Skip to main content Accessibility help

Glutathione peroxidases in poultry biology: Part 1. Classification and mechanisms of action

  • P.F. SURAI (a1) (a2) (a3) (a4) (a5), I.I. KOCHISH (a2) and V.I. FISININ (a6)


Glutathione peroxidase (GSH-Px) was described as a selenoprotein in 1973 and, since then, a great body of information has been accumulated to validate its important role in the antioxidant defence network in all animals, including poultry. The GSH-Px family includes at least eight members, and four of them (GSH-Px1, GSH-Px2, GSH-Px3 and GSH-Px4) are shown to be selenoproteins in animals. They are characterised by species- and tissue-specificity in their expression and activity. An optimal Se status in tissues/body is key for maximum expression of GSH-Px and therefore, in avian research GSH-Px activity is widely used as a biomarker for determining Se status and requirements. On the other hand, GSH-Px is an inducible enzyme and its activity depends on the level of stress and can be used as an index of antioxidant defences. In poultry production two forms of Se-dependent GSH-Px (GSH-Px1 and GSH-Px4) have received most attention. The aim of this paper is to review GSH-Px properties and functions in relation to poultry biology with special emphasis to its role in chicken adaptation to various stress conditions. Recent advances in selenoprotein identification and characterisation in relation to poultry Se status, dietary sources of Se and stress conditions can shed light on the roles of GSH-Px in avian biology.


Corresponding author

Corresponding author:


Hide All
ARAI, T., SUGAWARA, M., SAKO, T., MOTOYOSHI, S., SHIMURA, T., TSUTSUI, N. and KONNO, T. (1994) Glutathione peroxidase activity in tissues of chickens supplemented with dietary selenium. Comparative Biochemistry and Physiology 107A: 245-248.
BANNING, A., DEUBEL, S., KLUTH, D., ZHOU, Z. and BRIGELIUS-FLOHÉ, R. (2005) The GI-GPx gene is a target for Nrf2. Molecular and Cell Biology 25: 4914-4923.
BERTELSMANN, H., KUEHBACHER, M., WESELOH, G., KYRIAKOPOULOS, A. and BEHNE, D. (2007) Sperm nuclei glutathione peroxidases and their occurrence in animal species with cysteine-containing protamines. Biochimica et Biophysica Acta 1770: 1459-1467.
BREQUE, C., SURAI, P. and BRILLARD, J.P. (2006) Antioxidant status of the lower oviduct in the chicken varies with age and dietary vitamin E supplementation. Molecular Reproduction and Development 73: 1045-1051.
BRIGELIUS-FLOHÉ, R. and MAIORINO, M. (2013) Glutathione peroxidases. Biochimica et Biophysica Acta 1830: 3289-3303.
BUNK, M.J. and COMBS, G.F. (Jr) (1980) Effect of selenium on appetite in the selenium-deficient chick. Journal of Nutrition 110: 743-749.
CHADIO, S.E., PAPPAS, A.C., PAPANASTASATOS, A., PANTELIA, D., DARDAMANI, A., FEGEROS, K. and ZERVAS, G. (2015) Effects of high selenium and fat supplementation on growth performance and thyroid hormones concentration of broilers. Journal of Trace Elements in Medicine and Biology 29: 202-207.
CHANCE, B., SIES, H. and BOVERIES, A. (1979) Hydroperoxide metabolism in mammalian organs. Physiological Reviews 59: 527-605.
CHU, F.F., DOROSHOW, J.H. and ESWORTHY, R.S. (1993) Expression, Characterization, and Tissue Distribution of a New Cellular Selenium-dependent Glutathione Peroxidase, GSHPx-GI. The Journal of Biological Chemistry 268: 2571-2576.
COHEN, H.J. and AVISSAR, N. (1993) Molecular and biochemical aspects of selenium metabolism and deficiency. Progress in Clinical and Biological Research 380: 191-202.
COWAN, D.B., WEISEL, R.D., WILLIAMS, W.G. and MICKLE, D.A. (1993) Identification of oxygen responsive elements in the 5'-flanking region of the human glutathione peroxidase gene. Journal of Biological Chemistry 268: 26904-26910.
CRACK, P.J., TAYLOR, J.M., ALI, U., MANSELL, A. and HERTZOG, P.J. (2006) Potential contribution of NF-kappaB in neuronal cell death in the glutathione peroxidase-1 knockout mouse in response to ischemia-reperfusion injury. Stroke 37: 1533-1538.
DAUN, C. and AKESSON, B. (2004) Glutathione peroxidase activity, and content of total and soluble selenium in five bovine and porcine organs used in meat production. Meat Science 66: 801-807.
DE HAAN, J.B., CRACK, P.J., FLENTJAR, N., IANNELLO, R.C., HERTZOG, P.J. and KOLA, I. (2003) An imbalance in antioxidant defense affects cellular function: the pathophysiological consequences of a reduction in antioxidant defense in the glutathione peroxidase-1 (Gpx1) knockout mouse. Redox Report 8: 69-79.
ENGBERG, R.M., LAURIDSEN, C., JENSEN, S.K. and JAKOBSEN, K. (1996) Inclusion of oxidized vegetable oil in broiler diets. Its influence on nutrient balance and on the antioxidative status of broilers. Poultry Science 75: 1003-1011.
ESWORTHY, R.S., SWIDEREK, K.M., HO, Y.S. and CHU, F.F. (1998) Selenium-dependent glutathione peroxidase-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine . Biochimica et Biophysica Acta 1381: 213-226.
FLOHE, L. and BRIGELIUS-FLOHE, R. (2016) Basics and news on glutathione peroxidases, in: HATFIELD, D.L., SCHWEIZER, U., TSUI, P.A. & GLADYSHEV, V.N. (Eds) Selenium. Its molecular biology and role in human health, pp.211-222 (Fourth Edition, Springer, New York).
GAO, Y., ZHANG, J., HUANG, X. and ZHANG, G. (2017) Glutathione Peroxidase 1, Selenoprotein K, and Selenoprotein H May Play Important Roles in Chicken Testes in Response to Selenium Deficiency. Biological Trace Element Research 179: 271-276.
GHEISARI, H.R. and MOTAMEDI, H. (2010) Chloride salt type/ionic strength and refrigeration effects on antioxidant enzymes and lipid oxidation in cattle, camel and chicken meat. Meat Science 86: 377-383.
HANDY, D.E., LUBOS, E., YANG, Y., GALBRAITH, J.D., KELLY, N., ZHANG, Y.Y., LEOPOLD, J.A. and LOSCALZO, J. (2009) Glutathione peroxidase-1 regulates mitochondrial function to modulate redox-dependent cellular responses. Journal of Biological Chemistry 284: 11913-11921.
HOAC, T., DAUN, C., TRAFIKOWSKA, U., ZACKRISSON, J. and ÅKESSON, B. (2006) Influence of heat treatment on lipid oxidation and glutathione peroxidase activity in chicken and duck meat. Innovative Food Science and Emerging Technologies 7: 88-93.
IMAI, H. and NAKAGAWA, Y. (2003) Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radical Biology & Medicine 34: 145-169.
IMAI, H., SUMI, D., HANAMOTO, A., ARAI, M. and SUGIYAMA, A. (1995) Molecular cloning and functional expression of a cDNA for rat phospholipid hydroperoxide glutathione peroxidase: 3'-untranslated region of the gene is necessary for functional expression. Journal of Biochemistry(Tokyo) 118: 1061-1067.
JIANG, X.Q., CAO, C.Y., LI, Z.Y., LI, W., ZHANG, C., LIN, J., LI, X.N. and LI, J.L. (2017) Delineating hierarchy of selenotranscriptome expression and their response to selenium status in chicken central nervous system. Journal of Inorganic Biochemistry 169: 13-22.
JIN, X., KENNEDY, S.W., DI MUCCIO, T. and MOON, T.W. (2001) Role of oxidative stress and antioxidant defense in 3,3',4,4',5-pentachlorobiphenyl-induced toxicity and species-differential sensitivity in chicken and duck embryos. Toxicology and Applied Pharmacology 172: 241-248.
KIM, Y.S. and COMBS, G.F. (1993) Effect of dietary selenium and vitamin E on glutathione concentrations and glutathione S-transferase activities in chick liver and plasma. Nutrition Research 13: 455-463.
KONG, B.W., KIM, H. and FOSTER, D.N. (2003) Cloning and expression analysis of chicken phospholipid-hydroperoxide glutathione peroxidase. Animal Biotechnology 14: 19-29.
LI, J.L. and SUNDE, R.A. (2016) Selenoprotein Transcript Level and Enzyme Activity as Biomarkers for Selenium Status and Selenium Requirements of Chickens (Gallus gallus). PLoS One 11 (4): e0152392.
LUAN, Y., ZHAO, J., YAO, H., ZHAO, X., FAN, R., ZHAO, W., ZHANG, Z. and XU, S. (2016) Selenium Deficiency Influences the mRNA Expression of Selenoproteins and Cytokines in Chicken Erythrocytes. Biological Trace Element Research 171: 427-436.
LUBOS, E., LOSCALZO, J. and HANDY, D.E. (2011) Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxidants & Redox Signaling 15: 1957-1997.
MADDIPATI, K.R. and MARNETT, L.J. (1987) Characterization of the Major Hydroperoxide-Reducing Activity of Human Plasma. Purification and Properties of a Selenium-Dependent Glutathione Peroxidase. The Journal of Biological Chemistry 262: 17398-17403.
MANN, K. and MANN, M. (2008) The chicken egg yolk plasma and granule proteomes. Proteomics 8: 178-191.
MIYAZAKI, S. (1991) Effect of chemicals on glutathione peroxidase of chick liver. Research in Veterinary Science 51: 120-122.
MIYAZAKI, S. and MOTOI, Y. (1992) Tissue distribution of monomeric glutathione peroxidase in broiler chicks. Research in Veterinary Science 53: 47-51.
MIYAZAKI, S. and MOTOI, Y. (1996) Purification and characterisation of chicken liver monomeric glutathione peroxidase. British Poultry Science 37: 651-660.
MORK, H., LEX, B., SCHEURLEN, M., DREHER, I., SCHUTZE, N., KOHRLE, J. and JAKOB, F. (1998) Expression pattern of gastrointestinal selenoproteins - targets for selenium supplementation. Nutrition and Cancer 32: 64-70.
MUGESH, G. and SINGH, H.B. (2000) Synthetic organoselenium compounds as antioxidants: glutathione peroxidase activity. Chemical Society Reviews 29: 347-357.
NAM, S.Y., BAEK, I.J., LEE, B.J., IN, C.H., JUNG, E.Y., YON, J.M., AHN, B., KANG, J.K., YU, W.J. and YUN, Y.W. (2003) Effects of 17beta-estradiol and tamoxifen on the selenoprotein phospholipid hydroperoxide glutathione peroxidase (PHGPx) mRNA expression in male reproductive organs of rats. The Journal of Reproduction and Development 49: 389-396.
NAYERNIA, K., DIACONU, M., AUMULLER, G., WENNEMUTH, G., SCHWANDT, I., KLEENE, K., KUEHN, H. and ENGEL, W. (2004) Phospholipid hydroperoxide glutathione peroxidase: expression pattern during testicular development in mouse and evolutionary conservation in spermatozoa. Molecular Reproduction and Development 67: 458-464.
OMAYE, S.T. and TAPPEL, A.L. (1974) Effect of dietary selenium on glutathione peroxidase in the chick. Journal of Nutrition 104: 747-753.
PANNALA, V.R., BAZIL, J.N., CAMARA, A.K. and DASH, R.K. (2014) A mechanistic mathematical model for the catalytic action of glutathione peroxidase. Free Radical Research 48: 487-502.
PARTYKA, A., LUKASZEWICZ, E. and NIŻAŃSKI, W. (2012) Lipid peroxidation and antioxidant enzymes activity in avian semen. Animal Reproduction Science 134: 184-190.
PARTYKA, A., ŁUKASZEWICZ, E. and NIŻAŃSKI, W. (2012a) Effect of cryopreservation on sperm parameters, lipid peroxidation and antioxidant enzymes activity in fowl semen. Theriogenology 77: 1497-1504.
ROTRUCK, J.T., POPE, A.L., GANTHER, H.E., SWANSON, A.B., HAFEMAN, D.G. and HOEKSTRA, W.G. (1973) Selenium: biochemical role as a component of glutathione peroxidase. Science 179: 588-590.
ROVERI, A., MAIORINO, M., NISII, C. and URSINI, F. (1994) Purification and characterization of phospholipid hydroperoxide glutathione peroxidase from rat testis mitochondrial membranes. Biochimica et Biophysica Acta 1208: 211-221.
SAVASKAN, N.E., UFER, C., KÜHN, H. and BORCHERT, A. (2007) Molecular biology of glutathione peroxidase 4: from genomic structure to developmental expression and neural function. Biological Chemistry 388: 1007-1017.
SHARMA, A., YUEN, D., HUET, O., PICKERING, R., STEFANOVIC, N., BERNATCHEZ, P. and DE HAAN, J.B. (2016) Lack of glutathione peroxidase-1 facilitates a pro-inflammatory and activated vascular endothelium. Vascular Pharmacology 79: 32-42.
SINGH, A., RANGASAMY, T., THIMMULAPPA, R.K., LEE, H., OSBURN, W.O., BRIGELIUS-FLOHÉ, R., KENSLER, T.W., YAMAMOTO, M. and BISWAL, S. (2006) Glutathione peroxidase 2, the major cigarette smoke-inducible isoform of GPX in lungs, is regulated by Nrf2. American Journal of Respiratory Cell and Molecular Biology 35: 639-650.
STARRS, A.P., ORGEIG, S., DANIELS, C.B., DAVIES, M. and LOPATKO, O.V. (2001) Antioxidant enzymes in the developing lungs of egg-laying and metamorphosing vertebrates. Journal of Experimental Biology 204: 3973-3981.
SUNDE, R.A. (1993) Intracellular glutathione peroxidases - structure, regulation, and function, in: BURK, RF. (Ed.) Selenium in Biology and Human Health, pp.45-77 (Springer-Verlag New-York).
SUNDE, R.A. and HADLEY, K.B. (2010) Phospholipid hydroperoxide glutathione peroxidase (Gpx4) is highly regulated in male turkey poults and can be used to determine dietary selenium requirements. Experimental Biology and Medicine 235: 23-31.
SUNDE, R.A., SUNDE, G.R., SUNDE, C.M., SUNDE, M.L. and EVENSON, J.K. (2015) Cloning, Sequencing, and Expression of Selenoprotein Transcripts in the Turkey (Meleagris gallopavo). PLoS One 10 (6): e0129801.
SURAI, P.F. (1999) Tissue-specific changes in the activities of antioxidant enzymes during the development of the chicken embryo. British Poultry Science 40: 397-405.
SURAI, P.F. (2006) Selenium in Nutrition and Health. Nottingham University Press, Nottingham, UK.
SURAI, P.F. (2015) Carnitine Enigma: From Antioxidant Action to Vitagene Regulation. Part 2. Transcription Factors and Practical Applications. Journal of Veterinary Science and Medicine 3 (2): 17.
SURAI, P.F., BLESBOIS, E., GRASSEAU, I., GHALAH, T., BRILLARD, J-P., WISHART, G., CEROLINI, S. and SPARKS, N.H.C. (1998a) Fatty acid composition, glutathione peroxidase and superoxide dismutase activity and total antioxidant activity of avian semen. Comparative Biochemistry and Physiology 120B: 527-533.
SURAI, P.F., BRILLARD, J-P., SPEAKE, B.K., BLESBOIS, E., SEIGNEURIN, F. and SPARKS, N.H.C. (2000) Phospholipid fatty acid composition, vitamin E content and susceptibility to lipid peroxidation of duck spermatozoa. Theriogenology 53: 1025-1039.
SURAI, P.F., CEROLINI, S., WISHART, G.J., SPEAKE, B.K., NOBLE, R.C. and SPARKS, N.H.C. (1998b) Lipid and antioxidant composition of chicken semen and its susceptibility to peroxidation. Poultry and Avian Biology Reviews 9: 11-23.
SURAI, P.F. and FISININ, V.I. (2016a) Vitagenes in poultry production. Part 1. Environmental and technological stresses. World's Poultry Science Journal 72: 721-734.
SURAI, P.F. and FISININ, V.I. (2016b) Vitagenes in poultry production. Part 1. Nutritional and Internal stresses. World's Poultry Science Journal 72: 761-772.
SURAI, P.F., KOSTJUK, I.A., WISHART, G., MACPHERSON, A., SPEAKE, B., NOBLE, R.C., IONOV, I.A. and KUTZ, E. (1998c) Effect of vitamin E and selenium of cockerel diets on glutathione peroxidase activity and lipid peroxidation susceptibility in sperm, testes and liver. Biological Trace Element Research 64: 119-132.
SURAI, P.F., SPEAKE, B.K., NOBLE, R.C. and SPARKS, N.H.C. (1999) Tissue-specific antioxidant profiles and susceptibility to lipid peroxidation of the newly hatched chick. Biological Trace Element Research 68: 63-78.
TAKAHASHI, K., AVISSAR, N., WHITIN, J. and COHEN, H. (1987) Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme. Archives of Biochemistry and Biophysics 256: 677-686.
TAPPEL, M.E., CHAUDIERE, J. and TAPPEL, A.L. (1982) Glutathione peroxidase activities of animal tissues. Comparative Biochemistry and Physiology B. 73: 945-949.
TAYLOR, R.M. and SUNDE, R.A. (2016) Selenoprotein Transcript Level and Enzyme Activity as Biomarkers for Selenium Status and Selenium Requirements in the Turkey (Meleagris gallopavo). PLoS One 11 (3): e0151665.
URSINI, F., MAIORINO, M. and GREGOLIN, C. (1985) The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochimica et Biophysica Acta 839: 62-70.
URSINI, F., HEIM, S., KIESS, M., MAIORINO, M., ROVERI, A., WISSING, J. and FLOHÉ, L. (1999) Dual function of the selenoprotein PHGPx during sperm maturation. Science 285: 1393-1396.
VENDITTI, P., DANIELE, C.M., BALESTRIERI, M. and DI MEO, S. (1999) Protection against oxidative stress in liver of four different vertebrates. Journal of Experimental Zoology 284: 610-616.
YAO, H., ZHAO, W., ZHAO, X., FAN, R., KHOSO, P.A., ZHANG, Z., LIU, W. and XU, S. (2014) Selenium deficiency mainly influences the gene expressions of antioxidative selenoproteins in chicken muscles. Biological Trace Element Research 161: 318-327.
ZENTENO-SAVIN, T., ST LEGER, J. and PONGANIS, P.J. (2010) Hypoxemic and ischemic tolerance in emperor penguins. Comparative Biochemistry and Physiology C. Toxicology and Pharmacology 152: 18-23.
ZHANG, J.L., XU, B., HUANG, X.D., GAO, Y.H., CHEN, Y. and SHAN, A.S. (2016) Selenium Deficiency Affects the mRNA Expression of Inflammatory Factors and Selenoprotein Genes in the Kidneys of Broiler Chicks. Biological Trace Element Research 171: 201-207.
ZOIDIS, E., PAPPAS, A.C., GEORGIOU, C.A., KOMAITIS, E. and FEGGEROS, K. (2010) Selenium affects the expression of GPx4 and catalase in the liver of chicken. Comparative Biochemistry and Physiology. B Biochemistry and Molecular Biology 155: 294-300.



Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Abstract views

Total abstract views: 0 *
Loading metrics...

* Views captured on Cambridge Core between <date>. This data will be updated every 24 hours.

Usage data cannot currently be displayed