2002, Number 2
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Vet Mex 2002; 33 (2)
Comparative study of the concentration of reduced glutathione and the activity of gamma-glutamyl-transferase and glutathione transferase in liver and kidney of broilers and rats
Quezada TT, Jaramillo JF, Valdivia FA, Reyes SJL, Ortiz MR, Rodríguez VML
Language: English/Spanish
References: 43
Page: 125-135
PDF size: 137.28 Kb.
ABSTRACT
The objective of this study was to compare protein concentration (PC), adenosine 5'-triphosphate (ATP) and reduced glutathion (GSH), as well as the specific enzymatic activities of transferase of glutathion (SEA-TG), and gamma-glutamyl-transferase (SEA-GGT) in liver and kidney homogenates of broilers and rats. Due to the fact that these processes are involved in the detoxification process of the cells, twenty-five four-week-old broilers, and twenty-five 35 day-old rats were divided at random in five groups. Animals were weighed, anesthetized, and perfused using chicken buffer solution, and their liver and kidneys were removed. Samples from both tissues were taken and homogenized in a buffer solution (4°C). Aliquots were made and stored at –25°C until analyzed. Protein concentration (mg/g of tissue), ATP (ng/mg of tissue), and GSH (Mol/mg of tissue) were determined. AEE-TG and AEE-GGT were measured. Data was analyzed by the analysis of variance (ANOVA), and the multiple comparison means was obtained through the Tukey test. ATP and GSH, as well as SEA-GGT-and SEA-TG concentrations were significant among species and tissues (P ‹ 0.01). PC among species in both tissues did not show significant differences (P › 0.05), while that among the tissues of the same species proved to be different (P ‹ 0.01). Results of the comparison of the studied species suggest, in general, discrepancy between species, and the possible difference of response of cellular detoxification mechanisms in presence of xenobiotics.
REFERENCES
McCormick ChC. Symposium: liver metabolism in the chicken (Introduction). Poultry Sci 1990;69:1182.
2. Lin JK, Miller JA, Miller EC. 2,3-dihydro-2(N7-guanyl)-(guanyl-7)-3 hydroxy-aflatoxin B1, a major acid hidrolysis product of aflatoxin B-DNA of ribosomal RNA adducts formed in hepatic microsome-mediated reactions and in the rat liver in vivo. Cancer Lett 1977;24:241-250.
3. Shoental R. Hepatotoxic activity of retrosine, senkirkine and hydroxysenkirkine in newborn rats, and the role of epoxides in carcinogenesis by pyrrolizidine alkaloids and aflatoxins. Nature 1970;221:401-402.
4. Essigmann JM, Croy RG, Bennett RA, Wogan GN. Metabolic activation of aflatoxin B1: patterns of DNA adduct formation, removal, and excretion in relation to carcinogenesis. Drug Metab Rev 1982;13:581-602.
5. Degen GH, Neumann HG. The major metabolite of aflatoxin B1 in the rat is a glutathione conjugate. Chem Biol Interact 1978;22:239-255.
6. Boyland E, Chasseaud LF. The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis. Adv Enzymol 1969;32:173-219.
7. Wirth PJ, Thorgeirsson SS. Glutathione synthesis and degradation in fetal and adult rat liver and Novikoff hepatoma. Cancer Res 1976;38:2861-2865.
8. Meister A, Anderson ME. Glutathione. Ann Rev Biochem 1983;52:711-760.
9. Shan X, Aw TY, Jones DP. Glutathione-dependent protection against oxidative injury. Pharmacol Ther 1990;47:61-71.
Meister A. New aspects of glutathione biochemistry and transport: selective alteration of glutathione metabolism. Fed Proc 1984;43:3031-3042.
Anderson ME, Meister A. Transport and direct utilization of gamma-glutamylcyst(e)ine for glutathione synthesis. Proc Natl Acad Sci (USA) 1983;80:707-711.
Bannai S, Tateishi N. Role of membrane transport in metabolism and function of glutathione in mammals. J Memb Biol 1986;89:1-8.
Mgbodile MUK, Holscher M, Neal RA. A possible protective role for reduced glutathione in aflatoxin B1 toxicity: effect of pretreatment of rats with phenobarbital and 3-methylcholanthrene on aflatoxin toxicity. Toxicol Appl Pharmacol 1975;43:128-142.
Beers KW, Nejad H, Bottje WG. Aflatoxin and glutathione in domestic fowl (Gallus domesticus) I. Glutathione elevation and attenuation by high dietary methionine. Comp Biochem Physiol 1992b;101C:239-244.
Enkvetchakul B, Bottje WG, Anthony N, Moore R, Huff W. Compromised antioxidant status associated with ascites in broilers. Poultry Sci 1993;72:2272-2280.
Enkvetchakul B, Anthony NB, Bottje WG. Liver and blood glutathione in male broiler chickens, turkeys, and quail. Poultry Sci 1995;74:885-889.
Veltmann JR Jr, Wyatt RD, Voight MN, Shamsuddin Z. Influence of dietary sulfur amino acid levels on performance, free amino acids and biochemical parameters in plasma and hepatic glutathione of broiler chicks fed aflatoxin. J Poultry Sci 1983;62:1518-1519.
Emerole GO, Neskovic N, Dixon RL. The detoxification of aflatoxin B1, with glutathione in the rat. Xenobiotica 1979;9:737-743.
Mainigi KD, Campbell TC. Effects of low dietary protein and dietary aflatoxin on hepatic glutathione levels in F-344 rats. Toxicol Appl Pharmacol 1981;59:196-203.
Beers KW, Glahn RP, Bottje WG, Huff WE. Aflatoxin and glutathione in domestic fowl (Gallus domesticus) II. Effects on hepatic blood flow. Comp Biochem Physiol 1992a;101C:463-467.
National Research Council. Nutrient requirements of poultry. 8th ed. Washington (DC): National Academy Press, 1984.
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the folin phenol reagent. J Biol Chem 1951;193:265-275.
Peterson GL. A simplification of the protein assay method of Lowry et al., which is more generally applicable. Anal Biochem 1977;83:346-356.
Adams H. Adenosine 5’-triphosphate determination with phosphoglycerate kinase. In: Bergmeyer HU, editor. Methods of enzymatic analysis. New York: Academic Press, 1963:539-543.
Cohn VH, Lyle J. A fluorometric assay for glutathione. Anal Biochem 1966;14:434-440.
Habig WH, Pabst MJ, Jakoby WB. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J Biol Chem 1974;249:7130-7139.
Glossman H, Neville DM Jr. g-glutamyltransferase in kidney brush border membranes. Feb Lett 1972;19:340-344.
SAS/STAT. Guide for personal computers. 6th ed. Cary (NC): SAS Institute Inc., 1985.
Quezada TT, Rebollar SE, Cuéllar PL, Martínez AA, Valdivia FA. Secuencia de los efectos de la aflatoxina B1 sobre el riñón e hígado de pollos en desarrollo. Memorias de la XVIII Convención Nacional de la ANECA; 5-9 mayo 1993; Cancún (Q. Roo). México (DF): Asociación Nacional de Especialistas en Ciencias Avícolas, A.C., 1993:226-231.
Orlowski M, Meister A. The g-glutamil cycle; a possible transport system for amino acids. Proc Natl Acad Sci (USA) 1970;67:1248-1255.
Strubelt O, Kremer J, Tilse A, Keogh J, Pentz R, Younes M. Comparative studies on the toxicity of mercury, cadmium, and copper toward the isolated perfused rat liver. J Toxicol Environm Health 1996;47:267-283.
Larsson A, Orrenius S, Holmgren A. Functions of glutathione: biochemical, physiological, toxicological, and clinical aspects. New York: Raven Press, 1983.
Sies HK. Glutathione conjugation: its mechanism and biological significance. London (UK): Academic Press, 1988.
Larsen C, Erlich M, Discoll C, Gross WB. Aflatoxin- antioxidant effects on growth of young chicks. J Poultry Sci 1985;64:2287-2291.
Wang SY, Bottje W, Maynard P, Dibner J, Shermer W. Effect of santoquin and oxided fat on liver and intestinal glutathione in broilers. J Poultry Sci 1997;76:961-967.
Beers K, Nejad H, Bottje W. Indomethacin attenuation of celiac blood flow hyperemia following glutathione depletion. Biochem Pharmacol 1990;40:2331-2335.
Tateishi N, Higashi T, Naruse A, Nakashima K, Shiozaki H, Sakamoto Y. Rat liver glutathione: possible role as a reservoir of cysteine. J Nutr 1977;107:51-60.
Chanda S, Mehendale MH. Role of nutrition in the survival after hepatotoxic injury. Toxicology 1996;111:163-178.
Maynard PM, Graupner GW, Bottje WG. Effect of glutathione depletion on tissue and plasma prostacyclin and thromboxane in rats. Biochem Pharmacol 1992;43:1043-1051.
Meijer C, Mulder NH, Hospers GAP, Uges DRA, Decries EGE. The role of glutathione in resistance to cisplatin in a human small cell lung cancer cell line. Br J Cancer 1990;62:72-77.
Quinn BA, Crane TL, Kocal TE, Best SJ, Cameron RG, Tushmore TH et al. Protective activity of different hepatic cytosolic glutathione-S-transferases against DNA-binding metabolites of aflatoxin B1. Toxicol Appl Pharmacol 1990;105:351-363.
Ramsdell HS, Eaton DL. Mouse liver glutathione-S-transferase isoenzyme activity toward aflatoxin B1-8-9-epoxide and benzo(a)pyrene-7,8-dihydrodiol-9,10-epoxide. Toxicol Appl Pharmacol 1990;105:216-225.
Raney KD, Meyer DJ, Ketterer B, Harris TM, Guengerich FP. Glutathione conjugation of aflatoxin B1 exo and endo-epoxides by rat and human glutathione-S-transferases. Chem Res Toxicol 1992;5:470-478.