شنبه 8 دی 1403
[Archive]
دوره 8، شماره 3 - ( 4-1389 )
جلد 8 شماره 3 صفحات 124-119 |
برگشت به فهرست نسخه ها
Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
Talaei T, Esmaeelpour T, Aekiyash F, Bahmanpour S. Effects of cryopreservation on plasma membrane glycoconjugates of human spermatozoa. IJRM 2010; 8 (3) :119-124
URL: http://ijrm.ir/article-1-183-fa.html
URL: http://ijrm.ir/article-1-183-fa.html
Effects of cryopreservation on plasma membrane glycoconjugates of human spermatozoa. International Journal of Reproductive BioMedicine. 1389; 8 (3) :119-124
چکیده: (2025 مشاهده)
Background: Cryopreservation has some detrimental impacts on sperms surface molecules. Modification of the sperm surface molecules can affect on fertility rate. One of the important surface molecules are glycoconjugates.
Objective: The objective of this study was to evaluate the changes of content of the glycocalyx after standard cryopreservation procedure.
Materials and Methods: Forty five healthy semen samples were frozen in 0.5ml plastic straws and kept in liquid nitrogen and thaw after 48 hours. Sperm smears were prepared before and after freezing and thawing. The smears were stained with the lectins and also with acridin orange. The smears were studied by fluorescents microscopy and the intensities of the reactions to lectins were measured by image analyses software.
Results: The reactions of the sperm samples to Peanut agglutinin (PNA) Wheat germ agglutinin (WGA) and Dolichos biflorus (DBA) changed after cryopreservation and the percentage of samples that showed modifications were 46.67% 34.09% and 73.34% respectively. The crypreservation led to both increase and decrease the intensities of the reactions. It means that there are various mechanisms that impact on the carbohydrate contents of the sperm surface. There is no correlation between DNA denaturation of sperms and their lectin binding patterns.
Conclusion: Cryopreservation affected the surface glycoconjugates at least in a subset of spermatozoa. These results might cause to modify the future application of sperm banking techniques.
Objective: The objective of this study was to evaluate the changes of content of the glycocalyx after standard cryopreservation procedure.
Materials and Methods: Forty five healthy semen samples were frozen in 0.5ml plastic straws and kept in liquid nitrogen and thaw after 48 hours. Sperm smears were prepared before and after freezing and thawing. The smears were stained with the lectins and also with acridin orange. The smears were studied by fluorescents microscopy and the intensities of the reactions to lectins were measured by image analyses software.
Results: The reactions of the sperm samples to Peanut agglutinin (PNA) Wheat germ agglutinin (WGA) and Dolichos biflorus (DBA) changed after cryopreservation and the percentage of samples that showed modifications were 46.67% 34.09% and 73.34% respectively. The crypreservation led to both increase and decrease the intensities of the reactions. It means that there are various mechanisms that impact on the carbohydrate contents of the sperm surface. There is no correlation between DNA denaturation of sperms and their lectin binding patterns.
Conclusion: Cryopreservation affected the surface glycoconjugates at least in a subset of spermatozoa. These results might cause to modify the future application of sperm banking techniques.
نوع مطالعه: Original Article |
فهرست منابع
1. Peláez J, Long JA. Characterizing the glycocalyx of poultry spermatozoa: I. Identification and distribution of carbohydrate residues using flow cytometry and epifluorescence microscopy. J Androl 2007; 28: 342-352. [DOI:10.2164/jandrol.106.001073]
2. Diekman AB. Glycoconjugates in sperm function and gamete interactions: how much sugar does it take to sweet-talk the egg? Cell Mol Life Sci 2003; 60: 298 –308. [DOI:10.1007/s000180300025]
3. Lassalle B, Testart J. Human zona pellucida recognition associated with removal of sialic acid from human sperm surface. J Reprod Fertil 1994; 101:703-711. [DOI:10.1530/jrf.0.1010703]
4. Grudzinskas JG, Yovich J. Cambridge review in human reproduction, Gametes: the spermatozoon. Cambridge University press: pp 57.
5. Chandra A, Srinivasan KR, Jamal F, Mehrotra PK, Singh RL, Srivastav A. Post-translational modifications in glycosylation status during epididymal passage and significance in fertility of a 33 kDa glycoprotein (MEF3) of rhesus monkey (Macaca mulatta). Reproduction 2008; 135:761-770. [DOI:10.1530/REP-07-0525]
6. Purohit S, Laloraya M, Kumar PG. Distribution of N- and O-linked oligosaccharides on surface of spermatozoa from normal and infertile subjects. Andrologia. 2008; 40: 7-12. [DOI:10.1111/j.1439-0272.2008.00801.x]
7. Curry MR. Cryopreservation of mammalian semen. Methods Mol Biol 2007; 368: 303-311. [DOI:10.1007/978-1-59745-362-2_21]
8. Bagchi A, Woods EJ, Critser JK. Cryopreservation and vitrification: recent advances in fertility preservation technologies. Expert Rev Med Devices 2008; 5: 359-370. [DOI:10.1586/17434440.5.3.359]
9. Critser JK, Arneson BW, Aaker DV, Huse-Benda AR, Ball GD. Cryopreservation of human spermatozoa. II. Post-thaw chronology of motility and zona-free hamster ova penetration. Fertil Steril 1987; 47: 980. [DOI:10.1016/S0015-0282(16)59233-4]
10. McLaughlin EA, Ford WC, Hull MG. Motility characteristics and membrane integrity of cryopreserved human spermatozoa. J Reprod Fertil 1992; 95, 527–534 [DOI:10.1530/jrf.0.0950527]
11. Alvarez JG, Storey BT. Evidence that membrane stress contributes more than lipid peroxidation to sublethal cryodamage in cryopreserved human sperm: glycerols and other polyols as sole cryoprotectant. J Androl 1993; 14, 199–208.
12. Mack SR, Zaneveld LJ. Acrosomal enzymes and ultrastructure of unfrozen and cryotreated human spermatozoa. Gamete Res 1987; 18, 375–383. [DOI:10.1002/mrd.1120180411]
13. Nallella KP, Sharma RK, Allamaneni SS, Aziz N, Agarwal A. Cryopreservation of human spermatozoa: comparison of two cryopreservation methods and three cryoprotectants. Fertil Steril 2004; 82: 913-918. [DOI:10.1016/j.fertnstert.2004.02.126]
14. Cross NL, Overstreet JW. Glycoconjugates of the human sperm surface: Distribution and alterations that accompany capacitation in vitro. Gamete Res 1987; 16; 23 – 35. [DOI:10.1002/mrd.1120160104]
15. Benoff S. Carbohydrates and fertilization: an overview. Molecular Human Reproduction 1997; 3: 599–637 [DOI:10.1093/molehr/3.7.599]
16. World Health Organization, Laboratory manual for the examination of human semen and sperm-cervical mucus interaction. 4th Ed. Cambridge University Press; Cambridge; 1999.
17. Medrano A, Holt WV, Watson PF. Controlled freezing studies on boar sperm cryopreservation. Andrologia 2009; 41:246-250. [DOI:10.1111/j.1439-0272.2009.00927.x]
18. Lee SH, Ahula KK. An investigation using lectin glycocomponents of mouse spermatozoa during capacitation and sperm- zona binding. J reprod fertility 1987; 80: 650-684.
19. Ngamwuttiwong T, Kunathikom S. Evaluation of Cryoinjury of Sperm Chromatin According to Liquid Nitrogen Vapour Method (I). J Med Assoc Thai 2007; 90: 224-228.
20. Perotti ME, Pasini ME. Glycoconjugates of the surface of the spermatozoa of Drosophila melanogaster: a qualitative and quantitative study. J Exp Zool 1995; 1; 272:311-318 [DOI:10.1002/jez.1402720409]
21. Zhan-xiang Z, Ze-pei D, Xiu-hua S. Distribution of surface glycoconjugates of bull sperm and the effect of washing. Acta Anatomica Synica 1994; 2; 71-75.
22. Bains UK, Sehgal S, Bawa SR. Human Sperm Surface Mapping with Lectins. Acta Anat 1992; 145, 207-211 [DOI:10.1159/000147367]
23. Lee MC, Damjanov I. Lectin binding sites on human sperm and permatogenic cells. Anat Rec 1985; 212: 282-287. [DOI:10.1002/ar.1092120310]
24. Kallajoki M, Virtanen I, Suominen J. The fate of acrosomal staining during the acrosome reaction of human spermatozoa as revealed by a monoclonal antibody and PNA-lectin. Int J Androl 1986; 9: 181-194. [DOI:10.1111/j.1365-2605.1986.tb00881.x]
25. Hotz MA, Traganos F, Darzynkiewicz Z. Changes in nuclear chromatin related to apoptosis or necrosis induced by the DNA topoisomerase II inhibitor fostriecin in MOLT-4 and HL-60 cells are revealed by altered DNA sensitivity to denaturation, Exp Cell Res 1992; 201: 184-191. [DOI:10.1016/0014-4827(92)90362-C]
26. Suzuki O, Nozawa Y, Abe M. Sialic acids linked to glycoconjugates of Fas regulate the caspase-9-dependent [DOI:10.3892/ijo.23.3.769]
27. He S, Woods LC. Effects of dimethyl sulfoxide and glycine on cryopreservation induced damage of plasma membranes and mitochondria to striped bass (Morone saxatilis) sperm. Cryobiology 2004; 48: 254–262. [DOI:10.1016/j.cryobiol.2004.01.009]
28. Barthelemy C, Royere D, Hammahah S, Lebos C, Tharanne MJ, Lansac J. Ultrastructural changes in membranes and acrosome of human sperm during cryopreservation. Arch Androl 1990; 25: 29-40. [DOI:10.3109/01485019008987591]
29. Krogenaes A, Andersen Berg K, Hafne AL, Engeland E. Membrane alterations in bull spermatozoa after freezing and thawing and after in vitro fertilization. Acta Vet Scand 1994; 35:17-26.
30. Hofmo PO, Andersen Berg K. Electron microscopical studies of membrane injuries in blue fox spermatozoa subjected to the process of freezing and thawing. Cryobiology 1989; 26: 124-131. [DOI:10.1016/0011-2240(89)90042-4]
| بازنشر اطلاعات | |
 |
این مقاله تحت شرایط Creative Commons Attribution-NonCommercial 4.0 International License قابل بازنشر است. |
