Influência do zinco sobre o efeito do selênio na atividade da enzima δ-ALA-D de fígado, rim e cérebro de camundongos adultos in vitro

Authors

  • Nilda Vargas Barbosa Departamento de Química, Centro de Ciências Naturais e Exatas - CCNE Universidade Federal de Santa Maria - UFSM, Santa Maria, RS.
  • João Batista T. da Rocha Departamento de Química, Centro de Ciências Naturais e Exatas - CCNE Universidade Federal de Santa Maria - UFSM, Santa Maria, RS.

DOI:

https://doi.org/10.5902/2179460X27224

Abstract

Selenium is an essential dietary trace element and its deficiency can cause some pathologies such as cardiac diseases. However, investigations have evidencied the toxicologic effect of organic and inorganic selenium compounds in the organs and enzymes.
The present work examined the toxic effect of selenium on δ-ALA-D an enzyme involved in the biosynthesis of tetrapyrrol heme. A possible protective role of zinc on inhibitory effect of selenium was also evaluated. The organic selenium compound, (CH3)2C (Seφ) (0CH3) caused a dose dependent inhibition of renal, hepatic and cerebral δ-ALA-D (p< 0.01). Also was evidencied that the selenium and zinc interaction not was able to restore the δ-ALA-D activity inhibited by selenium but increasing the inhibitory effect from the compound on the renal and cerebral enzyme.

Downloads

Download data is not yet available.

References

Barbosa, N.B.V.; Rocha, J.B.T.; Zeni, G.; Emanuelli, T.; Beque, M.C. & Braga, A L. (1998). Effect of organic forms selenium on daminolevulinate dehydratase from liver, kidney and brain of adult rats. Toxicology Applied Pharmacology. 49, 243-253.

Beber, F A; Wolsmeister, J; Brigo, M.J.K; Silva, M.C.J; Pereira, C.N. and Rocha, J.B.T. (1998). Ascorbic acid inhibition of hepatic deltaaminolevulinate dehydratase is mediated by na oxyding system present in liver supernatants. Int. J. Vitam. Nutr. Res. (In press).

Behne D.; Kyriakopoulos, A (1990). Indentification of type I iodothyronine 5' -deiodinase as a selenoenzyme. Biochem. Biophys. Res. Commun. 173, 1143-1149.

Bechara E.J.H; Medeiros, M.H.G.; Monteiro, H.P.; Lima, H.; Pereira, M.; Demasi, B.; Costa, M.; Abdall, C. A; Onuki, J.; Wendel, C.M.A and Masci, P.D. (1993). A free radical hypothesis of lead poisoning and inborn porphyrias associated with 5-aminolevulinic acid overload. Química Nova. 16, 385-392.

Bevan, D.R.; Bodlaender, P. and Shemin. D. (1980)Mechanism of porphobilinogen synthase. Requirement of Zn2+ for enzyme activity. Journal of Biological Chemistry. 255, 2030-2035.

Cotgreave, I.A.; Moudeus, P.; Brattsand, R.; Hallberg, A ; Andersson, C.M.; Engman, L. (192). a (phenylselenyl) acetophenone derivatives with glutathione peroxidase: Like activity. A comparisom with Ebselen. Biochem. Pharmacol. 4443, 793-802.

Dent, A J.; Beyersmann, D.; Block, C. and Hasnain, S.S. (1990). Two different zinc sites in bovine 5-aminolevulinate dehydratase distinguished by exyend X-ray absorption fine structure. Biochemistry. 29, 7822-7828.

Emanuelli, T.; Rocha, J.B.T.; Pereira, M. E.; Porciúncula, L.O and Souza, D. (1996). Effects of mercuric chloride intoxication and 2,3-dimercaptopropanol (BAL) treatment on delta-minolevulinate dehydratase from brain, kidney and liver of adult mice. Pharmacology & Toxicology. 79, 136-143.

Emanuelli, T.; Rocha, J.B.T.; Pereira, M.E.; Nascimento, P.C.; Souza, D.O G & Beber, F.A (1998). Delta-aminolevulinate dehydratase inhibition by 2,3- dimercaptopropanol is mediated by chelation of zinc from a site involved in maintaining cysteynil residues in reduced state. Pharmacology and Toxicology. 83, 95-103.

Farina, M.; Folmer, V.; Bolzan, R.; Andrade, L.;Zeni, G.; Braga, A and Rocha, J.B.T. (2001). Selenoxides inhibit d-aminolevulinic acid dehydratase. Toxicology Letters. 119, 27-37.

Flohe, L.; Gunzler, W. A; Schock, H.H. (1973). Glutathione peroxidase: A selenium enzyme. FEBS Lett. 32, 132-134.

Ganther, H.E. (1971). Reduction of the selenotrisulfide derivative of glutathione to a persulfide analog by glutathione reductase. Biochemistry. 10, 4089-4098.

Ganther, H.E. (1968). Selenotrisulfides. Formation by reaction of thiols with selenious acid. Biochemistry. 7, 2898-2905.

Ganther, H.E. (1966). Enzimic synthesis of dimethyl selenide from sodium selenite in mouse extract. Biochemistry. 10, 4089-4098.

Ganther, H.E.; Corcoran, C. (1969). Selenotrisulfide. 11. Cross-linking of reduced pancreatic ribonuclease with selenium. Biochemistry. 8, 2557-2563.

Gibson, K.D.; Neuberger, A; Scott, J.J. (1955). The purification and properties of delta-aminolevulinic acid dehydratase. Biochem. J. 61, 618-629.

Goering, P.L. (1993). Lead protein interactions as a basis for lead toxicity. Neurotoxicology. 14, 45-60.

Goering, P.L. and Fowler, B.A (1984). Regulation of lead inhibition of d-aminolevulinic acid dehydratase by a low molecular weigth, high affinity renal lead-binding protein. J. Pharmacol. Exp. Therap. 14,45-60.

Goering, P.L.; Fowler, B.A (1986). Mechanism of renal lead-binding protein reversal of d-aminolevulinic acid dehydratase inhibition by lead. Pharmacol. Exp. Therap. 237, 220-225.

Goering, P.L.; Mistry, P. and Fowler, B.A (1986). A low molecular weight lead-binding protein in brain attenuates lead inhibition of delta-aminolevulinic acid dehydratase. Comparison with a renal lead-binding protein. J. Phamacol. Exp. Therap. 237, 220-225.

Greger, J.L. and Lane, H.W. (1987). The toxicology of dietary tin, aluminium and selenium. Nutritional Toxicology. (J.N.Hathcock, ed). Vo1.2. Academic. Press, San Diego, C.A.

Jacques-Silva M.C.; Nogueira, C.W.; Broch, L.C.; Flores, E.E.M & Rocha, J.B.T. (2000). Diphenyl diselenide and ascorbic acidchange deposition of selenium and ascorbic acid in liver and brain of mices. Pharmacology & Toxicology. In Press.

Jaffe, E.K. (1995). Porphobilinogen synthase, the first source of heme's asymmetry. J. Bioenergetics and Biomembranes. 27, no 2.

Linder, M.C. (1990). Nutrition and metabolism of the trace elements. 7,216-276.

Maciel, E.N.; Bolzan, R.; Braga, A L and Rocha, J.B.T. (2000). Diphenyl diselenide and diphenyl ditelluride differentially affect daminolevulinate dehydratase from liver, kidney and brain of mice. Journal of Biochemical and Molecular Toxicology, 14,1-10.

Nelson, H.M.; Ughes, M. A; Meredith, P.A (1981). Zinc, cooper and delta-aminolevulinic acid dehydratase in vitro. Toxicology, 21,261-266.

Painter, E.P. (1941). The chemistry and toxicity of selenium compounds which special reference to the selenium problem. Chem. Rev. 28, 179-213.

Rocha, J.B.T.; Freitas, A J.; Marquez., M.B.; Pereira, M. E.; Emanuelli, T & Souza, D.O (1993). 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. Brazilian Journal of Medical and Biological Research. 26, 1077-1083.

Rocha, J.B.T.; Pereira, M.E.; Emanuelli, T.; Christofari, R.S. & Souza, D. O (1995). Effeccts of mercury chloride and lead acetate treatment during the secound stage of rapid postnatal brain growth on ALA-D activity in brain, liver, kidney and blood of suckling rats. Toxicology. 100, 27-37.

Rodrigues, A L.; Bellinaso, M. L. and Dick, T (1989). Effect of some metais ions on blood and liver delta-aminolevulinate dehydratase of Pimelodus malacatus (pisces, pimelodidae). Comp. Biochem. Physiol. 94B, 65-69.

Rodrigues, A L.; Rocha, J.B.T; Pereira, M.E. & Souza, D.O (1996). Delta-aminolevulinic acid dehydratase activity in weanling and adult rats exposed to lead acetate. BulI. Environ. Contam. Toxicol. 57,47-53.

Rotruck, J.T.; Pope, A L.; Ganther, H.E.; Swanson, A B.; Hafeman, D.G.; Hoestra, W.G. (1973). Selenium: Biochemical role as a component of glutathione peroxidase. Science. 179, 558-560.

Sassa, S. (1982). Delta-aminolevulinic acid dehydratase assay. Enzyme. 28,133-145.

Seko,Y.; Satio, Y.; Kitahara, J.; Imura, N. (1989). Active oxygen generation by the reaction of selenite with reduced glutathione in vitro. In: Wendel, A (ed). Selenium in biology and medicine. Springer, Berlin Heidelberg. New York. pp:70-73.

Spallhoz, J.E. (1994). On the nature of selenium toxicity and carcinostatic activity. Free Radical Biology & Medicine. 17,45-64.

Tsen, C.C., Tappel, A L. (1958). Catalytic oxidation of glutathione and other sulphydril compounds biselenite. J. Bio. Chem. 233, 1230-1232.

Tsukamoto, I.; Youshinaga, T; and Sano, S. (1979). The role of zinc with special reference to the essential thiol groups in deltaaminolevulinic acid dehydratase of bovine liver. Biochimica et Biophysica Acta. 570, 167-178.

Ursini, F.; Maorino, M.; Valente, M.; Ferri, K.; Gregolin, C. (1982). Purification of pig liver of a protein which protects lipossomes and biomembranes from peroxidadtive degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxidase. Biochem. Biophys. Acta. 710,197-211.

Ursini, F.; Maiorino, M and Grregolin, Carlo. (1985). The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochimica. Et. Biophysica. Acta. 839, 62-70.

Ursini, F and Bindoli, A (1987). The role of selenium peroxidases in the protection against oxidative damage of membranes. Chemistry and Physics of Lipids. 44, 255-276.

Published

2002-12-09

How to Cite

Barbosa, N. V., & Rocha, J. B. T. da. (2002). Influência do zinco sobre o efeito do selênio na atividade da enzima δ-ALA-D de fígado, rim e cérebro de camundongos adultos in vitro. Ciência E Natura, 24(24), 49–62. https://doi.org/10.5902/2179460X27224