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Volumn 40, Issue 6, 2003, Pages 632-642

Methemoglobinemia and eccentrocytosis in equine erythrocyte flavin adenine dinucleotide deficiency

Author keywords

Cytochrome b5; Eccentrocytes; Erythrocytes; FAD; Flavin adenine dinucleotide; Glutathione reductase deficiency; Methemoglobinemia; Reductase deficiency; Riboflavin

Indexed keywords

CYTOCHROME B5 REDUCTASE; FLAVINE ADENINE NUCLEOTIDE; GLUTATHIONE; GLUTATHIONE REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; CYTOCHROME REDUCTASE; RIBOFLAVIN;

EID: 1542706086     PISSN: 03009858     EISSN: None     Source Type: Journal    
DOI: 10.1354/vp.40-6-632     Document Type: Article
Times cited : (21)

References (50)
  • 1
    • 0016301268 scopus 로고
    • Studies on glucose-6-phosphate dehydrogenase, glutathione reductase and regeneration of reduced glutathione in the red blood cells of various mammalian species
    • Agar NS, Gruca M, Harley JD: Studies on glucose-6-phosphate dehydrogenase, glutathione reductase and regeneration of reduced glutathione in the red blood cells of various mammalian species. Aust J Exp Biol Med Sci 52:607-614, 1974
    • (1974) Aust J Exp Biol Med Sci , vol.52 , pp. 607-614
    • Agar, N.S.1    Gruca, M.2    Harley, J.D.3
  • 2
    • 0015393838 scopus 로고
    • Effect of primaquine on erythrocytes with NADH-methaemoglobin reductase deficiency and low glutathione reductase activity
    • Ajmar F, Gaetani G, Garre C, Bianchi G, Salvidio E: Effect of primaquine on erythrocytes with NADH-methaemoglobin reductase deficiency and low glutathione reductase activity. Br J Haematol 23:333-341, 1972
    • (1972) Br J Haematol , vol.23 , pp. 333-341
    • Ajmar, F.1    Gaetani, G.2    Garre, C.3    Bianchi, G.4    Salvidio, E.5
  • 3
    • 0027198723 scopus 로고
    • Low red blood cell glutathione reductase and pyridoxine phosphate oxidase activities not related to dietary riboflavin: Selection by malaria?
    • Anderson BB, Giuberti M, Perry GM, Salsini G, Casadio I, Vullo C: Low red blood cell glutathione reductase and pyridoxine phosphate oxidase activities not related to dietary riboflavin: selection by malaria? Am J Clin Nutr 57:666-672, 1993
    • (1993) Am J Clin Nutr , vol.57 , pp. 666-672
    • Anderson, B.B.1    Giuberti, M.2    Perry, G.M.3    Salsini, G.4    Casadio, I.5    Vullo, C.6
  • 4
    • 0014592051 scopus 로고
    • Effect of flavin compounds on glutathione reductase activity: In vivo and in vitro studies
    • Beutler E: Effect of flavin compounds on glutathione reductase activity: in vivo and in vitro studies. J Clin Invest 48:1957-1966, 1969
    • (1969) J Clin Invest , vol.48 , pp. 1957-1966
    • Beutler, E.1
  • 6
    • 0019809213 scopus 로고
    • Methaemoglobinaemia resulting from heterozygosity of two NADH-methaemoglobin reductase variants: Characterization as NADH-ferricyanide reductase
    • Board PG, Pidcock ME: Methaemoglobinaemia resulting from heterozygosity of two NADH-methaemoglobin reductase variants: characterization as NADH-ferricyanide reductase. Br J Haematol 47:361-370, 1981
    • (1981) Br J Haematol , vol.47 , pp. 361-370
    • Board, P.G.1    Pidcock, M.E.2
  • 7
    • 0024970081 scopus 로고
    • Relation of endogenous Heinz bodies to disease and anemia in cats: 120 Cases (1978-1987)
    • Christopher MM: Relation of endogenous Heinz bodies to disease and anemia in cats: 120 cases (1978-1987). J Am Vet Med Assoc 194:1089-1095, 1989
    • (1989) J Am Vet Med Assoc , vol.194 , pp. 1089-1095
    • Christopher, M.M.1
  • 11
    • 0017545726 scopus 로고
    • Familial methaemoglobinaemia and haemolytic anaemia in the horse associated with decreased erythrocytic glutathione reductase and glutathione
    • Dixon PM, McPherson EA: Familial methaemoglobinaemia and haemolytic anaemia in the horse associated with decreased erythrocytic glutathione reductase and glutathione. Equine Vet J 9:198-201, 1977
    • (1977) Equine Vet J , vol.9 , pp. 198-201
    • Dixon, P.M.1    McPherson, E.A.2
  • 12
    • 0028247881 scopus 로고
    • Optimal and stable conditions for the determination of erythrocyte glutathione reductase activation coefficient to evaluate riboflavin status
    • Dror Y, Stern F, Komarnitsky M: Optimal and stable conditions for the determination of erythrocyte glutathione reductase activation coefficient to evaluate riboflavin status. Int J Vitam Nutr Res 64:257-262, 1994
    • (1994) Int J Vitam Nutr Res , vol.64 , pp. 257-262
    • Dror, Y.1    Stern, F.2    Komarnitsky, M.3
  • 13
    • 0030768203 scopus 로고    scopus 로고
    • Oxidatively damaged erythrocytes are recognized by membrane proteins of macrophages
    • Eda S, Kikugawa K, Beppu M: Oxidatively damaged erythrocytes are recognized by membrane proteins of macrophages. Free Radic Res 27:23-30, 1997
    • (1997) Free Radic Res , vol.27 , pp. 23-30
    • Eda, S.1    Kikugawa, K.2    Beppu, M.3
  • 14
    • 0022517018 scopus 로고
    • Transcellular cross bonding of red blood cell membrane
    • Fischer TM: Transcellular cross bonding of red blood cell membrane. Biochim Biophys Acta 861:277-286, 1986
    • (1986) Biochim Biophys Acta , vol.861 , pp. 277-286
    • Fischer, T.M.1
  • 15
    • 0021967304 scopus 로고
    • Membrane cross bonding in red cells in favic crises: A missing link in the mechanism of extravascular haemolysis
    • Fischer TM, Meloni T, Pescarmona GP, Arese P: Membrane cross bonding in red cells in favic crises: a missing link in the mechanism of extravascular haemolysis. Br J Haematol 59:159-169, 1985
    • (1985) Br J Haematol , vol.59 , pp. 159-169
    • Fischer, T.M.1    Meloni, T.2    Pescarmona, G.P.3    Arese, P.4
  • 16
    • 0021950081 scopus 로고
    • High performance liquid chromatographic analysis of flavin adenine dinucleotide in whole blood
    • Floridi A, Palmerini CA, Fini C, Pupita M, Fidanza F: High performance liquid chromatographic analysis of flavin adenine dinucleotide in whole blood. Int J Vitam Nutr Res 55:187-191, 1985
    • (1985) Int J Vitam Nutr Res , vol.55 , pp. 187-191
    • Floridi, A.1    Palmerini, C.A.2    Fini, C.3    Pupita, M.4    Fidanza, F.5
  • 17
    • 0015820609 scopus 로고
    • Influence of riboflavin and of erythrocyte stroma on glutathione reductase activity in normal, glucose 6 phosphate dehydrogenase deficient and low glutathione reductase individuals
    • Gaetani GF, Garre C, Ajmar F, Bianchi GL: Influence of riboflavin and of erythrocyte stroma on glutathione reductase activity in normal, glucose 6 phosphate dehydrogenase deficient and low glutathione reductase individuals. Biomedicine 19:469-474, 1973
    • (1973) Biomedicine , vol.19 , pp. 469-474
    • Gaetani, G.F.1    Garre, C.2    Ajmar, F.3    Bianchi, G.L.4
  • 18
    • 0012927348 scopus 로고    scopus 로고
    • The erythrocyte: Physiology, metabolism and biochemical disorders
    • ed. Kaneko JJ, Harvey JW, and Bruss ML, 5th ed., Academic Press, San Diego, CA
    • Harvey JW: The erythrocyte: physiology, metabolism and biochemical disorders. In: Clinical Biochemistry of Domestic Animals, ed. Kaneko JJ, Harvey JW, and Bruss ML, 5th ed., pp. 157-203. Academic Press, San Diego, CA, 1997
    • (1997) Clinical Biochemistry of Domestic Animals , pp. 157-203
    • Harvey, J.W.1
  • 19
    • 1642327895 scopus 로고    scopus 로고
    • Hereditary methemoglobinemia
    • ed. Feldman BF, Zinkl JG, and Jain NC, 5th ed., Lippincott Williams & Wilkins, Philadelphia, PA
    • Harvey JW: Hereditary methemoglobinemia. In: Schalm's Veterinary Hematology, ed. Feldman BF, Zinkl JG, and Jain NC, 5th ed., pp. 1008-1011. Lippincott Williams & Wilkins, Philadelphia, PA, 2000
    • (2000) Schalm's Veterinary Hematology , pp. 1008-1011
    • Harvey, J.W.1
  • 21
    • 0016835085 scopus 로고
    • Mammalian erythrocyte glutathione reductase: Kinetic constants and saturation with cofactor
    • Harvey JW, Kaneko JJ: Mammalian erythrocyte glutathione reductase: kinetic constants and saturation with cofactor. Am J Vet Res 36:1511-1513, 1975
    • (1975) Am J Vet Res , vol.36 , pp. 1511-1513
    • Harvey, J.W.1    Kaneko, J.J.2
  • 22
    • 0017707562 scopus 로고
    • Mammalian erythrocyte metabolism and oxidant drugs
    • Harvey JW, Kaneko JJ: Mammalian erythrocyte metabolism and oxidant drugs. Toxicol Appl Pharmacol 42: 253-261, 1977
    • (1977) Toxicol Appl Pharmacol , vol.42 , pp. 253-261
    • Harvey, J.W.1    Kaneko, J.J.2
  • 26
    • 0019770316 scopus 로고
    • Congenital methaemoglobinaemia due to NADH methemoglobin reductase deficiency: Successful treatment with oral riboflavin
    • Hirano M, Matsuki T, Tanishima K, Takeshita M, Shimizu S, Nagamura Y, Yoneyama Y: Congenital methaemoglobinaemia due to NADH methemoglobin reductase deficiency: successful treatment with oral riboflavin. Br J Haematol 47:353-359, 1981
    • (1981) Br J Haematol , vol.47 , pp. 353-359
    • Hirano, M.1    Matsuki, T.2    Tanishima, K.3    Takeshita, M.4    Shimizu, S.5    Nagamura, Y.6    Yoneyama, Y.7
  • 27
    • 0022412491 scopus 로고
    • Characteristics of hexokinase, pyruvate kinase, and glucose-6-phosphate dehydrogenase during adult and neonatal reticulocyte maturation
    • Jansen G, Koenderman L, Rijksen G, Cats BP, Staal GEJ: Characteristics of hexokinase, pyruvate kinase, and glucose-6-phosphate dehydrogenase during adult and neonatal reticulocyte maturation. Am J Hematol 20:203-215, 1985
    • (1985) Am J Hematol , vol.20 , pp. 203-215
    • Jansen, G.1    Koenderman, L.2    Rijksen, G.3    Cats, B.P.4    Staal, G.E.J.5
  • 28
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P, Lamas S: Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem 267:4928-4944, 2000
    • (2000) Eur J Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 29
    • 0025344772 scopus 로고
    • Riboflavin deficiency and the function and fluidity of rat erythrocyte membranes
    • Levin G, Cogan U, Levy Y, Mokady S: Riboflavin deficiency and the function and fluidity of rat erythrocyte membranes. J Nutr 120:857-861, 1990
    • (1990) J Nutr , vol.120 , pp. 857-861
    • Levin, G.1    Cogan, U.2    Levy, Y.3    Mokady, S.4
  • 30
    • 0017062372 scopus 로고
    • Familial deficiency of glutathione reductase in human blood cells
    • Loos H, Roos D, Weening R, Houwerzijl J: Familial deficiency of glutathione reductase in human blood cells. Blood 48:53-62, 1976
    • (1976) Blood , vol.48 , pp. 53-62
    • Loos, H.1    Roos, D.2    Weening, R.3    Houwerzijl, J.4
  • 31
    • 0006164136 scopus 로고
    • Species differences in erythrocyte glutathione reduction rates after oxidation with t-butyl hydroperoxide
    • Mahaffey E, Smith JE: Species differences in erythrocyte glutathione reduction rates after oxidation with t-butyl hydroperoxide. Int J Biochem 6:853-854, 1975
    • (1975) Int J Biochem , vol.6 , pp. 853-854
    • Mahaffey, E.1    Smith, J.E.2
  • 32
    • 0014863883 scopus 로고
    • Synthesis of riboflavin nucleotides by mature human erythrocytes
    • Mandula B, Beutler E: Synthesis of riboflavin nucleotides by mature human erythrocytes. Blood 36:491-499, 1970
    • (1970) Blood , vol.36 , pp. 491-499
    • Mandula, B.1    Beutler, E.2
  • 35
    • 0015507629 scopus 로고
    • Erythrocyte NADH-methemoglobin reductase activity in experimental riboflavin deficiency
    • Nicolaisen K, Rogers LE: Erythrocyte NADH-methemoglobin reductase activity in experimental riboflavin deficiency. Experientia 28:263-264, 1972
    • (1972) Experientia , vol.28 , pp. 263-264
    • Nicolaisen, K.1    Rogers, L.E.2
  • 36
    • 26144470957 scopus 로고
    • A missense mutation in the glucose-6-phosphate dehydrogenase gene associated with hemolytic anemia in an American saddlebred horse
    • Abstract
    • Nonneman D, Stockham SL, Shibuya H, Messer NT, Johnson GS: A missense mutation in the glucose-6-phosphate dehydrogenase gene associated with hemolytic anemia in an American saddlebred horse. Blood 82(Suppl 1):466a, 1993 [Abstract]
    • (1993) Blood , vol.82 , Issue.1 SUPPL.
    • Nonneman, D.1    Stockham, S.L.2    Shibuya, H.3    Messer, N.T.4    Johnson, G.S.5
  • 37
    • 0014958875 scopus 로고
    • Glutathione metabolism of the red cells. Effect of glutathione reductase deficiency on the stimulation of hexose monophosphate shunt under oxidative stress
    • Paniker NV, Srivastava SK, Beutler E: Glutathione metabolism of the red cells. Effect of glutathione reductase deficiency on the stimulation of hexose monophosphate shunt under oxidative stress. Biochim Biophys Acta 215: 456-460, 1970
    • (1970) Biochim Biophys Acta , vol.215 , pp. 456-460
    • Paniker, N.V.1    Srivastava, S.K.2    Beutler, E.3
  • 38
    • 0025906046 scopus 로고
    • Utilization of red-cell FAD by methaemoglobin reductases at the expense of glutathione reductase in heterozygous beta-thalassaemia
    • Perry GM, Anderson BB: Utilization of red-cell FAD by methaemoglobin reductases at the expense of glutathione reductase in heterozygous beta-thalassaemia. Eur J Haematol 46:290-295, 1991
    • (1991) Eur J Haematol , vol.46 , pp. 290-295
    • Perry, G.M.1    Anderson, B.B.2
  • 40
    • 0016692703 scopus 로고
    • The effect of phlebotomy on canine erythrocyte metabolism
    • Smith JE, Agar NS: The effect of phlebotomy on canine erythrocyte metabolism. Res Vet Sci 18:231-236, 1975
    • (1975) Res Vet Sci , vol.18 , pp. 231-236
    • Smith, J.E.1    Agar, N.S.2
  • 42
    • 0014589030 scopus 로고
    • The transport of oxidized glutathione from the erythrocytes of various species in the presence of chromate
    • Srivastava SK, Beutler E: The transport of oxidized glutathione from the erythrocytes of various species in the presence of chromate. Biochem J 114:833-837, 1969
    • (1969) Biochem J , vol.114 , pp. 833-837
    • Srivastava, S.K.1    Beutler, E.2
  • 43
    • 0028510509 scopus 로고
    • Equine glucose-6-phosphate dehydrogenase deficiency
    • Stockham SL, Harvey JW, Kinden DA: Equine glucose-6-phosphate dehydrogenase deficiency. Vet Pathol 31: 518-527, 1994
    • (1994) Vet Pathol , vol.31 , pp. 518-527
    • Stockham, S.L.1    Harvey, J.W.2    Kinden, D.A.3
  • 44
    • 0028081399 scopus 로고
    • Single extraction method for the spectrophotometric quantification of oxidized and reduced pyridine nucleotides in erythrocytes
    • Wagner TC, Scott MD: Single extraction method for the spectrophotometric quantification of oxidized and reduced pyridine nucleotides in erythrocytes. Anal Biochem 222:417-426, 1994
    • (1994) Anal Biochem , vol.222 , pp. 417-426
    • Wagner, T.C.1    Scott, M.D.2
  • 45
    • 0026543468 scopus 로고
    • Neutrophil-induced immunoglobulin binding to erythrocytes involves proteolytic and oxidative injury
    • Weiss DJ, Aird B, Murtaugh MP: Neutrophil-induced immunoglobulin binding to erythrocytes involves proteolytic and oxidative injury. J Leukoc Biol 51:19-23, 1992
    • (1992) J Leukoc Biol , vol.51 , pp. 19-23
    • Weiss, D.J.1    Aird, B.2    Murtaugh, M.P.3
  • 46
    • 0025083101 scopus 로고
    • Inflammation and cancer: Role of phagocyte-generated oxidants in carcinogenesis
    • Weitzman SA, Gordon LI: Inflammation and cancer: role of phagocyte-generated oxidants in carcinogenesis. Blood 76:655-663, 1990
    • (1990) Blood , vol.76 , pp. 655-663
    • Weitzman, S.A.1    Gordon, L.I.2
  • 47
    • 0015987973 scopus 로고
    • Regulatory mechanism of glutathione reductase activity in human red cells
    • Yawata Y, Tanaka KR: Regulatory mechanism of glutathione reductase activity in human red cells. Blood 43: 99-109, 1974
    • (1974) Blood , vol.43 , pp. 99-109
    • Yawata, Y.1    Tanaka, K.R.2
  • 48
    • 0017401042 scopus 로고
    • NADPH-flavin reductase in human erythrocytes and the reduction of methemoglobin through flavin by the enzyme
    • Yubisui T, Matsuki T, Tanishima K, Takeshita M, Yoneyama Y: NADPH-flavin reductase in human erythrocytes and the reduction of methemoglobin through flavin by the enzyme. Biochem Biophys Res Commun 76:174-182, 1977
    • (1977) Biochem Biophys Res Commun , vol.76 , pp. 174-182
    • Yubisui, T.1    Matsuki, T.2    Tanishima, K.3    Takeshita, M.4    Yoneyama, Y.5
  • 49
    • 0026462089 scopus 로고
    • The transport of thiamine, riboflavin, and pyridoxal 5′-phosphate by human placenta
    • Zempleni J, Link G, Kubler W: The transport of thiamine, riboflavin, and pyridoxal 5′-phosphate by human placenta. Int J Vitam Nutr Res 62:165-172, 1992
    • (1992) Int J Vitam Nutr Res , vol.62 , pp. 165-172
    • Zempleni, J.1    Link, G.2    Kubler, W.3
  • 50
    • 0023221206 scopus 로고
    • Spectrophotometric determination of oxidized and reduced pyridine nucleotides in erythrocytes using a single extraction procedure
    • Zerez CR, Lee SJ, Tanaka KR: Spectrophotometric determination of oxidized and reduced pyridine nucleotides in erythrocytes using a single extraction procedure. Anal Biochem 164:367-373, 1987
    • (1987) Anal Biochem , vol.164 , pp. 367-373
    • Zerez, C.R.1    Lee, S.J.2    Tanaka, K.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.