A new role for glutathione: Protection of vitamin B12 from depletion by xenobiotics

Chemical Research in Toxicology

Volumn 17, Issue 12, 2004, Pages 1562-1567

  Watson, William P ^a   Munter, Tony ^a   Golding, Bernard T ^b  

^a JEALOTT S HILL INTERNATIONAL RESEARCH CENTRE   (United Kingdom)

^b NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

1,3 BUTADIENE; ALKADIENE; CHLOROPRENE; COBALAMIN; CYANOCOBALAMIN; EPOXIDE; GLUTATHIONE; GLUTATHIONYLCOBALAMIN COMPLEX; HYDROXOCOBALAMIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STYRENE; STYRENE OXIDE; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CANCER; CONTROLLED STUDY; CYANOCOBALAMIN DEFICIENCY; DEGENERATIVE DISEASE; LIVER MICROSOME; MALE; NONHUMAN; PERNICIOUS ANEMIA; RAT; REDUCTION; VITAMIN METABOLISM;

ANIMALS; BUTADIENES; CHLOROPRENE; GLUTATHIONE; MALE; MICROSOMES, LIVER; RATS; STYRENE; VITAMIN B 12; VITAMIN B 12 DEFICIENCY; XENOBIOTICS;

ANIMALIA; MAMMALIA;

EID: 10844238998     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx0497898     Document Type: Article

References (44)

1. Chanarin, I. (2000) Historical review: A history of pernicious anemia. Br. J. Haematol. 111, 407-415.
2. 12 Proteins (Kräutler, B., Arigoni, D., and Golding, B. T., Eds.) pp 461-475, Wiley VCH, Weinheim, Germany.
3. Higdon, J. (2003) In An Evidence Based Approach to Vitamins and Minerals. Health Benefits and Intake Recommendations, Chapter 9, Thieme, New York.
4. 12 deficiency and Alzheimer disease. Neurology 58, 1395-1399.
5. Dow, J. L., and Green, T. (2000) Trichloroethylene induced vitamin Bi2 and folate deficiency leads to increased formic acid excretion in the rat. Toxicology 146, 123-136.
6. Green, T., Dow, J., and Foster, J. (2003) Increased formic acid excretion and the development of kidney toxicity in rats following chronic dosing with trichloroethanol, a major metabolite of trichloroethylene. Toxicology 191, 109-119.
7. Vamvakas, S., Brüning, T., Thomasson, B., Lammert, M., Baumüller, A., Bolt, H. M., Dekant, W., Bierner, G., Henschler, D., and Ulm, K. (1998) Renal cell cancer correlated with occupational exposure to trichloroethene. J. Cancer Res. Clin. Oncol. 124, 374-382.
8. Ames, B. N., and Wakimoto, P. (2002) Are vitamin and mineral deficiencies a major cancer risk? Nat. Rev. Cancer 2, 694-704.
9. Fenech, M. F., Dreosti, I. E., and Rinaldi, J. R. (1997) Folate, vitamin B12, homocysteine status and chromosome damage rate in lymphocytes of older men. Carcinogenesis 18, 1329-1336.
10. Fenech, M. (2001) The role of folic acid and vitamin B12 in genomic stability of human cells. Mutat. Res. 475, 57-67.
11. Wald, D. S., Law, M., and Morris, J. K. (2002) Homocysteine and cardiovascular disease: Evidence on causality from meta-analysis. Br. Med. J. 325, 1202-1206.
12. Ames, B. N. (2003) The metabolic tune-up: Metabolic harmony and disease prevention. J. Nutr. 133 (5 Suppl. 1), 1544S-1548S.
13. Ames, B. N. (2001) DNA damage from micronutrient deficiencies is likely to be a major cause of cancer. Mutat. Res. 475, 7-20.
14. Carmel, R. (2000) Current concepts in cobalamin deficiency. Annu. Rev. Med. 51, 357-375.
15. Golding, B. T., and Buckel, W. (1997) In Comprehensive Biological Catalysis (Sinnott, M. L., Ed.) pp 239-259, Academic Press, London.
16. 12, Wiley, New York.
17. Pratt, J. M. (2001) In Handbook on Metalloproteins (Bertini, I., Sigel, A., and Sigel, H., Eds.) pp 603-668, Marcel Dekker, New York.
18. 12: Catalysis by cobalamin-dependent enzymes. Annu. Rev. Biochem. 72, 209-247.
19. Matthews, R. G., Smith, A. E., Zhou, Z. S., Taurog, R. E., Bandarian, V., Evans, J. C., and Ludwig, M. (2003) Cobalamin-dependent and cobalamin-independent methionine synthases: Are there two solutions to the same chemical problem? Helv. Chim. Acta 86, 3939-3954.
20. Schrauzer, G. N., and Deutsch, E. (1969) Reactions of cobalt(I) supernucleophiles. The alkylation of vitamin B12s, cobaloximes(I), and related compounds. J. Am. Chem. Soc. 91, 3341-3350.
21. 1H NMR spectroscopy of diastereoisomeric hydroxy- and dihydroxy-alkylcobalamins. J. Chem. Soc. Chem. Commun. 243-245.
22. 1H NMR spectra and conformational analysis of the alkyl group. J. Organomet. Chem. 437, 227-237.
23. 12) using reversed phase high performance liquid chromatography with electrospray tandem mass spectrometry and ultraviolet diode array detection. Rapid Commun. Mass Spectrom. 15, 2438-2445.
24. Seidegård, J., and Ekström, G. (1997) The role of human glutathione transferases and epoxide hydrolases in the metabolism of xenobiotics. Environ. Health Perspect. 105 (Suppl. 4), 791-799.
25. Haglund, J., Rafiq, A., Ehrenberg, L., Golding, B. T., and Törnqvist, M. (2000) Transalkylation of phosphotriesters using cob(I)alamin: Toward specific determination of DNA-phosphate adducts. Chem. Res. Toxicol. 13, 253-256.
26. Swain, C. G., and Scott, C. B. (1953) Quantitative correlation of relative rates. Comparison of hydroxide ion with other nucleophilic reagents toward alkyl halides, esters, epoxides and acyl halides. J. Am. Chem. Soc. 75, 141-147.
27. Carmel, R. (2003) Mild transcobalamin I (haptocorrin) deficiency and low serum cobalamin concentrations. Clin. Chem. 49, 1367-1374.
28. Cottrell, L., Golding, B. T., Munter, T., and Watson, W. P. (2001) In vitro metabolism of chloroprene: Species differences, epoxide stereochemistry and a de-chlorination pathway. Chem. Res. Toxicol. 14, 1552-1562.
29. Munter, T., Cottrell, L., Golding, B. T., and Watson, W. P. (2003) Detoxication pathways involving glutathione and epoxide hydrolase in the in vitro metabolism of chloroprene. Chem. Res. Toxicol. 16, 1287-1297.
30. 1H NMR structure analysis and kinetic studies with glycerol dehydratase and diol dehydratase. Helv. Chim. Acta 82, 1250-1265.
31. 12r with organic halides. J. Am. Chem. Soc. 102, 1684-1689.
32. Pezacka, E., Green, R., and Jacobsen, D. W. (1990) Glutathionylcobalamin as an intermediate in the formation of cobalamin coenzymes. Biochem. Biophys. Res. Commun. 169, 443-450.
33. Suto, R. K., Brasch, N. E., Anderson, O. P., and Finke, R. G. (2001) Synthesis, characterization, solution stability, and X-ray crystal structure of the thiolatocobalamin γ-glutamylcysteinylcobalamin, a dipeptide analogue of glutathionylcobalamin: Insights into the enhanced Co-S bond stability of the natural product glutathionylcobalamin. Inorg. Chem. 40, 2686-2692.
34. Scheuring, E. M., Sagi, I., and Chance, M. R. (1994) Sulfur-containing cobalamins: X-ray absorption spectroscopic characterization. Biochemistry 33, 6310-6315.
35. Sumner, S. J., and Fennel, T. R. (1994) Review of the metabolic fate of styrene. Crit. Rev. Toxicol. 24, S11-S33.
36. Barnett, R., Hogenkamp, H. P. C., and Abeles, R. H. (1966) Reactions of the carbon-cobalt bond of alkylcobalamins. J. Biol. Chem. 241, 1483-1486.
37. Watanabe, F., Nakano, Y., Maruno, S., Tachikake, N., Tamura, Y., and Kitaoka, S. (1989) NADH-and NADPH-linked aquacobalamin reductases occur in both mitochondrial and microsomal membranes of rat liver. Biochem. Biophys. Res. Commun. 165, 675-679.
38. Watanabe, F., Nakano, Y., Saido, H., Tamura, Y., and Yamanaka, H. (1992) NADPH-cytochrome c (P-450) reductase has the activity of NADPH-linked aquacobalamin reductase in rat liver microsomes. Biochim. Biophys. Acta 1119, 175-177.
39. Golding, B. T., and Maudsley, J. Unpublished data [Maudsley, J. (1991) MSc. Thesis, University of Newcastle upon Tyne, United Kingdom].
40. Watanabe, F., Nakano, Y., Tachikake, N., Kitaoka, S., Tamura, Y., Yamanaka, S., Haga, S., Imai, S., and Saido, H. (1991) Occurrence and subcellular location of NADH- and NADPH-linked aquacobalamin reductases in human liver. Int. J. Biochem. 23, 531-533.
41. Watson, W. P., Munter, T., and Golding, B. T. (2004) Unpublished data.
42. Zheng, D., and Birke R. L. (2001) The reaction of nitric oxide with glutathionylcobalamin. J. Am. Chem. Soc. 124, 9096-9097.
43. World Health Organization (1998) Human Vitamin and Mineral Requirements, Report of a Joint FAO/WHO Expert Consultation, Chapter 5, WHO, Geneva, Switzerland.
44. Xia, L., Cregan, A. G., Berben, L. A., and Brasch, N. E. (2004) Studies on the formation of glutathionylcobalamin: Any free intracellular aquocobalamin is likely to be rapidly and irreversibly converted to glutathionylcobalamin. Inorg. Chem. 43, 6848-6857.