Volume 13, Issue 9 (10-2015)                   IJRM 2015, 13(9): 541-548 | Back to browse issues page

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Menendez-Helman R J, Sanjurjo C, Miranda P V. Seminal plasma hexosaminidase in patients with normal and abnormal spermograms. IJRM 2015; 13 (9) :541-548
URL: http://ijrm.ir/article-1-683-en.html
Seminal plasma hexosaminidase in patients with normal and abnormal spermograms
Renata Julia Menendez-Helman * 1, Claudia Sanjurjo2 , Patricia Vivian Miranda3
1- Instituto de Biología y Medicina Experimental – CONICET. Buenos Aires, Argentina , rmenendez@qi.fcen.uba.ar
2- Fertilab Buenos Aires, Argentina
3- Instituto de Biología y Medicina Experimental – CONICET. Buenos Aires, Argentina
Abstract:   (2558 Views)
Background: Glycosidases profusion in male reproductive fluids suggests a possible relationship with sperm function. Although Hexosaminidase (Hex) is the most active glycosidase in epididymal fluid and seminal plasma, as well as in spermatozoa, Glucosidase is considered a marker for epididymal function and azoospermia.
Objective: The aim of this study was to determine Hex activity in seminal plasma from patients with normal and abnormal spermograms and analyze its correlation with seminal parameters.
Materials and Methods: In this cross sectional study, seminal plasma from azoospermic, asthenozoospermic, teratozoospermic, and normozoospermic patients was analyzed for the activity of: total Hex, HexA isoform, and glucosidase. Besides, hexosamine levels were determined, and the amount of Hex was quantified by immunoblot with a specific antibody. Correlation of Hex activity with seminal parameters was also analyzed.
Results: Hex activity, like glucosidase, was significantly reduced in azoospermic samples (44, 49, and 60% reduction for total Hex, HexA and glucosidase, respectively). A reduced amount of Hex in azoospermic samples was confirmed by western immunoblot. Hex activity was negatively correlated with round cells in azoospermic samples and positively correlated with motility in asthenozoospermic ones.
Conclusion: The results suggested that Hex activity was reduced in azoospermic samples and this was due to a lower amount of enzyme. The correlation to seminal parameters related to particular pathologies suggests a possible relationship of Hex with fertilizing capacity.
Keywords: Glycosidases, Seminal plasma, Hexosaminidase, N-acetylglucosaminidase, Semen Analysis.
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Type of Study: Original Article |
References
1. Conchie J, Findlay J, Levvy GA. Mammalian Glycosidases. Biochem J 1959; 71:318-325. [DOI:10.1042/bj0710318]
2. Kytzia HJ, Sandhoff K. Evidence for two different active sites on human beta-Hexosaminidase A. Interaction of GM2 activator protein with beta-Hexosaminidase A. J Biol Chem 1985; 260:7568-7572.
3. Guerin JF, Rollet J, Perrin P, Menezo Y, Orgiazzi A, Czyba JC. Enzymes in the seminal plasma from azoospermic men: correlation with the origin of their azoospermia. Fertil Steril 1981; 36:368-372. [DOI:10.1016/S0015-0282(16)45740-7]
4. García Díez LC, Esteban Ruiz PF, Villar E, Corrales Hernandez JJ, Burgo R, Delgado M, et al. Enzyme and hormonal markers in the differential diagnosis of human azoospermia. Arch Androl 1992; 28:181-194. [DOI:10.3109/01485019208987697]
5. Conchie J, Mann T. Glycosidases in mammalian sperm and seminal plasma. Nature 1957; 179:1190-1191. [DOI:10.1038/1791190a0]
6. Miller DJ, Gong X, Shur BD. Sperm require beta-N-acetylglucosaminidase to penetrate through the egg zona pellucida. Development 1993; 118:1279-1289.
7. Miranda PV, Brandelli A, Tezón JG. Characterization of beta-N acetylglucosaminidase from human epididymis. Int J Androl 1995; 18:263-270.
8. Miranda PV, Gonzalez Echeverria F, Blaquier JA, Mahuran DJ, Tezon JG. Evidence for the participation of beta-hexosaminidase in human sperm-zona pellucida interaction in vitro. Mol Hum Reprod 2000; 6:699-706. [DOI:10.1093/molehr/6.8.699]
9. Brandelli A, Miranda PV, Tezon JG. Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase. Biochim Biophys Acta 1994; 1220:299-304. [DOI:10.1016/0167-4889(94)90152-X]
10. Perez Martinez SL, Menendez Helman RJ, Zitta KS, Brandelli A, Miranda PV. Characterization of human sperm N-acetylglucosaminidase. Int J Androl 2008; 31:315-324. [DOI:10.1111/j.1365-2605.2007.00766.x]
11. Ashrafzadeh A, Karsani SA, Nathan S. Mammalian Sperm Fertility Related Proteins. Int J Med Sci 2013; 10:1649-1657. [DOI:10.7150/ijms.6395]
12. Kovac JR, Pastuszak AW, Lamb DJ. The use of genomics, proteomics, and metabolomics in identifying biomarkers of male infertility. Fertil Steril 2013, 99: 998-1007. [DOI:10.1016/j.fertnstert.2013.01.111]
13. World Health Organization. WHO laboratory manual for the examination of human semen and sperm cervical mucus interaction. Forth Edition. New York: Cambridge University Press, 1999.
14. Jungwirth A, Giwercman A, Tournaye H, Diemer T, Kopa Z, Dohle G, et al. European Association of Urology guidelines on Male Infertility: the 2012 update. Europ Urol 2012; 62:324-332. [DOI:10.1016/j.eururo.2012.04.048]
15. Roy S, Banerjee A, Pandey HC, Singh G, Kumari GL. Application of seminal germ cell morphology and semen biochemistry in the diagnosis and management of azoospermic subjects. Asian J Androl 2001;3:55-62.
16. Reissig JL, Storminger JL, Leloir LF. A modified colorimetric method for the estimation of N-acetylamino sugars. J Biol Chem 1955; 217:959-966.
17. Brandelli A, Miranda PV, A-ón-Vazquez MG, Marín-Briggiler CI, Sanjurjo C, Gonzalez-Echeverría F, et al. A new predictive test for in-vitro fertilization based on the induction of sperm acrosome reaction by N-acetylglucosamine-neoglycoprotein. Hum Reprod 1995; 10:1751-1756. [DOI:10.1093/oxfordjournals.humrep.a136168]
18. Dandekar SP, Harikumar P. Seminal profiles of lysosomal enzymes in normal and infertile men. J Postgrad Med 1997; 43:33-37.
19. Casal JA, Vizcaino L, Garcia-Devesa J, Tutor JC. Thermodynamic study of beta-N-acetylhexosaminidase enzyme heterogeneity in human seminal plasma. Clin Chim Acta 2005; 355:55-60. [DOI:10.1016/j.cccn.2004.12.015]
20. Tassi C, Angelini A, Beccari T, Capodicasa E. Fluorimetric determination of activity and isoenzyme composition of N-acetyl-beta-D-hexosaminidase in seminal plasma of fertile men and infertile patients with secretory azoospermia. Clin Chem Lab Med 2006; 44:843-847. [DOI:10.1515/CCLM.2006.154]
21. Brown-Woodman PDC, Marley PB, Morris S, Rodger JC, White IG. Origin of glycerylphosphorylcholine, inositol, N-acetylaminosugar, and prostaglandins in human seminal plasma and their effects on sperm metabolism. Arch Androl 1980; 4:149-155. [DOI:10.3109/01485018008986482]
22. Van der Ven HH, Jeyendran RS, Perez-Pelaez M, Al Hasani S, Diedrich K, Krebs D. Leucospermia and the fertilizing capacity of spermatozoa. Eur J Obstet Gynecol Reprod Biol 1987; 24:49-52. [DOI:10.1016/0028-2243(87)90036-0]
23. Tomlinson MJ, Lenton EA, Barratt CLR, Roberts HB, Bolton AE, Cooke ID. Round cells and sperm fertilizing capacity: The presence of immature germ cells but not seminal leukocytes are associated with reduced success of in vitro fertilization. Fertil Steril 1992; 58:1257-1259. [DOI:10.1016/S0015-0282(16)55583-6]
24. Kumar GP, Laloraya M, Agrawal P, Laloraya MM. The involvement of surface sugars of mammalian spermatozoa in epididymal maturation and in vitro sperm-zona recognition. Andrologia 1990; 22:184-194. [DOI:10.1111/j.1439-0272.1990.tb01964.x]
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