Activity of glutathione-dependent enzymes in spermatozoa in patients with pathospermia

O. K. Onufrovych, R. V. Fafula, Io. A. Nakonechnyi, D. Z. Vorobets, U. P. Iefremova, Z. D. Vorobets

Abstract


The results of glutathione peroxidase and glutathione reductase activity in spermatozoa of patients with different forms pathospermia are presented in the paper. It was shown that glutathione peroxidase and glutathione reductase activity in sperm cells of patients is reduced in comparison with healthy men with preserved fertility. However, the most expressed changes in the activity of glutathione peroxidase and glutathione reductase are in spermatozoa of infertile men with associated forms patospermia and leucospermia. These changes indicate exhaustion of compensatory mechanisms of glutathione antioxidant system in the sperm cells of infertile men with pahospermia.


Keywords


sperm; antioxidant system; hydrogen peroxide; reactive oxygen species; glutathione peroxidase; glutathione reductase; male infertility.

References


Aitken Robert J. Redox Regulation of Human Sperm Function: From the Physiological Control of Sperm Capacitation to the Etiology of Infertility and DNA Damage in the Germ Line / Robert J. Aitken and Benjamin J. Curry // Antioxidants & Redox Signaling. – 2011. – 14, № 3. – P. 367–381.

Kashou A. H. Assessment of oxidative stress in sperm and semen / A. H. Kashou, R. Sharma, A. Agarwal // Methods in Mol. Biol. – 2013. – 927. – P. 351–361.

Makker K. Oxidative stress and male infertility / K. Makker, A. Agarwal, R. Sharma // Indian J. of Med. Res. – 2009. – 129, № 4. – Р. 357–367.

Sperm viability, apoptosis, and intracellular reactive oxygen species levels in human spermatozoa before and after induction of oxidative stress / R. Z. Mahfouz, S. S. du Plessis, N. Aziz [et al.] // Fertil. and Steril. – 2010. – 93, № 3. – P. 814–821.

Ko E. Y. Male infertility testing: reactive oxygen species and antioxidant capacity / E. Y. Ko, E. S. Jr. Sabanegh, A. Agarwal // Fertil. and Steril. – 2014. – 102. – P. 1518–1527.

Zhadan V. M. Vyvchennia funktsionalnoho stanu hlutationzalezhnykh fermentiv erytrotsytiv u khvorykh na idiopatychni interstytsialni pnevmonii / V. M. Zhadan // Tuberkuloz, lehenevi khvoroby, VIL-infektsiia. – 2012. – 10, № 3 – S. 36–41.

World Health Organization. WHO laboratory manual for the examination and processing of human semen. 5th ed. Geneva: World Health Organization Press. – 2010. – P. 286.

Vorobets D. Z. Neplidnist ta erektylna dysfunktsiia cholovikiv: biokhimichni ta klinichni aspekty / D. Z. Vorobets, N. S. Kocheshkova. − Ternopil: Ukrmedknyha, 2008. – 204 s.

9. Herush I. V. Ratsionalna propozytsiia Chernivetskoho derzhavnoho medychnoho universytetu № 25/95 / I. V. Herush, N. P. Hryhor’ieva, I. F. Meshchyshen.

Moin V. M. Prostoi i spetcificheskii metod opredeleniia aktivnosti glutationperoksidazy v eritrotcitakh / V. M. Moin // Lab. delo. − 1986. − 12. − S. 124−126.

11. Vlasov S. N. Aktivnost glutationzavisimykh fermentov eritrotcitov pri khronicheskikh zabolevaniiakh pecheni u detei / S. N. Vlasova, E. I. Shabunina, I. A. Pereslegina // Lab. delo. – 1990. − № 8. − S. 19−22.

Onufrovych O. K. Stan hlutationovoi antyoksydantnoi systemy spermatozoidiv pry ekskretorno-toksychnii formi neplidnosti cholovikiv / O. K. Onufrovych, R. V. Fafula, D. Z. Vorobets // Zdobutky klinich. i eksperym. medytsyny. − 2013. − № 2. − S. 148−151.

Fafula R. V. The peculiarities of arginase pathway of l-arginine in spermatozoa in men with different forms of pathospermia / R. V. Fafula, O. K. Onufrovych, U. P. Iefremova [et al.] // Fiziol. J. – 2016. – 62, № 5. – P. 83–90.

Vorobets D. Z. The NO-synthase pathway of L-arginine transformation in spermatozoa of infertile men with different forms of patospermia / D. Z. Vorobets, О. K. Оnufrovych, R. V. Fafula [et al.] // Exper. and Clin. Phys. and Bioch. – 2016. – 3, № 75. – P. 47–53.

Muller F. L. Trends in oxidative aging theories / F. L. Muller, M. S. Lustgarten, Y. Jang [et al.] // Free Radic. Biol. Med. – 2007. – 43, № 4. – P. 477–503.

Ran Q. Reduction in glutathione peroxidase 4 increases life span through increased sensitivity to apoptosis / Q. Ran, H. Liang, Y. Ikeno [et al.] // A Biol. Sci. Med. Sci. – 2007. – 62, № 9. – Р. 932–942.

Deprem T. Distribution of glutathione peroxidase 1 in liver tissues of healthy and diabetic rats treated with capsaisin / T. Deprem, S. E. Yildiz, E. K. Sari [et al.] // Biotech. Histochem. – 2015. – 90. – P. 1–7.

Tramer F. Native specific activity of glutathione peroxidase (GPx-1), phospholipid hydroperoxide glutathione peroxidase (PHGPx) and glutathione reductase (GR) does not differ between normo- and hypomotile human sperm samples / F. Tramer, L. Caponecchia, P. Sgrò [et al.] // Int. J. Androl. –2004. – 27, № 2. – Р. 88–93.

Dandekar S. P. Lipid peroxidation and antioxidant enzymes in male infertility / S. P. Dandekar, G. D. Nadkarni, V. S. Kulkarni [et al.] // J. Postgrad. Med. – 2002. – 48, № 3. – P. 186–189.

Tkaczuk-Włach J. Activity of superoxide dismutase and glutathione peroxidase in human semen in normozoospermia and spermatopathy / J. Tkaczuk-Włach, M. Kankofer, G. Jakiel // Ann. Univ. Mariae Curie Sklodowska Med. – 2002. – 57, № 2. – P. 369–375.

Diaconu M. Failure of phospholipid hydroperoxide glutathione peroxidise expression in oligoasthenozoospermia and mutations in the PHGPx gene / M. Diaconu, Y. Tangat, D. Böhm [et al.] // Andrologia. – 2006. – 38, № 4. – P. 152–157.

Zhang W. D. Oxygen free radicals and mitochondrial signaling in oligospermia and asthenospermia / W. D. Zhang, Z. Zhang, L. T. Jia [et al.] // Mol. Med. Rep. – 2014. – 10, № 4. – P. 1875–1880.

Yan J. Glutathione Reductase Facilitates Host Defense by Sustaining Phagocytic Oxidative Burst and Promoting the Development of Neutrophil Extracellular Traps / J. Yan, X. Meng, L. M. Wancket [et al.] // The Journal of Immunology. – 2012. – 188, № 5. – P. 2316–2327.

Kand’ar R. Assay of total glutathione and glutathione disulphide in seminal plasma of male partners of couples presenting for a fertility evaluation / R. Kand’ar, N. Hajkova // Andrologia. – 2014. – 46, P. 1079–1088.




DOI: http://dx.doi.org/10.11603/mcch.2410-681X.2016.v0.i4.7246

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