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Volumn 193, Issue 1, 2003, Pages 1-8

Oxidation and detoxification of trivalent arsenic species

Author keywords

[No Author keywords available]

Indexed keywords

ALLOPURINOL; ARSENIC ACID; ARSENIC DERIVATIVE; ARSENIC TRIOXIDE; CATALASE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; MANNITOL; MELATONIN; METHANEARSONIC ACID; ORGANOARSENIC DERIVATIVE; POTASSIUM IODIDE; XANTHINE OXIDASE;

EID: 0242594013     PISSN: 0041008X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-008X(03)00324-7     Document Type: Article
Times cited : (112)

References (62)
  • 1
    • 0034667885 scopus 로고    scopus 로고
    • Arsenic species that cause release of iron from ferritin and generation of activated oxygen
    • Ahmad K., Kitchin K.T., Cullen W.R. Arsenic species that cause release of iron from ferritin and generation of activated oxygen. Arch. Biochem. Biophys. 382:2000;195-202.
    • (2000) Arch. Biochem. Biophys. , vol.382 , pp. 195-202
    • Ahmad, K.1    Kitchin, K.T.2    Cullen, W.R.3
  • 2
    • 0008517022 scopus 로고    scopus 로고
    • Enzymatic methylation of arsenic species and other new approaches to arsenic toxicity
    • Aposhian H.V. Enzymatic methylation of arsenic species and other new approaches to arsenic toxicity. Annu. Rev. Pharmacol. Toxicol. 37:1997;397-419.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 397-419
    • Aposhian, H.V.1
  • 5
    • 0033429247 scopus 로고    scopus 로고
    • Stimulation of reactive oxygen, but not reactive nitrogen species, in vascular endothelial cells exposed to low levels of arsenite
    • Barchowsky A., Klei L.R., Dudek E.J., Swartz H.M., James P.E. Stimulation of reactive oxygen, but not reactive nitrogen species, in vascular endothelial cells exposed to low levels of arsenite. Free Radical Biol. Med. 27:1999;1405-1412.
    • (1999) Free Radical Biol. Med. , vol.27 , pp. 1405-1412
    • Barchowsky, A.1    Klei, L.R.2    Dudek, E.J.3    Swartz, H.M.4    James, P.E.5
  • 7
    • 0032240291 scopus 로고    scopus 로고
    • Biochemistry of free radicals: From electrons to tissues
    • Boveris Alberto. Biochemistry of free radicals from electrons to tissues . Medicina (Buenos Aires). 58:1998;350-356.
    • (1998) Medicina (Buenos Aires) , vol.58 , pp. 350-356
    • Boveris Alberto1
  • 9
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sles H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59:1979;527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sles, H.2    Boveris, A.3
  • 10
    • 0014690530 scopus 로고
    • The role of molybdenum in xanthine oxidase and related enzymes
    • Coughlan M.P., Rajagopalan K.V., Handler P. The role of molybdenum in xanthine oxidase and related enzymes. J. Biol. Chem. 244:1969;2658-2663.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2658-2663
    • Coughlan, M.P.1    Rajagopalan, K.V.2    Handler, P.3
  • 12
    • 0034718556 scopus 로고    scopus 로고
    • Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
    • Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase structure-based mechanism of conversion . Proc. Natl. Acad. Sci. USA. 97:2000;10723-10728.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10723-10728
    • Enroth, C.1    Eger, B.T.2    Okamoto, K.3    Nishino, T.4    Nishino, T.5    Pai, E.F.6
  • 14
    • 0033936088 scopus 로고    scopus 로고
    • Biliary and urinary excretion of inorganic arsenic: Monomethylarsonous acid as a major biliary metabolite in rats
    • Gregus Z., Gyurasics A., Csanaky I. Biliary and urinary excretion of inorganic arsenic monomethylarsonous acid as a major biliary metabolite in rats . Toxicol. Sci. 56:2000;18-25.
    • (2000) Toxicol. Sci. , vol.56 , pp. 18-25
    • Gregus, Z.1    Gyurasics, A.2    Csanaky, I.3
  • 15
    • 0036848202 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylase as a cytosolic arsenate reductase
    • Gregus Z., Németi B. Purine nucleoside phosphorylase as a cytosolic arsenate reductase. Toxicol. Sci. 70:2002;13-19.
    • (2002) Toxicol. Sci. , vol.70 , pp. 13-19
    • Gregus, Z.1    Németi, B.2
  • 16
    • 0030793517 scopus 로고    scopus 로고
    • Enzymatic methylation of arsenic compounds. IV. In vitro and in vivo deficiency of the methylation of arsenite and monomethylarsonic acid in the guinea pig
    • Healy S.M., Zakharyan R.A., Aposhian H.V. Enzymatic methylation of arsenic compounds. IV. In vitro and in vivo deficiency of the methylation of arsenite and monomethylarsonic acid in the guinea pig. Mutat. Res. 386:1997;229-239.
    • (1997) Mutat. Res. , vol.386 , pp. 229-239
    • Healy, S.M.1    Zakharyan, R.A.2    Aposhian, H.V.3
  • 18
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille R. The mononuclear molybdenum enzymes. Chem. Rev. 96:1996;2757-2816.
    • (1996) Chem. Rev. , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 19
    • 0029347181 scopus 로고
    • Xanthine oxidase and xanthine dehydrogenase
    • Hille R., Nishino T. Xanthine oxidase and xanthine dehydrogenase. FASEB J. 9:1995;995-1003.
    • (1995) FASEB J. , vol.9 , pp. 995-1003
    • Hille, R.1    Nishino, T.2
  • 20
    • 0020537753 scopus 로고
    • The interaction of arsenite with xanthine oxidase
    • Hille R., Stewart R.C., Fee J.A., Massey V. The interaction of arsenite with xanthine oxidase. J. Biol. Chem. 258:1983;4849-4856.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4849-4856
    • Hille, R.1    Stewart, R.C.2    Fee, J.A.3    Massey, V.4
  • 21
    • 0035194165 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling
    • Hoidal J.R. Reactive oxygen species and cell signaling. Am. J. Respir. Cell Mol. Biol. 25:2001;661-663.
    • (2001) Am. J. Respir. Cell Mol. Biol. , vol.25 , pp. 661-663
    • Hoidal, J.R.1
  • 22
    • 0037036578 scopus 로고    scopus 로고
    • Arsenic toxicity and potential mechanisms of action
    • Hughes M.F. Arsenic toxicity and potential mechanisms of action. Toxicol. Lett. 133:2002;1-16.
    • (2002) Toxicol. Lett. , vol.133 , pp. 1-16
    • Hughes, M.F.1
  • 25
    • 0027438935 scopus 로고
    • Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): Structural analysis of the protein and chromosomal location of the gene
    • Ichida K., Amaya Y., Noda K., Minoshima S., Hosoya T., Sakai O., Shimizu N., Nishino T. Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase) structural analysis of the protein and chromosomal location of the gene . Gene. 133:1993;279-284.
    • (1993) Gene , vol.133 , pp. 279-284
    • Ichida, K.1    Amaya, Y.2    Noda, K.3    Minoshima, S.4    Hosoya, T.5    Sakai, O.6    Shimizu, N.7    Nishino, T.8
  • 26
    • 0034721764 scopus 로고    scopus 로고
    • The MRP2/cMOAT transporter and arsenic-glutathione complex formation are required for biliary excretion of arsenic
    • Kala S.V., Neely M.W., Kala G., Prater C.I., Atwood D.W., Rice J.S., Lieberman M.W. The MRP2/cMOAT transporter and arsenic-glutathione complex formation are required for biliary excretion of arsenic. J. Biol. Chem. 275:2000;33404-33408.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33404-33408
    • Kala, S.V.1    Neely, M.W.2    Kala, G.3    Prater, C.I.4    Atwood, D.W.5    Rice, J.S.6    Lieberman, M.W.7
  • 28
    • 0034329575 scopus 로고    scopus 로고
    • Speciation of key arsenic metabolic intermediates in human urine
    • Le X.C., Lu X., Ma M., Cullen W.R., Aposhian H.V., Zheng B. Speciation of key arsenic metabolic intermediates in human urine. Ana. Chem. 72:2000;5172-5177.
    • (2000) Ana. Chem. , vol.72 , pp. 5172-5177
    • Le, X.C.1    Lu, X.2    Ma, M.3    Cullen, W.R.4    Aposhian, H.V.5    Zheng, B.6
  • 29
    • 0033675692 scopus 로고    scopus 로고
    • Determination of monomethylarsonous acid, a key arsenic methylation intermediate, in human urine
    • Le X.C., Ma M., Lu X., Cullen W.R., Aposhian H.V., Zheng B. Determination of monomethylarsonous acid, a key arsenic methylation intermediate, in human urine. Environ. Health Perspect. 108:2000;1015-1018.
    • (2000) Environ. Health Perspect. , vol.108 , pp. 1015-1018
    • Le, X.C.1    Ma, M.2    Lu, X.3    Cullen, W.R.4    Aposhian, H.V.5    Zheng, B.6
  • 30
    • 0035852735 scopus 로고    scopus 로고
    • Induction of oxyradicals by arsenic: Implication for mechanism of genotoxicity
    • Liu S.X., Athar M., Lippai I., Waldren C., Hei Tom K. Induction of oxyradicals by arsenic implication for mechanism of genotoxicity . Proc. Natl. Acad. Sci. USA. 98:2001;1643-1648.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1643-1648
    • Liu, S.X.1    Athar, M.2    Lippai, I.3    Waldren, C.4    Hei Tom, K.5
  • 31
    • 0036544597 scopus 로고    scopus 로고
    • Xanthine oxidase and aldehyde oxidase: A simple procedure for the simultaneous purification from rat liver
    • Maia L., Mira L. Xanthine oxidase and aldehyde oxidase a simple procedure for the simultaneous purification from rat liver . Arch. Biochem. Biophys. 400:2002;48-53.
    • (2002) Arch. Biochem. Biophys. , vol.400 , pp. 48-53
    • Maia, L.1    Mira, L.2
  • 32
    • 0035056158 scopus 로고    scopus 로고
    • Identification of dimethylarsinous and monomethylarsonous acids in human urine of the arsenic-affected areas in West Bengal, India
    • Mandal B.K., Ogra Y., Suzuki K.T. Identification of dimethylarsinous and monomethylarsonous acids in human urine of the arsenic-affected areas in West Bengal, India. Chem. Res. Toxicol. 14:2001;371-378.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 371-378
    • Mandal, B.K.1    Ogra, Y.2    Suzuki, K.T.3
  • 33
    • 0025805681 scopus 로고
    • Purification and characterization of peroxisomal L-pipecolic acid oxidase from monkey liver
    • Mihalik S.J., McGuinness M., Watkins P.A. Purification and characterization of peroxisomal L-pipecolic acid oxidase from monkey liver. J. Biol. Chem. 266:1991;4822-4830.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4822-4830
    • Mihalik, S.J.1    McGuinness, M.2    Watkins, P.A.3
  • 34
    • 0024501676 scopus 로고
    • L-pipecolic acid oxidation in the rabbit and cynomolgus monkey: Evidence for differing organellar locations and cofactor requirements in each species
    • Mihalik S.J., Rhead W.J. L-pipecolic acid oxidation in the rabbit and cynomolgus monkey evidence for differing organellar locations and cofactor requirements in each species . J. Biol. Chem. 264:1989;2509-2517.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2509-2517
    • Mihalik, S.J.1    Rhead, W.J.2
  • 35
    • 0036849298 scopus 로고    scopus 로고
    • Reduction of arsenate to arsenite in hepatic cytosol
    • Németi B., Gregus Z. Reduction of arsenate to arsenite in hepatic cytosol. Toxicol. Sci. 70:2002;4-12.
    • (2002) Toxicol. Sci. , vol.70 , pp. 4-12
    • Németi, B.1    Gregus, Z.2
  • 36
    • 0037150531 scopus 로고    scopus 로고
    • Worldwide occurrences of arsenic in ground water
    • Nordstrom D.K. Worldwide occurrences of arsenic in ground water. Science. 296:2002;2143-2145.
    • (2002) Science , vol.296 , pp. 2143-2145
    • Nordstrom, D.K.1
  • 37
    • 0022502428 scopus 로고
    • Xanthine oxidase: Biochemistry distribution and physiology
    • Parks D.A., Granger D.N. Xanthine oxidase biochemistry distribution and physiology . Acta Physiol. Scand. 548:1986;87-99.
    • (1986) Acta Physiol. Scand. , vol.548 , pp. 87-99
    • Parks, D.A.1    Granger, D.N.2
  • 38
    • 0006676703 scopus 로고
    • Effect of arsenite and cadmium ions on xanthine oxidase
    • Peters J.M., Sanadi D.R. Effect of arsenite and cadmium ions on xanthine oxidase. Arch. Biochem. Biophys. 93:1961;312-313.
    • (1961) Arch. Biochem. Biophys. , vol.93 , pp. 312-313
    • Peters, J.M.1    Sanadi, D.R.2
  • 43
    • 0036093079 scopus 로고    scopus 로고
    • Arsenate reductase II. Purine nucleoside phosphorylase in the presence of dihydrolipoic acid is a route for reduction of arsenate to arsenite in mammalian systems
    • Radabaugh T.R., Sampayo-Reyes A., Zakharyan R.A., Aposhian H.V. Arsenate reductase II. Purine nucleoside phosphorylase in the presence of dihydrolipoic acid is a route for reduction of arsenate to arsenite in mammalian systems. Chem. Res. Toxicol. 15:2002;692-698.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 692-698
    • Radabaugh, T.R.1    Sampayo-Reyes, A.2    Zakharyan, R.A.3    Aposhian, H.V.4
  • 44
    • 0017367539 scopus 로고
    • 74As-labeled arsenate and arsenite for use in biological experiments
    • 74As-labeled arsenate and arsenite for use in biological experiments. Anal. Biochem. 78:1977;557-560.
    • (1977) Anal. Biochem. , vol.78 , pp. 557-560
    • Reay, P.F.1    Asher, C.J.2
  • 45
    • 0035473801 scopus 로고    scopus 로고
    • Arsenite is a cocarcinogen with solar ultraviolet radiation for mouse skin: An animal model for arsenic carcinogenesis
    • Rossman T.G., Uddin A.N., Burns F.J., Bosland M.C. Arsenite is a cocarcinogen with solar ultraviolet radiation for mouse skin an animal model for arsenic carcinogenesis . Toxicol. Appl. Pharmacol. 176:2001;64-71.
    • (2001) Toxicol. Appl. Pharmacol. , vol.176 , pp. 64-71
    • Rossman, T.G.1    Uddin, A.N.2    Burns, F.J.3    Bosland, M.C.4
  • 47
  • 49
    • 0021740944 scopus 로고
    • Characterization of arsenite-complexed xanthine oxidase at room temperature
    • Stewart R.C., Hille R., Massey V. Characterization of arsenite-complexed xanthine oxidase at room temperature. J. Biol. Chem. 259:1984;14426-14436.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14426-14436
    • Stewart, R.C.1    Hille, R.2    Massey, V.3
  • 51
    • 0025024869 scopus 로고
    • Long-term effects of peroxisome proliferators on the balance between hydrogen peroxide-generating and scavenging capacities in the liver of Fisher-344 rats
    • Tamura H., Iida T., Watanabe T., Suga T. Long-term effects of peroxisome proliferators on the balance between hydrogen peroxide-generating and scavenging capacities in the liver of Fisher-344 rats. Toxicology. 63:1990;199-213.
    • (1990) Toxicology , vol.63 , pp. 199-213
    • Tamura, H.1    Iida, T.2    Watanabe, T.3    Suga, T.4
  • 52
    • 0029417335 scopus 로고
    • 2-generating NADH oxidase in human lung fibroblasts by transforming growth factor β1
    • 2-generating NADH oxidase in human lung fibroblasts by transforming growth factor β1. J. Biol. Chem. 270:1995;30334-30338.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30334-30338
    • Thannickal, V.J.1    Fanburg, B.L.2
  • 53
    • 0034759637 scopus 로고    scopus 로고
    • The cellular metabolism and systemic toxicity of arsenic
    • Thomas D.J., Styblo M., Lin S. The cellular metabolism and systemic toxicity of arsenic. Toxicol. Appl. Pharmacol. 176:2001;127-144.
    • (2001) Toxicol. Appl. Pharmacol. , vol.176 , pp. 127-144
    • Thomas, D.J.1    Styblo, M.2    Lin, S.3
  • 54
    • 84989576535 scopus 로고
    • Species differences in the metabolism of arsenic compounds
    • Vahter M. Species differences in the metabolism of arsenic compounds. Appl. Organomet. Chem. 8:1994;175-182.
    • (1994) Appl. Organomet. Chem. , vol.8 , pp. 175-182
    • Vahter, M.1
  • 56
    • 0001396383 scopus 로고
    • In vivo methylation and detoxication of arsenic
    • P.J. Craig, & F. Glocking. London: Royal Society of Chemistry, Special Publication
    • Vahter M., Marafante E. In vivo methylation and detoxication of arsenic. Craig P.J., Glocking F. The Biological Alkylation of Heavy Elements. 66:1988;105-119 Royal Society of Chemistry, Special Publication, London.
    • (1988) The Biological Alkylation of Heavy Elements , vol.66 , pp. 105-119
    • Vahter, M.1    Marafante, E.2
  • 58
    • 0035976392 scopus 로고    scopus 로고
    • Enzymatic methylation of arsenic compounds. IX. Liver arsenite methyltransferase and arsenate reductase activities in primates
    • Wildfang E., Radabaugh T.R., Aposhian H.V. Enzymatic methylation of arsenic compounds. IX. Liver arsenite methyltransferase and arsenate reductase activities in primates. Toxicology. 168:2001;213-221.
    • (2001) Toxicology , vol.168 , pp. 213-221
    • Wildfang, E.1    Radabaugh, T.R.2    Aposhian, H.V.3
  • 60
    • 0030247067 scopus 로고    scopus 로고
    • Enzymatic methylation of arsenic compounds. III. The marmoset and tamarin, but not the rhesus, monkey are deficient in methyltransferase that methylate inorganic arsenic
    • Zakharyan R.A., Wildfang E., Aposhian H.V. Enzymatic methylation of arsenic compounds. III. The marmoset and tamarin, but not the rhesus, monkey are deficient in methyltransferase that methylate inorganic arsenic. Toxicol. Appl. Pharmacol. 140:1996;77-84.
    • (1996) Toxicol. Appl. Pharmacol. , vol.140 , pp. 77-84
    • Zakharyan, R.A.1    Wildfang, E.2    Aposhian, H.V.3
  • 61
    • 0028861888 scopus 로고
    • Enzymatic methylation of arsenic compounds: Assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver
    • Zakharyan R.A., Wu Y., Bogdan G.M., Aposhian H.V. Enzymatic methylation of arsenic compounds assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver . Chem. Res. Toxicol. 8:1995;1029-1038.
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 1029-1038
    • Zakharyan, R.A.1    Wu, Y.2    Bogdan, G.M.3    Aposhian, H.V.4
  • 62
    • 0030885707 scopus 로고    scopus 로고
    • Association of arsenic-induced malignant transformation with DNA hypomethylation and aberrant gene expression
    • Zhao C.Q., Young M.R., Diwan B.A., Coogan T.P., Waalkes M.P. Association of arsenic-induced malignant transformation with DNA hypomethylation and aberrant gene expression. Proc. Natl. Acad. Sci. USA. 94:1997;10907-10912.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10907-10912
    • Zhao, C.Q.1    Young, M.R.2    Diwan, B.A.3    Coogan, T.P.4    Waalkes, M.P.5


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