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Volumn 264, Issue 1, 2012, Pages 121-130

Methylation of arsenic by recombinant human wild-type arsenic (+3 oxidation state) methyltransferase and its methionine 287 threonine (M287T) polymorph: Role of glutathione

Author keywords

Arsenic methylation; AS3MT polymorphism; Glutathione; Thioredoxin reductase

Indexed keywords

ARSENIC; ARSENIC METHYLTRANSFERASE; ARSENIC TRIOXIDE; CACODYLIC ACID; GLUTATHIONE; METHANEARSONIC ACID; METHIONINE; S ADENOSYLMETHIONINE; THIOREDOXIN REDUCTASE; THREONINE; UNCLASSIFIED DRUG;

EID: 84865980440     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2012.07.024     Document Type: Article
Times cited : (46)

References (43)
  • 2
    • 84889770800 scopus 로고
    • Biological methylation
    • Challenger F. Biological methylation. Adv. Enzymol. 1951, 12:429-491.
    • (1951) Adv. Enzymol. , vol.12 , pp. 429-491
    • Challenger, F.1
  • 3
    • 81855168354 scopus 로고    scopus 로고
    • Mouse arsenic (+3 oxidation state) methyltransferase genotype affects metabolism and tissue dosimetry of arsenicals after arsenite administration in drinking water
    • Chen B., Arnold L.L., Cohen S.M., Thomas D.J., Le X.C. Mouse arsenic (+3 oxidation state) methyltransferase genotype affects metabolism and tissue dosimetry of arsenicals after arsenite administration in drinking water. Toxicol. Sci. 2011, 124:320-326.
    • (2011) Toxicol. Sci. , vol.124 , pp. 320-326
    • Chen, B.1    Arnold, L.L.2    Cohen, S.M.3    Thomas, D.J.4    Le, X.C.5
  • 5
    • 0021263213 scopus 로고
    • The reduction of trimethylarsine oxide to trimethylarsine by thiols: a mechanistic model for the biological reduction of arsenicals
    • Cullen W.R., McBride B.C., Reglinski J. The reduction of trimethylarsine oxide to trimethylarsine by thiols: a mechanistic model for the biological reduction of arsenicals. J. Inorg. Biochem. 1984, 21:45-60.
    • (1984) J. Inorg. Biochem. , vol.21 , pp. 45-60
    • Cullen, W.R.1    McBride, B.C.2    Reglinski, J.3
  • 11
    • 79955867370 scopus 로고    scopus 로고
    • Polymorphisms in arsenic(+III oxidation state) methyltransferase (AS3MT) predict gene expression of AS3MT as well as arsenic metabolism
    • Engström K., Vahter M., Mlakar S.J., Concha G., Nermell B., Raqib R., Cardozo A., Broberg K. Polymorphisms in arsenic(+III oxidation state) methyltransferase (AS3MT) predict gene expression of AS3MT as well as arsenic metabolism. Environ. Health Perspect. 2011, 119:182-188.
    • (2011) Environ. Health Perspect. , vol.119 , pp. 182-188
    • Engström, K.1    Vahter, M.2    Mlakar, S.J.3    Concha, G.4    Nermell, B.5    Raqib, R.6    Cardozo, A.7    Broberg, K.8
  • 12
    • 57149107969 scopus 로고    scopus 로고
    • Ethnic differences in five intronic polymorphisms associated with arsenic metabolism within human arsenic (+3 oxidation state) methyltransferase (AS3MT) gene
    • Fujihara J., Fujii Y., Agusa T., Kunito T., Yasuda T., Moritani T., Takeshita H. Ethnic differences in five intronic polymorphisms associated with arsenic metabolism within human arsenic (+3 oxidation state) methyltransferase (AS3MT) gene. Toxicol. Appl. Pharmacol. 2009, 234:41-46.
    • (2009) Toxicol. Appl. Pharmacol. , vol.234 , pp. 41-46
    • Fujihara, J.1    Fujii, Y.2    Agusa, T.3    Kunito, T.4    Yasuda, T.5    Moritani, T.6    Takeshita, H.7
  • 13
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
    • Gallogly M.M., Mieyal J.J. Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr. Opin. Pharmacol. 2007, 7:381-391.
    • (2007) Curr. Opin. Pharmacol. , vol.7 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 14
    • 18044372615 scopus 로고    scopus 로고
    • A new metabolic pathway of arsenite: arsenite-glutathione complexes are substrates for human arsenic methyltransferase Cyt19
    • Hayakawa T., Kobayashi Y., Cui X., Hirano S. A new metabolic pathway of arsenite: arsenite-glutathione complexes are substrates for human arsenic methyltransferase Cyt19. Arch. Toxicol. 2005, 79:183-191.
    • (2005) Arch. Toxicol. , vol.79 , pp. 183-191
    • Hayakawa, T.1    Kobayashi, Y.2    Cui, X.3    Hirano, S.4
  • 15
    • 50149111331 scopus 로고    scopus 로고
    • Genetic variations associated with interindividual sensitivity in the response to arsenic exposure
    • Hernández A., Marcos R. Genetic variations associated with interindividual sensitivity in the response to arsenic exposure. Pharmacogenomics 2008, 9:1113-1132.
    • (2008) Pharmacogenomics , vol.9 , pp. 1113-1132
    • Hernández, A.1    Marcos, R.2
  • 18
    • 39749099463 scopus 로고    scopus 로고
    • Speciation of arsenic in biological matrices by automated hydride generation-cryotrapping-atomic absorption spectrometry with multiple microflame quartz tube atomizer (multiatomizer)
    • Hernández-Zavala A., Matoušek T., Drobná Z., Adair B.M., Dědina J., Thomas D.J., Stýblo M. Speciation of arsenic in biological matrices by automated hydride generation-cryotrapping-atomic absorption spectrometry with multiple microflame quartz tube atomizer (multiatomizer). J. Anal. At. Spectrom. 2008, 23:342-351.
    • (2008) J. Anal. At. Spectrom. , vol.23 , pp. 342-351
    • Hernández-Zavala, A.1    Matoušek, T.2    Drobná, Z.3    Adair, B.M.4    Dědina, J.5    Thomas, D.J.6    Stýblo, M.7
  • 19
    • 79960639404 scopus 로고    scopus 로고
    • Significantly increased risk of carotid atherosclerosis with arsenic exposure and polymorphisms in arsenic metabolism genes
    • Hsieh Y.C., Lien L.M., Chung W.T., Hsieh F.I., Hsieh P.F., Wu M.M., Tseng H.P., Chiou H.Y., Chen C.J. Significantly increased risk of carotid atherosclerosis with arsenic exposure and polymorphisms in arsenic metabolism genes. Environ. Res. 2011, 111:804-810.
    • (2011) Environ. Res. , vol.111 , pp. 804-810
    • Hsieh, Y.C.1    Lien, L.M.2    Chung, W.T.3    Hsieh, F.I.4    Hsieh, P.F.5    Wu, M.M.6    Tseng, H.P.7    Chiou, H.Y.8    Chen, C.J.9
  • 20
    • 78149406437 scopus 로고    scopus 로고
    • Arsenic (+3 oxidation state) methyltransferase genotype affects steady-state distribution and clearance of arsenic in arsenate-treated mice
    • Hughes M.F., Edwards B.C., Herbin-Davis K.M., Saunders J., Styblo M., Thomas D.J. Arsenic (+3 oxidation state) methyltransferase genotype affects steady-state distribution and clearance of arsenic in arsenate-treated mice. Toxicol. Appl. Pharmacol. 2010, 249:217-223.
    • (2010) Toxicol. Appl. Pharmacol. , vol.249 , pp. 217-223
    • Hughes, M.F.1    Edwards, B.C.2    Herbin-Davis, K.M.3    Saunders, J.4    Styblo, M.5    Thomas, D.J.6
  • 21
    • 77953395439 scopus 로고    scopus 로고
    • Genetic polymorphism of As3MT and delayed urinary DMA excretion after organic arsenic intake from oyster ingestion
    • Hwang Y.H., Chen Y.H., Su Y.N., Hsu C.C., Chen Y.H., Yuan T.H. Genetic polymorphism of As3MT and delayed urinary DMA excretion after organic arsenic intake from oyster ingestion. J. Environ. Monit. 2010, 12:1247-1254.
    • (2010) J. Environ. Monit. , vol.12 , pp. 1247-1254
    • Hwang, Y.H.1    Chen, Y.H.2    Su, Y.N.3    Hsu, C.C.4    Chen, Y.H.5    Yuan, T.H.6
  • 22
    • 0032705863 scopus 로고    scopus 로고
    • Methylarsenicals and arsinothiols are potent inhibitors of mouse liver thioredoxin reductase
    • Lin S., Cullen W.R., Thomas D.J. Methylarsenicals and arsinothiols are potent inhibitors of mouse liver thioredoxin reductase. Chem. Res. Toxicol. 1999, 12:924-930.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 924-930
    • Lin, S.1    Cullen, W.R.2    Thomas, D.J.3
  • 26
    • 84856737967 scopus 로고    scopus 로고
    • Identification of catalytic residues in the As(III) S-adenosylmethionine methyltransferase
    • Marapakala K., Qin J., Rosen B.P. Identification of catalytic residues in the As(III) S-adenosylmethionine methyltransferase. Biochemistry 2012, 51:944-951.
    • (2012) Biochemistry , vol.51 , pp. 944-951
    • Marapakala, K.1    Qin, J.2    Rosen, B.P.3
  • 27
    • 39249085745 scopus 로고    scopus 로고
    • Oxidation state specific generation of arsines from methylated arsenicals based on L-cysteine treatment in buffered media for speciation analysis by hydride generation-automated cryotrapping-gas chromatography-atomic absorption spectrometry with the multiatomizer
    • Matoušek T., Hernández-Zavala A., Svoboda M., Langerová L., Adair B.M., Drobná Z., Thomas D.J., Stýblo M., Dědina J. Oxidation state specific generation of arsines from methylated arsenicals based on L-cysteine treatment in buffered media for speciation analysis by hydride generation-automated cryotrapping-gas chromatography-atomic absorption spectrometry with the multiatomizer. Spetrochim. Acta Part B 2008, 63:396-406.
    • (2008) Spetrochim. Acta Part B , vol.63 , pp. 396-406
    • Matoušek, T.1    Hernández-Zavala, A.2    Svoboda, M.3    Langerová, L.4    Adair, B.M.5    Drobná, Z.6    Thomas, D.J.7    Stýblo, M.8    Dědina, J.9
  • 28
    • 33747357184 scopus 로고    scopus 로고
    • Arsenate reduction: thiol cascade chemistry with convergent evolution
    • Messens J., Silver S. Arsenate reduction: thiol cascade chemistry with convergent evolution. J. Mol. Biol. 2006, 362:1-17.
    • (2006) J. Mol. Biol. , vol.362 , pp. 1-17
    • Messens, J.1    Silver, S.2
  • 32
    • 62549098120 scopus 로고    scopus 로고
    • Structure-function roles of four cysteine residues in the human arsenic (+3 oxidation state) methyltransferase (hAS3MT) by site-directed mutagenesis
    • Song X., Geng Z., Zhu J., Li C., Hu X., Bian N., Zhang X., Wang Z. Structure-function roles of four cysteine residues in the human arsenic (+3 oxidation state) methyltransferase (hAS3MT) by site-directed mutagenesis. Chem. Biol. Interact. 2009, 179:321-328.
    • (2009) Chem. Biol. Interact. , vol.179 , pp. 321-328
    • Song, X.1    Geng, Z.2    Zhu, J.3    Li, C.4    Hu, X.5    Bian, N.6    Zhang, X.7    Wang, Z.8
  • 33
    • 77957171383 scopus 로고    scopus 로고
    • New insights into the mechanism of arsenite methylation with the recombinant human arsenic (+3) methyltransferase (hAS3MT)
    • Song X., Geng Z., Li X., Hu X., Bian N., Zhang X., Wang Z. New insights into the mechanism of arsenite methylation with the recombinant human arsenic (+3) methyltransferase (hAS3MT). Biochimie 2010, 92:1397-1406.
    • (2010) Biochimie , vol.92 , pp. 1397-1406
    • Song, X.1    Geng, Z.2    Li, X.3    Hu, X.4    Bian, N.5    Zhang, X.6    Wang, Z.7
  • 34
    • 0001101391 scopus 로고
    • Biological mechanisms and toxicological consequences of the methylation of arsenic
    • Springer Verlag, Berlin, M.G. Cherian, R.A. Goyer (Eds.) Toxicology of Metals-Biochemical Aspects
    • Styblo M., Delnomdedieu M., Thomas D.J. Biological mechanisms and toxicological consequences of the methylation of arsenic. Handbook of Experimental Pharmacology 1995, vol. 115:407-433. Springer Verlag, Berlin. M.G. Cherian, R.A. Goyer (Eds.).
    • (1995) Handbook of Experimental Pharmacology , vol.115 , pp. 407-433
    • Styblo, M.1    Delnomdedieu, M.2    Thomas, D.J.3
  • 36
    • 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. 2001, 176:127-144.
    • (2001) Toxicol. Appl. Pharmacol. , vol.176 , pp. 127-144
    • Thomas, D.J.1    Styblo, M.2    Lin, S.3
  • 38
    • 0032604253 scopus 로고    scopus 로고
    • Methylation of inorganic arsenic in different mammalian species and population groups
    • Vahter M. Methylation of inorganic arsenic in different mammalian species and population groups. Sci. Prog. 1999, 82:69-88.
    • (1999) Sci. Prog. , vol.82 , pp. 69-88
    • Vahter, M.1
  • 41
    • 1642360907 scopus 로고    scopus 로고
    • Endogenous reductants support catalytic function of recombinant rat cyt19, an arsenic methyltransferase
    • Waters S.B., Devesa-Perez V., Del Razo L.M., Styblo M., Thomas D.J. Endogenous reductants support catalytic function of recombinant rat cyt19, an arsenic methyltransferase. Chem. Res. Toxicol. 2004, 17:404-409.
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 404-409
    • Waters, S.B.1    Devesa-Perez, V.2    Del Razo, L.M.3    Styblo, M.4    Thomas, D.J.5
  • 42
    • 10844253121 scopus 로고    scopus 로고
    • Glutathione modulates recombinant rat arsenic (+3 oxidation state) methyltransferase-catalyzed formation of trimethylarsine oxide and trimethylarsine
    • Waters S.B., Devesa V., Fricke M.W., Creed J.T., Styblo M., Thomas D.J. Glutathione modulates recombinant rat arsenic (+3 oxidation state) methyltransferase-catalyzed formation of trimethylarsine oxide and trimethylarsine. Chem. Res. Toxicol. 2004, 17:1621-1629.
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 1621-1629
    • Waters, S.B.1    Devesa, V.2    Fricke, M.W.3    Creed, J.T.4    Styblo, M.5    Thomas, D.J.6


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