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A. Spodniewska, D. Barski and H. Ziółkowski

References Abdallah FB, Gargouri B, Bejaoui H, Lassoued S, Ammar- Keskes L (2011) Dimethoate-induced oxidative stress in human erythrocytes and the protective effect of vitamins C and E in vitro. Environ Toxicol 26: 287-291. Abou Ghalia AH, Fouad IM (2000) Glutathione and its metabolizing enzymes in patients with different benign and malignant diseases. Clin Biochem 33: 657-662. Ajiboye TO (2010) Redox status of the liver and kidney of 2,2-dichlorovinyl dimethyl phosphate (DDVP) treated rats. Chem Biol Interact

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Abdellah Ali and Phalisteen Sultan

. Oxygen radicals and human disease. Ann Int Med 2001; 107: 526-45. Nikolić-Kokić A, Blagojević D, Spasić B. M. Complexity of free radical metabolism in human erythrocytes. Journal of Medical Biochemistry 2010; 29: 189-95. Buege JA, Aust SD. Microsomal lipid peroxidation. Methods Enzymol 1978; 52: 302-10. Beutler E, Duran O, Kelly BM. Improved method for determination of blood glutathione. J Lab Clin Med 1963; 61: 882-8. Paglia DE, Valentine WN. Studies on the

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Ewa Karwicka

glutathione transporters and their roles in cell physiology and pathophysiology. Mol Aspects Med 2009; 30(1-2): 13-28. [5] BALLATORI N, REBBEOR JF. Roles of MRP2 and oatp1 in hepatocellular export of reduced glutathione. Semin Liver Dis 1998; 18(4): 377-387. [6] BILSKA A, KRAWCZYK A, WŁODEK L. Różne oblicza biologicznej roli glutationu. Postepy Hig Med Dosw 2007; 61: 438-453. [7] BODA D, NÉMETH I, PINTÉR S. Surface tension, glutathione content and redox ratio of the tracheal aspirate fluid of premature infants with IRDS. Biol

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S. Gupta, N. Banu and A. Srivastava

[1] Anders, M. W. (1978): Inhibition and enhancement of microsomal drug metabolism by diethylmaleate. Biochem. Pharmacol., 27: 1098–1101 http://dx.doi.org/10.1016/0006-2952(78)90164-8 [2] Barnhart, J. L., Combes, B. (1978): Choleresis associated with metabolism and biliary excretion of diethylmaleate in the rat and dog. J. Pharmacol. Exp. Ther., 206: 614–623 [3] Boyland, E., Chasseaud, L. F. (1967): Enzyme-catalysed conjugations of glutathione with unsaturated compounds. Biochem. J., 104

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Sreenivasulu Dasari, Muni Swamy Ganjayi and Balaji Meriga

REFERENCES Abbott NJ, Rönnbäck L, Hansson E. (2006). Astrocyte–endothelial interactions at the blood–brain barrier. Nat Rev Neurosci 7 (1): 41–53. Abramovitz M, Listowsky I. (1987). Selective expression of a unique glutathione S-transferase Yb3 gene in rat brain. Journal of Biological Chemistry 262 (16): 7770–7773. Adler ID, Zouh R, Schmid E. (1993). Perturbation of cell division by acrylamide in vitro and in vivo. Mutat Res 301 (4): 249–54. Allam A, El-Ghareeb AA, Abdul-Hamid M, Baikry A, Sabri MI. (2011). Prenatal and perinatal

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R. Ahmad and A. Srivastava

[1] Armstrong, R. N. (1997): Structure, catalytic mechanism and evolution of the glutathione-S-transferase(s). Chem. Res. Toxicol., 10: 2–18 http://dx.doi.org/10.1021/tx960072x [2] Brophy, P. M., Barrett, J. (1990): Glutathione-S-transferase in helminths. Parasitol., 100: 345–349 http://dx.doi.org/10.1017/S0031182000061369 [3] Brophy, P. M., Campbell, A. M., Van Eldick, A. J., Teesdale-spittle, P. H., Liebau, E., Wang, M. F. (2000): β-Carbonyl substituted glutathione conjugates as

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Martin Nikolovski, Ljupco Mickov, Monika Dovenska, Vladimir Petkov, Branko Atanasov and Toni Dovenski

human spermatozoa. I. Effects on the motility of intact spermatozoa and on sperm axonemes. J. Androl. 13, 368-378. PMid:1331006 11. Griveau, J. F., Le Lannou, D. (1994). Effects of antioxidants on human sperm preparation techniques. Int. J. Androl., 17, 225-231. http://dx.doi.org/10.1111/j.1365-2605.1994.tb01247.x PMid:7698847 12. Lenzi A., Gandini L., Picardo M. (1998). A rationale for glutathione therapy. Hum Reprod.13(6):1419-22. PMid:9688363 13. Irvine, D.S. (1996). Gluthatione as a treatment for male infertility

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Tatjana Simić, Ana Savić-Radojević, Marija Plješa-Ercegovac, Marija Matić, Tatjana Sašić, Dejan Dragičević and Jasmina Mimić-Oka

References Longuemaux S, Deloménie C, Gallou C, Méjean A, Vincent-Viry M, Bouvier R, et al. Candidate genetic modifiers of individual susceptibility to renal cell carcinoma: a study of polymorphic human xenobiotic-metabolizing enzymes. Cancer Res 1999; 59 (12): 2903-8. Kempkes M, Golka K, Reich S, Reckwitz T, Bolt HM. Glutathione S-transferase GSTM1 and GSTT1 null genotypes as potential risk factors for urothelial cancer of the bladder. Arch Toxicol 1996; 71 (1-2): 123-6. Okkels

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Dijana Mirić, Bojana Kisić, Lepša Žorić, Zana Dolićanin, Radoslav Mitić and Marko Mirić

. Clin Biochem 2007; 40: 705-9. Faschinger C, Schmut O, Wachswender C, Mossbock G. Glaucoma and oxidative stress. Determination of malondialdehyde - a product of lipid peroxidation. Ophthalmologe 2006; 103: 953-9. Azeem AAA, Mahmoud AA, Salaheldine MM, Amr K. Implication of glutathione S-transferase M1 and T1 polymorphisms in the development of senile cataract among Egyptians. Bratisl Lek Listy 2009; 110: 678-83. Brigelius-Flohe R, Banning A, Schnurr K. Selenium-dependent enzymes in

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B. Pilarczyk, A. Tomza-Marciniak, T. Stankiewicz, B. Błaszczyk, D. Gączarzewicz, M. Smugała, J. Udała, A. Tylkowska, J. Kuba and A. Cieśla

References Balicka-Ramisz A, Ramisz A, Nicpoh J, Pikula R (2002) Untersuchungen zur Selen-Versorgung von Pferden in Nordwestpolen. Tierarztl Umsch 57: 496-498. Bedwal RS, Nair N, SharmaMP, Mathur RS (1993) Selenium - its biological perspectives. Med Hypotheses 41: 150-159. Behne D, Duk M, Elger W (1986) Selenium content and glutathione peroxidase activity in the testis of the maturing rat. J Nutr 116: 1442-1447. Crisman MV, Carmel DK, Lessard P, Ley WB (1994) A survey of whole blood selenium