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Comparative Effects of Various Forms of Selenium on Thioredoxin Reductase Activity in Broiler Chickens
Abstract
An experiment was conducted to measure thioredoxin reductase (TrxR) and glutathione peroxidase (GSH-Px) enzymatic activity in organs and TrxR activity in liver subcellular fractions in young broiler chickens. Broilers were fed either a (1) Control basal diet (no supplemental selenium but with a background level of 0.095 mg/kg) or diets providing supplemental selenium at 0.3 mg/kg as either (2) sodium selenite (SE; inorganic selenium), (3) Sel-Plex® (SY; organic selenium yeast), or (4) a combination (SS) of 0.15 mg/kg of both selenium forms. GSH-Px (measured in liver only) and TrxR activities were elevated by selenium, regardless of dietary form, in each organ examined. The TrxR activities in subcellular fractions were greatest in the mitochondrial lysate, nuclear pellet and post-mitochondrial supernatant, respectively and the lowest activity was associated with the mitochondrial pellet. Aurothioglucose (ATG; 0.1 μM/g BW) inhibited hepatic cell GSH-Px activity by more than 30% and TrxR activity by more than 80%, but glutathione reductase was not affected. The TrxR enzyme in the chicken might be different from the mammalian enzyme.
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Chickens, selenium, thioredoxin reductaseArticle Metrics
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Copyright (c) 2015 Asian Network for Scientific Information
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Gowdy, K., Edens , F., & Mahmoud, K. (2015). Comparative Effects of Various Forms of Selenium on Thioredoxin Reductase Activity in Broiler Chickens. International Journal of Poultry Science, 14(7), 376–382. https://doi.org/10.3923/ijps.2015.376.382
References
1.
Allan, C.B., G.M. Lacourciere and T.C. Stadtman, 1999. Responsiveness of selenoproteins to dietary selenium. Annu. Rev. Nutr., 19: 1-16.
2.
Barnes, K.M., J.K. Evenson, A.M. Raines and R.A. Sunde, 2009. Transcript analysis of the selenoproteome indicates that dietary selenium requirements of rats based on selenium-regulated selenoprotein mRNA levels are uniformly less than those based on glutathione peroxidase activity. J. Nutr., 139: 199-206.
3.
Berggren, M., A. Gallegos, J. Gasdaska and G. Powis, 1997. Cellular thioredoxin reductase activity is regulated by selenium. Anticancer Res., 17: 3377-3380.
4.
Berggren, M.M., J.F. Mangin, J.R. Gasdaska and G. Powis, 1999. Effect of selenium on rat thioredoxin reductase activity: Increase by supranutritional selenium and decrease by selenium deficiency. Biochem. Pharmacol., 57: 187-193.
5.
Burgos, S., F. Edens, J. Read-Snyder, A. Cantor and S.A. Burgos, 2006. Selenium sources affect protein concentration, thioredoxin reductase activity and selected production parameters in reovirus infected broiler chickens. Int. J. Poult. Sci., 5: 822-829.
6.
Chae, H.Z., S.J. Chung and S.G. Rhee, 1994. Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem., 269: 27670-27678.
7.
Chaudiere, J. and A.L. Tappel, 1984. Interaction of gold(I) with the active site of selenium-glutathione peroxidase. J. Inorg. Biochem., 20: 313-325.
8.
Chen, C., J. Zhao, P. Zhang and Z. Chai, 2002. Speciation and subcellular location of Se-containing proteins in human liver studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and hydride generation-atomic fluorescence spectrometric detection. Anal. Bioanal. Chem., 372: 426-430.
9.
Edens, F.W., 2002. Practical Applications for Selenomethionine: Broiler Breeder Reproduction. In: Biotechnology in the Feed Industry, Lyons, T.P. and K.A. Jacques (Eds.). Nottingham University Press, Nottingham, UK., pp: 29-42.
10.
Ejima, K., H. Nanri, N. Toki, M. Kashimura and M. Ikeda, 1999. Localization of thioredoxin reductase and thioredoxin in normal human placenta and their protective effect against oxidative stress. Placenta, 20: 95-101.
11.
Fischer, J., A. Bosse, E. Most, A. Mueller and J. Pallauf, 2008. Selenium requirement of growing male Turkeys. Br. Poult. Sci., 49: 583-591.
12.
Gallegos, A., M. Berggren, J.R. Gasdaska and G. Powis, 1997. Mechanisms of the regulation of thioredoxin reductase activity in cancer cells by the chemopreventive agent selenium. Cancer Res., 57: 4965-4970.
13.
Ganther, H.E., 1999. Selenium metabolism, selenoproteins and mechanisms of cancer prevention: Complexities with thioredoxin reductase. Carcinogenesis., 20: 1657-1666.
14.
Gladyshev, V.N., K.T. Jeang and T.C. Stadtman, 1996. Selenocysteine, identified as the penultimate c-terminal residue in human t-cell thioredoxin reductase, corresponds to tga in the human placental gene. Proc. Nat. Acad. Sci., 93: 6146-6151.
15.
Gladyshev, V.N., K.T. Jeang, J.C. Wootton and D.L. Hatfield, 1998. A new human selenium-containing protein purification, characterization and cDNA sequence. J. Biol. Chem., 273: 8910-8915.
16.
Gowdy, K.M., 2004. Selenium supplementation and antioxidant protection in broiler chickens. M.Sc. Thesis, The Graduate School, North Carolina State University, Raleigh, NC., USA.
17.
Gromer, S., L. Johansson, H. Bauer, L.D. Arscott and S. Rauch et al., 2003. Active sites of thioredoxin reductases: Why selenoproteins? Proc. Nat. Acad. Sci., 100: 12618-12623.
18.
Hill, K.E., G.W. McCollum, M.E. Boeglin and R.F. Burk, 1997. Thioredoxin reductase activity is decreased by selenium deficiency. Biochem. Biophys. Res. Commun., 234: 293-295.
19.
Hu, M.L., C.J. Dillard and A.L. Tappel, 1988. Aurothioglucose effect on sulfhydryls and glutathione-metabolizing enzymes: In vivo inhibition of selenium-dependent glutathione peroxidase. Res. Commun. Chem. Pathol. Pharmacol., 59: 147-160.
20.
Humann-Ziehank, E., K. Renko, A.S. Mueller, P. Roehrig, J. Wolfsen and M. Ganter, 2013. Comparing functional metabolic effects of marginal and sufficient selenium supply in sheep. J. Trace Elem. Med. Biol., 27: 380-390.
21.
Kim, T.S. and G.F. Combs, 1993. Effects of aurothioglucose and dietary Se on glutathione S-Transferase activities and glutathione concentrations in chick tissues. Biol. Trace Elem. Res., 37: 165-177.
22.
Kohrle, J., R. Brigelius-Flohe, A. Bock, R. Gartner, O. Meyer and L. Flohe, 2000. Selenium in biology: Facts and medical perspectives. Biol. Chem., 381: 849-864.
23.
Karunasinghe, N., L.R. Ferguson, J. Tuckey and J. Masters, 2006. Hemolysate thioredoxin reductase and glutathione peroxidase activities correlate with serum selenium in a group of New Zealand men at high prostate cancer risk. J. Nutr., 136: 2232-2235.
24.
Karunasinghe, N., D.Y. Han, S. Zhu, H. Duan and Y.J. Ko et al., 2013. Effects of supplementation with selenium, as selenized yeast, in a healthy male population from New Zealand. Nutr. Cancer, 65: 355-366.
25.
Levander, O.A., D.P. Deloach, V.C. Morris and P.B. Moser, 1983. Platelet glutathione peroxidase activity as an index of selenium status in rats. J. Nutr., 113: 55-63.
26.
Liu, S.Y. and T.C. Stadtman, 1997. Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells. Proc. Nat. Acad. Sci., 94: 6138-6141.
27.
Luthman, M. and A. Holmgren, 1982. Rat liver thioredoxin and thioredoxin reductase: Purification and characterization. Biochemistry, 21: 6628-6633.
28.
Mahmoud, K.Z. and F.W. Edens, 2003. Influence of selenium sources on age-related and mild heat stress-related changes of blood and liver glutathione redox cycle in broiler chickens (Gallus domesticus). Comp. Biochem. Physiol. Part B: Biochem. Mol. Biol., 136: 921-934.
29.
Marchionatti, A.M., A.V. Perez, G.E.D. de Barboza, B.M. Pereira and N.G.T. de Talamoni, 2008. Mitochondrial dysfunction is responsible for the intestinal calcium absorption inhibition induced by menadione. Biochimica et Biophysica Acta (BBA)-General Subjects, 1780: 101-107.
30.
Mercurio, S.D. and G.F. Jr. Combs, 1985. Drug-induced changes in selenium-dependent glutathione peroxidase activity in the chick. J. Nutr., 115: 1459-1470.
31.
Mercurio, S.D. and G.F. Jr. Combs, 1986. Selenium-dependent glutathione peroxidase inhibitors increase toxicity of prooxidant compounds in chicks. J. Nutr., 116: 1726-1734.
32.
Mustacich, D. and G. Powis, 2000. Thioredoxin reductase. Biochem. J., 346: 1-8.
33.
Oberley, T.D., E. Verwiebe, W. Zhong, S.W. Kang and S.G. Rhee, 2001. Localization of the thioredoxin system in normal rat kidney. Free Radic. Biol. Med., 30: 412-424.
34.
Oxis International Inc., 2009. Bioxytech GR-340TM technical manual. Revision 0397, Part No. 7598, Foster City, CA.
35.
Powis, G. and W.R. Montfort, 2001. Properties and biological activities of thioredoxins. Ann. Rev. Biophys. Biomol. Struct., 30: 421-455.
36.
Rigobello, M.P., M.T. Callegaro, E. Barzon, M. Benetti and A. Bindoli, 1998. Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability. Free Radic. Biol. Med., 24: 370-376.
37.
Rotruck, J.T., A.L. Pope, H.E. Ganther, A.B. Swanson, D.G. Hafeman and W.G. Hoekstra, 1973. Selenium: Biochemical role as a component of glutathione peroxidase. Science, 179: 588-590.
38.
Rozell, B., H.A. Hansson, M. Luthman and A. Holmgren, 1985. Immunohistochemical localization of thioredoxin and thioredoxin reductase in adult rats. Eur. J. Cell Biol., 38: 79-86.
39.
Rozell, B., A. Holmgren and H.A. Hansson, 1988. Ultrastructural demonstration of thioredoxin and thioredoxin reductase in rat hepatocytes. Eur. J. Cell Biol., 46: 470-477.
40.
SAS Institute, 2004. Statistical Analysis System, Version 9.3. SAS Institute Inc., Cary, NC., USA.
41.
Smith, A.D., C.A. Guidry, V.C. Morris and O.A. Levander, 1999. Aurothioglucose inhibits murine thioredoxin reductase activity in vivo. J. Nutr., 129: 194-198.
42.
Smith, A.D., V.C. Morris and O.A. Levander, 2001. Rapid determination of glutathione peroxidase and thioredoxin reductase activities using a 96-well microplate format: Comparison to standard cuvette-based assays. Int. J. Vitamin Nutr. Res., 71: 87-92.
43.
Soderberg, A., B. Sahaf and A. Rosen, 2000. Thioredoxin reductase, a redox-active selenoprotein, is secreted by normal and neoplastic cells: Presence in human plasma. Cancer Res., 60: 2281-2289.
44.
St. Clair, C. and C. Chow, 1996. Glutathione Peroxidase Activity and Steady State Level of mRNA. In: Free Radicals: A Practical Approach, Punchard, N. and F. Kelly (Eds.). Oxford University Press, Oxford, UK., pp: 227-240.
45.
Sunde, R.A. and K.B. Hadley, 2010. Phospholipid hydroperoxide glutathione peroxidase (Gpx4) is highly regulated in male turkey poults and can be used to determine dietary selenium requirements. Exp. Biol. Med., 235: 23-31.
46.
Upton, J.R., F.W. Edens and P.R. Ferket, 2009. The effects of dietary oxidized fat and selenium source on performance, glutathione peroxidase and glutathione reductase activity in broiler chickens. J. Applied Poult. Res., 18: 193-202.
