한국동물생명공학회지 (Journal of Animal Reproduction and Biotechnology)

  • 제34권3호
  • /
  • Pages.247-252
  • /
  • 2019
  • /
  • 2671-4639(pISSN)
  • /
  • 2671-4663(eISSN)
한국동물생명공학회 (The Korean Society of Animal Reproduction and Biotechnology)
권호 표지
DOI QR코드

DOI QR Code

동결융해 후 토끼 정자의 Matrix Metalloproteinases (MMPs)와 Their Tissue Inhibitors (TIMPs) 발현 양상

Expression of Matrix Metalloproteinases (MMPs) and Their Tissue Inhibitors (TIMPs) in Frozen Sperm of Rabbit

  • Kim, Sang Hwan (Institute of Genetic Engineering, Hankyong National University) ;
  • Choi, Hwa Sik (Department of Biomedial Laboratory Science, Shinan University) ;
  • Yoon, Jong Taek (Institute of Genetic Engineering, Hankyong National University)
  • 투고 : 2019.09.16
  • 심사 : 2019.09.23
  • 발행 : 2019.09.30
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

We observed MMPs expression in all sperm groups, with pro-MMP showing lower expression than active MMPs. According to the results from each freezing extender, the sperm membrane integrity (HOST: Hypoosmotic Swelling Test) analysis in TCGGD (Tris 250 mM, Citric acid 88 mM, Glucose 47 mM, Glycerol 3%, Dimethylsulpoxide 3.5 M) is 59.8 ± 0.7, TCGSD (Tris 250 mM, Citric acid 88 mM, Glucose 47 mM, Sucrose 0.1 M, Dimethylsulpoxide 3.5 M) is 59.3 ± 0.5 were significantly higher (p < 0.05) among the experimental groups. And MMPs analysis result, we observed MMPs expression in all sperm groups, with pro-MMP showing lower expression than active MMPs. The expression of active MMP-2 was the highest in sperms frozen in TCGSD and TCGD (Tris 250 mM, Citric acid 88 mM, Glucose 47 mM, Dimethylsulpoxide 3.5 M), Meanwhile, sperms from the TCGGD and TCGED (Tris 250 mM, Citric acid 88 mM, Glucose 47 mM, Ethylene glycol 3%, Dimethylsulpoxide 3.5 M) group showed lower level of active MMP-2 expression. Together, these results indicate that adding glycerol or sucrose to the sperm freezing buffer would not only suppress MMPs expression but also minimize DNA fragmentation, providing a mean to improve the success rate in the in vitro manipulation of rabbit sperms. Therefore, these results suggest that TCGGD or TCGSD extender method for freezing-thawing of rabbit sperm increased the viability after thawing.

키워드

참고문헌

  1. Arriola J. 1982. Interaction if formaldehyde and of sodium and triethanolamine lauryl surfate on the motility and fertilizing ability of rabbit and bull spermatozoa frozen in the egg yolk and milk extender. Ph.D.Thesis, Cornell University, Ithaca, New York.
  2. Ashida K, Nakatsukasa H, Higashi T, Ohguchi S, Hino N, Nouso K, Urabe Y, Yoshida K, Kinugasa N, Tsuji T. 1996. Cellular distribution of 92-kd type IV collagenase/gelatinase B in human hepatocellular carcinoma. Am. J. Pathol. 1803-1811.
  3. Cortell C, Viudes de Castro MP. 2008. Effect of gelatin addition to freezing extender on rabbit semen parameters and reproductive performance. In: Xiccato, G. (Ed.), 9th World Rabbit Congress. 327-332.
  4. Foote RH, Carney EW. 2000. The rabbit as a model for reproductive and developmental toxicity studies. Reprod. Toxicol. 14:477-493. https://doi.org/10.1016/S0890-6238(00)00101-5
  5. Gotze VG, Paufler S. 1976. Fertility results and prenatal mortality following artificial insemination with fresh and deep frozen semen in rabbits after normal induction of ovulation and superovulation. Zuchthyg. 11:169-174. https://doi.org/10.1111/j.1439-0531.1976.tb00322.x
  6. Gunnarsson M, Lecander I, Abrahamsson PA. 1995. Factors of the plasminogen activator system in human testis., as demonstrated by in-situ hybridization and immunohistochemistry. Mol. Hum. Reprod. 5:934-940. https://doi.org/10.1093/molehr/5.10.934
  7. Hammerstedt RH, Graham JK. 1992. Cryopreservation of poultry sperm: The enigma of glycerol. Cryobiology. 29:26-38. https://doi.org/10.1016/0011-2240(92)90004-L
  8. Hanada A, Nagase H. 1980. Cryoprotective effects of some amides on the rabbit spermatozoa. J. Reprod. Fertil. 60:247-252. https://doi.org/10.1530/jrf.0.0600247
  9. Huarte J, Belin D, Bosco D, Sappino AP, Vassalli JD. 1987. Plasminogen activator and mouse spermatozoa : urokinase synthesis in the male genital tract and binding of the enzyme to the sperm cell surface. J. Cell. Biol. 104:1281-1289. https://doi.org/10.1083/jcb.104.5.1281
  10. Hudson BG, Reeders ST, Tryggvason K. 1993. Type IV collagen : structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis. J. Bio. Chem. 26033-26036.
  11. Jeyendran RS, Van der Ven HK, Perez-Palaez M, Crabo BG, Zaneveld LJ. 1984. Development of an assay to asses the functional interity of the human sperm membrane and its relationship to other semen characteristics. J. Reprod. Fertil. 70:219-228. https://doi.org/10.1530/jrf.0.0700219
  12. Kim SH, Min KS, Kim NH, Yoon JT. 2012. Differential expression of programmed cell death on the follicular development in normal and miniature pig ovary. PLoS One.;7(10):e46194. doi: 10.1371/journal.pone.0046194.
  13. Larson JL, Miller DJ. 1999. Simple histochemical stain foracrosomes on sperm on sperm from several species. Mol. Reprod. Dev. 52:445-449. https://doi.org/10.1002/(SICI)1098-2795(199904)52:4<445::AID-MRD14>3.0.CO;2-6
  14. Longin J, Guillaumot P, Chauvin MA, Morera AM, Le Magueresse-Battistoni B. 2001. MT1-MMP in rat testicular development and the control of Sertoli cell proMMP-2 activation. J. Cell. Sci. 114:2125-2134. https://doi.org/10.1242/jcs.114.11.2125
  15. Longin J, Le Magueresse-Battistoni B. 2002. Evidence that MMP-2 and TIMP-2 are at play in the FSH-induced changes in Sertoli cells. Mol. Cell. Endocrinol. 189:25-35. https://doi.org/10.1016/S0303-7207(01)00756-0
  16. Michelle KYSIU, Will M, Lee C, Yan C. 2002. The interplay of collagen IV, tumor necrosis factor-gelatinase B (Matrix Metalloprotease-9), and tissue inhibitor of metalloproteases-1 in the basal lamina regulates sertoli cell-tight junction dynamics in the rat testis. Endocrinology. 144(1):371-387.
  17. Orit BS, Zaki K, Yael G, Shlomit G. 2002. Presence of Matrix Metalloproteinases and Tissue Inhibitor of Matrix Metalloproteinase in Human Sperm. J. Androl. 23(5):702-708.
  18. O'Shea T, Wales RG. 1969. Further studies of the deep freezing of rabbit spermatozoa in reconstituted skim milk powder. Aust. J. Biol. Sci. 22:709-719. https://doi.org/10.1071/bi9690709
  19. Polgar ZS, Virag GY, Baranyai B, Bodo SZ, Kovacs A, Gocza E. 2004. Evaluation of effects of cryopreservation on rabbit spermatozoa membranes with trypan blue-Giemsa staining. In: Becerril, Pro, A. (Eds.), 8th World Rabbit Congress. World Rabbit Sci. 322-329.
  20. Polge C, Smith AU and Parkes AS. 1949. Revival of spermatozoa after vitrification and dehydration at low temperatures. Nature. 164:666. https://doi.org/10.1038/164666a0
  21. Robinson LL, Sznajder NA, Riley SC, Anderson RA. 2001. Matrix metalloproteinases and tissue inhibitors of metalloprotein ases in human fetal testis and ovary. Mol. Hum. Reprod. 7:641-648. https://doi.org/10.1093/molehr/7.7.641
  22. Sawanda Y and Chang MC. 1964. Motility and fertilizing capacity of rabbit spermatozoa after freezing in a medium containing dimethyl sulfoxide. Fertil. Steril. 15:222-229. https://doi.org/10.1016/s0015-0282(16)35171-8
  23. Slongo ML, Zampieri M, Onisto M. 2002. Expression of matrix metalloproteases (MMP-2, MT1-MMP) and their tissue inhibitor (TIMP-2) by rat Sertoli cells in culture: implications for spermatogenesis. Biol. Chem. 383:235-239. https://doi.org/10.1515/BC.2002.025
  24. Sternlicht MD, Werb Z. 2001. How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell. Dev. Biol. 17:463-516. https://doi.org/10.1146/annurev.cellbio.17.1.463
  25. Theau M, Roustan A. 1982. Etude des possibilites de dilution du sperme de lapin congele pour l'insemination artificielle. 3emes Journees de la Recherche cunicole. 8-9.
  26. Watson PF. 2000. The causes of reduced fertility with cryopreserved semen. Anim. Reprod. Sci. 60:481-492. https://doi.org/10.1016/S0378-4320(00)00099-3
  27. Yamagata K, Murayama K, Okabe M, Toshimori K, Nakanishi T, Kashiwabara S, Baba T. 1998. Acrosin accelerates the dispersal of sperm acrosomal proteins during acrosome reaction. J. Biol. Chem. 273:10470-10474. https://doi.org/10.1074/jbc.273.17.10470
  28. 김상환, 강현아, 이명섭, 서강섭, 윤종택. 2012. Effect of TES Extender on Sperm Characteristics and Viability of Frozen Semen in Miniature Pig. 한국수정란이식학회. 27:45-50.