Mechanisms of the inhibitory effects of selenium and mercury on the activity of δ-aminolevulinate dehydratase from mouse liver, kidney and brain

Toxicology Letters

Volumn 139, Issue 1, 2003, Pages 55-66

  Farina, M ^a,b   Brandao R ^a   Lara, F S ^a   Soares, F A A ^b   Souza, D O ^b   Rocha, J B T ^c  

^a Depto de Engenharia de Alimentos   (Brazil)

^b FEDERAL UNIVERSITY OF RIO GRANDE DO SUL   (Brazil)

^c FEDERAL UNIVERSITY OF SANTA MARIA   (Brazil)

Author keywords

Selenium, mercury, sulfhydryl groups; Aminolevulinate dehydratase

Indexed keywords

ALBUMIN; BRAIN ENZYME; DITHIOL DERIVATIVE; DITHIOTHREITOL; GLUTATHIONE DERIVATIVE; KIDNEY ENZYME; LIVER ENZYME; MERCURIC CHLORIDE; PORPHOBILINOGEN SYNTHASE; PROTEIN; SODIUM SELENITE; THIOL GROUP;

ACUTE TOXICITY; ANIMAL TISSUE; ARTICLE; BRAIN; COMPLEX FORMATION; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME INHIBITION; KIDNEY; LIVER; MALE; MOUSE; NONHUMAN; OXIDATION; PRIORITY JOURNAL; RAT; SUPERNATANT;

EID: 84984555354     PISSN: 03784274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-4274(02)00454-X     Document Type: Article

References (47)

1. Barbosa N.B.V., Rocha J.B.T., Zeni G., Emanuelli T., Beque M.C., Braga A.L. Effect of organic forms of selenium on δ-aminolevulinate dehydratase from liver, kidney and brain of adult rats. Toxicol. Appl. Pharmacol. 149:1998;243-253.
2. Barnard G.F., Itoh R., Hohberger L.H., Shemin D. Mechanism of porphobilinogen synthase - possible role of essential thiol groups. J. Biol. Chem. 252:1977;8965-8974.
3. Bechara E.H.J., Medeiros M.H.G., Monteiro H.P., Hermes-Lima M., Pereira B., Demasi M., Costa C.A., Adballa D.S.P., Onuki J., Wendel C.M.A., Masci P.D. A free radical hypothesis of lead poisoning and inborn porphyrias associated with 5-aminolevulinic acid overload. Quím. Nova. 16:1993;385-392.
4. Bjornstedt M., Kumar S., Bjorkhem L., Spyrou G., Holmgren A. Selenium and the thioerdoxin and glutaredoxin systems. Biomed. Environ. Sci. 10:1997;271-279.
5. Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
6. Carter D.C., Ho J.X. Structure of serum albumin. Adv. Protein Chem. 45:1994;153-203.
7. Clarkson T.W. Toxicology of mercury. Crit. Rev. Clin. Lab. Sci. 34:1997;369-403.
8. Cuvin-Aralar M.L.A., Furness R.W. Mercury and selenium interaction: a review. Ecotoxicol. Environ. Saf. 21:1991;348-364.
9. 0) by copper, zinc, and aurintricarboxylic acid (ATA). Biochem. Pharmacol. 51:1996;1015-1020.
10. Dixon M., Webb E.C. Enzymes. second ed:1964; 950 Longmans, London and Colchester.
11. El-Demerdash F.M. Effects of selenium and mercury on the enzymatic activities and lipid peroxidation in brain, liver, and blood of rats. J. Environ. Sci. Health. 36:2001;489-499.
12. Ellman G.L. Tissue sulphydryl groups. Arch. Biochem. Biophys. 82:1959;70-77.
13. Emanuelli T., Rocha J.B.T., Pereira M.E., Porciuncula L.O., Morsch V.M., Martins A.F., Souza D.O.G. Effects of mercuric chloride intoxication and 2,3-dimercaptopropanol (BAL) treatment on delta-aminolevulinate dehydratase from brain, kidney and liver of adult mice. Pharmacol. Toxicol. 79:1996;138-143.
14. Emanuelli T., Rocha J.B.T., Pereira M.E., Nascimento P.C., Souza D.O.G., Beber F.A. Aminolevulinate dehydratase inhibition by 2,3-dimercaptopropanol is mediated by chelation of zinc from a site involved in maintaining cysteinyl residues in a reduced state. Pharmacol. Toxicol. 83:1998;95-103.
15. Farina M., Folmer V., Bolzan R.C., Andrade L.H., Zeni G., Braga A.L., Rocha J.B.T. Selenoxides inhibit δ-aminolevulinic acid dehydratase. Toxicol. Lett. 119:2001;27-37.
16. Farina M., Barbosa N.B., Nogueira C.W., Folmer V., Zeni G., Andrade L.H., Braga A.L., Rocha J.B.T. Reaction of diphenyl diselenide with hydrogen peroxide and inhibition of delta-aminolevulinate dehydratase from rat liver and cucumber leaves. Braz. J. Med. Biol. Res. 35:2002;623-631.
17. Farina, M., Brandão, R., deLara, F.S., Pagliosa, L.B., Soares, F.A., Souza, D.O., Rocha, J.B.T., 2003. Profile of nonprotein thiols, lipid peroxidation and δ-aminolevulinate dehydratase activity in mouse kidney and liver in response to acute exposure to mercuric chloride and sodium selenite. Toxicology 184, 179-187.
18. Folmer V., Soares J.C., Rocha J.B.T. Oxidative stress in mice is dependent on the free glucose content of the diet. Int. J. Biochem. Cell. Biol. 34:2002;1279-1285.
19. Ganther H.E. Selenotrisulfides. Formation by reaction of thiols with selenious acid. Biochemistry. 7:1968;2898-2905.
20. Ganther H.E. Reduction of the selenotrisulfide derivative of glutathione to a persulfide analog by glutathione reductase. Biochemistry. 10:1971;4089-4098.
21. Gasiewicz T.A., Smith J.C. The metabolism of selenite by intact rat erythrocytes in vitro. Chem. Biol. Interact. 21:1978;299-313.
22. Goering P.L. Lead protein interactions as a basis for lead toxicity. Neurotoxicology. 14:1993;45-60.
23. Jaffe E.K. Porphobilinogen synthase, the first source of heme's asymmetry. J. Bioenerg. Biomembr. 27:1995;169-179.
24. Jacques-Silva M.C., Nogueira C.W., Broch L.C., Flores E.M., Rocha J.B.T. Diphenyl diselenide and ascorbic acid changes deposition of selenium and ascorbic acid in liver and brain of mice. Pharmacol. Toxicol. 88:2001;119-125.
25. Komiya K., Koike I., Kawaguchi S., Sakurai H. Studies on protective effect of mercurial toxicity by selenium. I. Relationship between protective effects of various selenium compounds on the toxicity of mercuric chloride and distributions of mercury and selenium in rats tissues. Eisei. Kagaku. 23:1977;235-243.
26. Maciel E.N., Bolzan R.C., Braga A.L., Rocha J.B.T. Diphenyl diselenide and diphenyl ditelluride differentially affect delta-aminolevulinate dehydratase from liver, kidney, and brain of mice. J. Biochem. Mol. Toxicol. 14:2000;310-319.
27. Magos L., Webb M. The interaction of selenium with cadmium and mercury. CRC Crit. Rev. Toxicol. 8:1980;1-42.
28. Markham G.D., Myers C.M., Harris K.A., Volin J.R.M., Jaffe E.K. Spatial proximity and sequence localization of the reactive sulphydryls of porphobilinogen synthase. Protein Sci. 2:1993;71-79.
29. Neal R., Yang P., Fiechtl J., Yildiz D., Gurer H., Ercal N. Pro-oxidant effects of delta-aminolevulinic acid (delta-ALA) on Chinese hamster ovary (CHO) cells. Toxicol. Lett. 91:1997;169-178.
30. Nogueira, C.W., Soares, F.A., Nascimento, P.C., Muller, D., Rocha, J.B.T., 2003. 2,3-Dimercaptopropane-1-sulfonic acid and meso-2,3-dimercaptosuccinic acid increase mercury- and cadmium-induced inhibition of D-aminolevulinate dehydratase. Toxicology, 184, 85-95.
31. Parizek J., Ostadalova I. The protective effect of small amounts of selenite in sublimate intoxication. Experientia. 23:1967;142-143.
32. Princ F.G., Juknat A.A., Amitrano A.A., Batlle A. Effect of reactive oxygen species promoted by delta-aminolevulinic acid on porphyrin biosynthesis and glucose uptake in rat cerebellum. Gen. Pharmacol. 31:1998;143-148.
33. Rhead W.J., Scharauzer G.N. The selenium catalyzed reduction of methylene blue by thiols. Bioinorg. Chem. 3:1974;225-242.
34. Rocha J.B.T., Freitas A.J., Marquez M.B., Pereira M.E., Emanuelli T., Souza D.O. Effects of methylmercury exposure during the second stage of rapid postnatal brain growth on delta-aminolevulinate dehydratase (E.C. 4.2.1.24) of suckling rats. Braz. J. Med. Biol. Res. 26:1993;1077-1083.
35. Rocha J.B.T., Pereira M.E., Emanuelli T., Christofari R.S., Souza D.O. Effects of mercury chloride and lead acetate treatment during the second stage of rapid postnatal brain growth on ALA-D activity in brain, liver, kidney and blood of suckling rats. Toxicology. 100:1995;27-37.
36. Rocha J.B.T., Rocha L.K., Emanuelli T., Pereira M.E. Effects of mercury chloride and lead acetate treatment during the second stage of rapid postnatal brain growth on the behavioral response to chlorpromazine and on δ-ALA-D activity in weaning rats. Toxicol. Lett. 125:2001;143-150.
37. Rodrigues A.L.S., Belinasso M.L., Dick T. Effect of some metal ions on blood and liver delta-aminolevulinate dehydratase of Pimelodus malacatus (pisces, Pimelodidae). Comp. Biochem. Physiol. 94B:1989;65-69.
38. Sasakura C., Suzuki K.T. Biological interaction between transition metals (Ag, Cd and Hg), selenide/sulfide and selenoprotein P. J. Inorg. Biochem. 71:1998;159-162.
39. Sassa S. Delta-aminolevulinic acid dehydratase assay. Enzyme. 28:1982;133-145.
40. Seko Y., Saito Y., Kitahara J., Imura N. Active oxygen generation by the reaction of selenite with reduced glutathione in vitro. Wendel A. Selenium in Biology and Medicine. 1989;70-73 Springer, Berlin.
41. Spallholz J.E. Free radical generation by selenium compounds and their prooxidant toxicity. Biomed. Environ. Sci. 10:1997;260-270.
42. Strycks W., Kolthoff I.M. Reactions between mercuric mercury and cysteine and glutathione. Apparent dissociation constants, heats and entropies of formation of various forms of mercuric mercapto-cysteine and -glutathione. J. Am. Chem. Soc. 20:1953;5673-5681.
43. Sugiura Y., Tamai Y., Takaka H. Selenium protection against mercury toxicity: high binding affinity of methylmercury by selenium-containing ligands in comparison with sulfur-containing ligands. Bioinorg. Chem. 9:1978;167-180.
44. Tomokuni K. The in vitro effect of metal ions on the activity of erythrocyte delta-aminolevulinic acid dehydratase, Sangyo Igaku. Jpn. J. Ind. Health. 21:1979;240-245.
45. Tsen C.C., Tappel A.L. Catalytic oxidation of glutathione and other sulfhydryl compounds by selenite. J. Bio Chem. 233:1958;1230-1232.
46. Yoneda S., Suzuki K.T. Detoxification of mercury by selenium by binding of equimolar Hg-Se complex to a specific plasma protein. Toxicol. Appl. Pharmacol. 143:1997;274-280.
47. Yusof M., Yildiz D., Ercal N. N-acetyl-L-cysteine protects against delta-aminolevulinic acid-induced 8-hydroxydeoxyguanosine formation. Toxicol. Lett. 106:1999;41-47.