of inactivation of red cell enzymes
    • Bartosz, G. Aging of the erythrocyte. VII. On the possible causes of inactivation of red cell enzymes. Mech Ageing Dev 13: 379-385, 1980.
    • (1980) Mech Ageing Dev , vol.13 , pp. 379-385
    • Bartosz, G.1
  • 4
    • 0000197885 scopus 로고
    • The hemolytic effect of primaquine and related compounds: A review
    • Beutler, E. The hemolytic effect of primaquine and related compounds: A review. Blood 14: 103-139, 1959.
    • (1959) Blood , vol.14 , pp. 103-139
    • Beutler, E.1
  • 5
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphir-edoxin
    • Biteau B, Labarre J, and Toledano MB. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphir-edoxin. Nature 425: 980-984, 2003.
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 7
    • 0022259872 scopus 로고
    • Inactivation of glutathione peroxi-dase by superoxide radical
    • Blum J and Fridovich I. Inactivation of glutathione peroxi-dase by superoxide radical. Arch Biochem Biophys 240: 500-508, 1985.
    • (1985) Arch Biochem Biophys , vol.240 , pp. 500-508
    • Blum, J.1    Fridovich, I.2
  • 8
    • 0017410975 scopus 로고
    • Mechanism of decrease in erythrocyte enzyme activities during red cell aging in the newborn and the adult
    • Boyer C, Kahn A, Cottreau D, and Marie J. [Mechanism of decrease in erythrocyte enzyme activities during red cell aging in the newborn and the adult]. Nouv Rev Fr Hematol Blood Cells 18: 229-231, 1977.
    • (1977) Nouv Rev Fr Hematol Blood Cells , vol.18 , pp. 229-231
    • Boyer, C.1    Kahn, A.2    Cottreau, D.3    Marie, J.4
  • 9
    • 0033230807 scopus 로고    scopus 로고
    • Tissue-specific functions of individual glutathione peroxidases
    • Brigelius-Flohe, R. Tissue-specific functions of individual glutathione peroxidases. Free Radic Biol Med 27: 951-965, 1999.
    • (1999) Free Radic Biol Med , vol.27 , pp. 951-965
    • Brigelius-Flohe, R.1
  • 10
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae HZ, Chung SJ, and Rhee SG. Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 269: 27670-27678, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 11
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae HZ, Robison K, Poole LB, Church G, Storz G, and Rhee SG. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci USA 91: 7017-7021, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 12
    • 0036797684 scopus 로고    scopus 로고
    • Effect of oxidative stress on glutathione pathway in red blood cells from patients with insulin-dependent diabetes mellitus
    • Dincer Y, Akcay T, Alademir Z, and Ilkova H. Effect of oxidative stress on glutathione pathway in red blood cells from patients with insulin-dependent diabetes mellitus. Metabolism 51: 1360-1362, 2002.
    • (2002) Metabolism , vol.51 , pp. 1360-1362
    • Dincer, Y.1    Akcay, T.2    Alademir, Z.3    Ilkova, H.4
  • 13
    • 33750604769 scopus 로고    scopus 로고
    • Selenoproteins of the gluta-thione system
    • edited by Hatfield, dl. Boston, Dordrecht, London: Kluwer Academic Publishers.
    • Flohe L and Brigelius-Flohe R. Selenoproteins of the gluta-thione system. In: Selenium. Its Molecular Biology and Role in Human Health, edited by Hatfield, dl. Boston, Dordrecht, London: Kluwer Academic Publishers. 2001. pp. 161-172
    • (2001) Selenium. Its Molecular Biology and Role in Human Health , pp. 161-172
    • Flohe, L.1    Brigelius-Flohe, R.2
  • 14
    • 0036363570 scopus 로고    scopus 로고
    • Quan-titation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins
    • Hamann M, Zhang T, Hendrich S, and Thomas JA. Quan-titation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins. Methods Enzymol 348: 146-156, 2002.
    • (2002) Methods Enzymol , vol.348 , pp. 146-156
    • Hamann, M.1    Zhang, T.2    Hendrich, S.3    Thomas, J.A.4
  • 15
    • 0022508522 scopus 로고
    • Role of aniline metabolites in aniline-induced hemolytic anemia
    • Harrison JH, Jr. and Jollow DJ. Role of aniline metabolites in aniline-induced hemolytic anemia. J Pharmacol Exp Ther 238: 1045-1054, 1986.
    • (1986) J Pharmacol Exp Ther , vol.238 , pp. 1045-1054
    • Harrison JH, Jr.1    Jollow, D.J.2
  • 16
    • 0030971057 scopus 로고    scopus 로고
    • Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia
    • Ho YS, Magnenat JL, RBronson RT, Cao J, Gargano M, Sugawara M, and Funk CD. Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J Biol Chem 272: 16644-16651, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 16644-16651
    • Ho, Y.S.1    Magnenat, J.L.2    Rbronson, R.T.3    Cao, J.4    Gargano, M.5    Sugawara, M.6    Funk, C.D.7
  • 17
    • 3543040601 scopus 로고    scopus 로고
    • Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury
    • Ho YS, Xiong Y, Ma W, Spector A, and Ho DS. Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury. J Biol Chem 279: 32804-32812, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 32804-32812
    • Ho, Y.S.1    Xiong, Y.2    Ma, W.3    Spector, A.4    Ho, D.S.5
  • 18
    • 0000476830 scopus 로고
    • Oxidative hemolysis and erythrocyte metabolism in hereditary acatalasia
    • Jacob HS, Ingbar SH, and Jandl JH. Oxidative hemolysis and erythrocyte metabolism in hereditary acatalasia. J Clin Invest 44: 1187-1199, 1965.
    • (1965) J Clin Invest , vol.44 , pp. 1187-1199
    • Jacob, H.S.1    Ingbar, S.H.2    Jandl, J.H.3
  • 19
    • 33744919853 scopus 로고    scopus 로고
    • Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin
    • Jeong W, Park SJ, Chang TS, Lee DY, and Rhee SG. Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. J Biol Chem 281: 14400-14407, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 14400-14407
    • Jeong, W.1    Park, S.J.2    Chang, T.S.3    Lee, D.Y.4    Rhee, S.G.5
  • 20
    • 27544508986 scopus 로고    scopus 로고
    • Hemoglobin autoxidation and regulation of endogenous H2O2 levels in erythrocytes
    • Johnson RM, Goyette G Jr, Ravindranath Y, and Ho YS. Hemoglobin autoxidation and regulation of endogenous H2O2 levels in erythrocytes. Free Radic Biol Med 39: 1407-1417, 2005.
    • (2005) Free Radic Biol Med , vol.39 , pp. 1407-1417
    • Johnson, R.M.1    Goyette Jr., G.2    Ravindranath, Y.3    Ho, Y.S.4
  • 21
    • 0034284002 scopus 로고    scopus 로고
    • Red cells from glutathione peroxidase-1-deficient mice have nearly normal defenses against exogenous peroxides
    • Johnson RM, Goyette G Jr, Ravindranath Y, and Ho YS. Red cells from glutathione peroxidase-1-deficient mice have nearly normal defenses against exogenous peroxides. Blood 96: 1985-1988, 2000.
    • (2000) Blood , vol.96 , pp. 1985-1988
    • Johnson, R.M.1    Goyette Jr., G.2    Ravindranath, Y.3    Ho, Y.S.4
  • 23
    • 33947204162 scopus 로고    scopus 로고
    • Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte
    • Low FM, Hampton MB, Peskin AV, and Winterbourn CC. Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood 109: 2611-2617, 2007.
    • (2007) Blood , vol.109 , pp. 2611-2617
    • Low, F.M.1    Hampton, M.B.2    Peskin, A.V.3    Winterbourn, C.C.4
  • 24
    • 46449103811 scopus 로고    scopus 로고
    • Peroxir-edoxin 2 and peroxide metabolism in the erythrocyte
    • Low FM, Hampton MB, and Winterbourn CC. Peroxir-edoxin 2 and peroxide metabolism in the erythrocyte. Anti-oxid Redox Signal 10: 1621-1630, 2008.
    • (2008) Anti-oxid Redox Signal , vol.10 , pp. 1621-1630
    • Low, F.M.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 25
    • 0037811713 scopus 로고    scopus 로고
    • Loss of selenium from selenoproteins: Conversion of selenocysteine to dehydroalanine in vitro
    • Ma S, Caprioli RM, Hill KE, and Burk RF. Loss of selenium from selenoproteins: conversion of selenocysteine to dehydroalanine in vitro. J Am Soc Mass Spectrom 14: 593-600, 2003.
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 593-600
    • Ma, S.1    Caprioli, R.M.2    Hill, K.E.3    Burk, R.F.4
  • 26
    • 0000474831 scopus 로고
    • Irreversible reaction of 3-amino-1:2:4-triazole and related inhibitors with the protein of catalase
    • Margoliash E, Novogrodsky A, and Schejter A. Irreversible reaction of 3-amino-1:2:4-triazole and related inhibitors with the protein of catalase. Biochem J 74: 339-348, 1960.
    • (1960) Biochem J , vol.74 , pp. 339-348
    • Margoliash, E.1    Novogrodsky, A.2    Schejter, A.3
  • 28
    • 0025996014 scopus 로고
    • Reconstitution of Ca(2\+)-dependent K\+ transport in erythrocyte membrane vesicles requires a cyto-plasmic protein
    • Moore RB, Mankad MV, Shriver SK, Mankad VN, and Plishker GA. Reconstitution of Ca(2\+)-dependent K\+ transport in erythrocyte membrane vesicles requires a cyto-plasmic protein. J Biol Chem 266: 18964-18968, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 18964-18968
    • Moore, R.B.1    Mankad, M.V.2    Shriver, S.K.3    Mankad, V.N.4    Plishker, G.A.5
  • 29
    • 0025779378 scopus 로고
    • Glucose-6-phosphate dehydrogenase activity and protein turnover in erythroblasts separated by velocity sedimentation at unit gravity and Percoll gradient centrifugation
    • Ninfali P, Palma F, Baronciani L, and Piacentini G. Glucose-6-phosphate dehydrogenase activity and protein turnover in erythroblasts separated by velocity sedimentation at unit gravity and Percoll gradient centrifugation. Mol Cell Biochem 106: 151-160, 1991.
    • (1991) Mol Cell Biochem , vol.106 , pp. 151-160
    • Ninfali, P.1    Palma, F.2    Baronciani, L.3    Piacentini, G.4
  • 30
    • 33847212487 scopus 로고    scopus 로고
    • Investigation of the stability of selenoproteins during storage of human serum by size-exclusion LC-ICP-MS
    • Palacios O and Lobinski R. Investigation of the stability of selenoproteins during storage of human serum by size-exclusion LC-ICP-MS. Talanta 71: 1813-1816, 2007.
    • (2007) Talanta , vol.71 , pp. 1813-1816
    • Palacios, O.1    Lobinski, R.2
  • 31
    • 34249703509 scopus 로고    scopus 로고
    • The high reactivity of peroxiredoxin 2 with H2O2 is not reflected in its reaction with other oxidants and thiol reagents
    • Peskin AV, Low FM, Paton LN, Maghzal GJ, Hampton MB, and Winterbourn CC. The high reactivity of peroxiredoxin 2 with H2O2 is not reflected in its reaction with other oxidants and thiol reagents. J Biol Chem 282: 11885-11892, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 11885-11892
    • Peskin, A.V.1    Low, F.M.2    Paton, L.N.3    Maghzal, G.J.4    Hampton, M.B.5    Winterbourn, C.C.6
  • 36
    • 0347600941 scopus 로고    scopus 로고
    • Regulation of the mammalian selenoprotein thioredoxin reductase 1 in relation to cellular phenotype, growth, and signaling events
    • Rundlof AK and Arner ES. Regulation of the mammalian selenoprotein thioredoxin reductase 1 in relation to cellular phenotype, growth, and signaling events. Antioxid Redox Signal 6: 41-52, 2004.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 41-52
    • Rundlof, A.K.1    Arner, E.S.2
  • 37
    • 0019944804 scopus 로고
    • Human erythrocyte separation according to age on a discontinuous "percoll" density gradient
    • Salvo GP, Caprari P, Samoggia P, Mariani G, and Salvati AM. Human erythrocyte separation according to age on a discontinuous "Percoll" density gradient. Clin Chim Acta 122: 293-300, 1982.
    • (1982) Clin Chim Acta , vol.122 , pp. 293-300
    • Salvo, G.P.1    Caprari, P.2    Samoggia, P.3    Mariani, G.4    Salvati, A.M.5
  • 39
    • 39749099462 scopus 로고    scopus 로고
    • Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: Application to glyceraldehyde-3-phosphate dehydrogenase
    • Seo J, Jeong J, Kim YM, Hwang N, Paek E, and Lee KJ. Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase. J Proteome Res 7: 587-602, 2008.
    • (2008) J Proteome Res , vol.7 , pp. 587-602
    • Seo, J.1    Jeong, J.2    Kim, Y.M.3    Hwang, N.4    Paek, E.5    Lee, K.J.6
  • 40
    • 35148867865 scopus 로고    scopus 로고
    • Mechanistic study on aniline-induced erythrocyte toxicity
    • Singh H, Purnell E, and Smith C. Mechanistic study on aniline-induced erythrocyte toxicity. Arh Hig Rada Toksikol 58: 275-285, 2007.
    • (2007) Arh Hig Rada Toksikol , vol.58 , pp. 275-285
    • Singh, H.1    Purnell, E.2    Smith, C.3
  • 41
    • 0016424755 scopus 로고
    • Substrate-induced redox change of selenium in glutathione peroxidase studied by X-ray photoelectron spectroscopy
    • Wendel A, Pilz W, Ladenstein R, Sawatzki G, and Weser U. Substrate-induced redox change of selenium in glutathione peroxidase studied by X-ray photoelectron spectroscopy. Biochim Biophys Acta 377: 211-215, 1975.
    • (1975) Biochim Biophys Acta , vol.377 , pp. 211-215
    • Wendel, A.1    Pilz, W.2    Ladenstein, R.3    Sawatzki, G.4    Weser, U.5
  • 42
    • 0022272178 scopus 로고
    • Free-radical production and oxidative reactions of hemoglobin
    • Winterbourn CC. Free-radical production and oxidative reactions of hemoglobin. Environ Health Perspect 64: 321-330, 1985.
    • (1985) Environ Health Perspect , vol.64 , pp. 321-330
    • Winterbourn, C.C.1
  • 43
    • 0017113866 scopus 로고
    • Reactions involving superoxide and normal and unstable haemoglobins
    • Winterbourn CC, McGrath BM, and Carrell RW. Reactions involving superoxide and normal and unstable haemoglobins. Biochem J 155: 493-502, 1976.
    • (1976) Biochem J , vol.155 , pp. 493-502
    • Winterbourn, C.C.1    McGrath, B.M.2    Carrell, R.W.3
  • 44
    • 0023600030 scopus 로고
    • Human red cells scavenge extracellular hydrogen peroxide and inhibit formation of hypochlorous acid and hydroxyl radical
    • Winterbourn CC and Stern A. Human red cells scavenge extracellular hydrogen peroxide and inhibit formation of hypochlorous acid and hydroxyl radical. J Clin Invest 80: 1486-1491, 1987.
    • (1987) J Clin Invest , vol.80 , pp. 1486-1491
    • Winterbourn, C.C.1    Stern, A.2
  • 45
    • 0028306066 scopus 로고
    • Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides
    • Wolff SS. Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides. Meth Enzymol 233: 182-189, 1994.
    • (1994) Meth Enzymol , vol.233 , pp. 182-189
    • Wolff, S.S.1
  • 46
    • 0242668688 scopus 로고    scopus 로고
    • Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
    • Woo HA, Chae HZ, Hwang SC, Yang KS, Kang SW, Kim K, and Rhee SG. Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science 300: 653-656, 2003.
    • (2003) Science , vol.300 , pp. 653-656
    • Woo, H.A.1    Chae, H.Z.2    Hwang, S.C.3    Yang, K.S.4    Kang, S.W.5    Kim, K.6    Rhee, S.G.7
  • 47
    • 13544272571 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins
    • Woo HA, Jeong W, Chang TS, Park KJ, Park SJ, Yang JS, and Rhee SG. Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. J Biol Chem 280: 3125-3128, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 3125-3128
    • Woo, H.A.1    Jeong, W.2    Chang, T.S.3    Park, K.J.4    Park, S.J.5    Yang, J.S.6    Rhee, S.G.7
  • 48
    • 0037064080 scopus 로고    scopus 로고
    • Inactivation of human peroxiredoxin i during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
    • Yang KS, Kang SW, Woo HA, Hwang SC, Chae HZ, Kim K, and Rhee SG. Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J Biol Chem 277: 38029-38036, 2002
    • (2002) J Biol Chem , vol.277 , pp. 38029-38036
    • Yang, K.S.1    Kang, S.W.2    Woo, H.A.3    Hwang, S.C.4    Chae, H.Z.5    Kim, K.6    Rhee, S.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.