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대한생식의학회지 제25권 제3호 2010년
돼지정자의 수정능력과 Reactive Oxygen Species의 관계분석 : I. Xanthine과 Xanthine Oxidase에 의한 정자의 전배양
강원대학교 축산대학, *세화산부인과 불임크리닉
박춘근, 정희태, 김종흥, 이상찬, 양부근, 김정익,
Analysis of Relationship Between Spermatozoa Ability and Reactive Oxygen Species in Porcine : I. Sperm Preincubation by Xanthine and Xanthine Oxidase
Park ck, Cheong ht, Kim jh, Lee sc, Yang bk, Kim ci
본 연구는 xanthine과 xanthine oxidase가 첨가된 배양액내에서 전배양된 돼지동결정액의 수정능력에 있어서 catalase의 영향을 검토하였다. 체외수정을 위한 기본 배양액내에서 0 또는 30분간 전배양한 정자는 catalase를 첨가(40 및 15%)한 경우 보다는 무첨가(66 및 38%)시 유의적으로 높은 정자침입율을 나타냈지만(P<0.05), 배양액내에 xanthine을 첨가해 정자를 0, 30 및 60분간 전배양했을 때에는 catalase 무첨가(33, 41 및 19%) 보다는 첨가시(68, 70 및 49%) 유의적으로 높은 정자침입율이 인정되었다(P<0.05). 그러나 xanthine oxidase를 첨가하여 정자의 전배양을 행하지 않은 경우는 catalase의 첨가(13%) 보다는 무첨가(51%)시 유의적으로 높은 정자침입율을 나타냈지만(P<0.01), 전배양(30 및 60분)후에는 catalase의 존재유무와 정자전배양시간에 관계없이 매우 낮은 정자침입율 (10-21%)을 나타냈다. xanthine과 xanthine oxidase를 동시에 첨가하여 0, 30 및 60분간 정자를 전배양한 경우 catalase의 무첨가(14, 4 및 8%)보다 첨가(75, 55 및 52%)시 유의적으로 높은 정자침입율을 나타냈다(P<0.001). 한편, 다정자침입율은 xanthine, xanthine+xanthine oxidase의 첨가시 정자전배양기간이 길어짐에 따라 감소하였으며, catalase의 첨가보다는 무첨가시 낮은 다정자침입율을 나타냈다. 본 연구의 결과로부터 xanthine과 xanthine oxidase를 동시에 첨가시 catalase의 존재는 정자의 전배양후에도 다정자침입을 억제하면서 수정능력의 유지를 위해 매우 효과적인 것으로 추측되었다.
Spermatozoa acquire the ability to successfully fertilize the oocyte during their transit in the female genital tract. Thus the female reproductive tract must be responsible for supporting motility to extend the fertile life span of sperm in the female reproductive tract by secreting motility factor(s) and/or by reducing sperm metabolism in certain locations to allow better survial. The spermatozoa, like all cells living under aerobic conditions, constantly faces the oxygen paradox. Oxygen is clearly required to support life, but its metabolites modify cell functions and/or can endanger cell survival. The generation of reactive oxygen species in sperm preparations became a real concern because of the toxic effects they have at high concentrations on sperm functions, and of their possible involvment in made idopathic infertility. Reactive oxygen species producrion in semen has been associated with loss of motility, decreased capacity for sperm-oocyte fusion and loss of fertility (Aitken et al., 1991). High concentrations of reactive oxygen species produced by spermatozoa themselves (Aitken & Clarkson, 1987 ; Alvarez et al., 1987) or by the combinations of xanthine plus xanthine oxidase (Aitken et al., 1993) induce the formation of toxic lipid peroxides (Windsor et al., 1993) and compromise sperm viability. Reactive oxygen species also effect the sperm axoneme as a result of ATP depletion (De Lamirand and Gagnon, 1992), inhibit mitochondrial functions, and synthesis of DNA, RNA and proteins (Comporti, 1989), produce cytoskeletal modifications (Hindshaw et al., 1986) and inhibit sperm-oocyte fusion (Aitken et al., 1993). However, the spermatozoa have enzymatic defence systems such as superoxide dismutase, glutathione peroxidas/reductase and catalase (Griveau et al., 1995) to counteract the toxic effects induced by reactive oxygen species. Although correlations have been reported between the effectiveness of reactive oxygen species and the duration of sperm motility (Alvarez & Storey, 1989 ; De Lamirande & Gagnon, 1997), the importance of their action in vitro has not been fully elucidated. It is known that fresh sperm have higher fertilization potential than frozen-thaw sperm (Hunter, 1990) and a lower survival rate is possibly the principle explanation for the reduced capacity. Polyspermy refers to the penetration of more than one spermatozoon into the cytoplasm of oocytes (Hunter, 1991), which can result in a polyploid zygote, a condition that results in abnormal embryonic development (Birkhead et al., 1993). Therefore, the present study was undertaken to determine the whether incubation of frozen-thawed boar sperm with xanthine and/or xanthine oxidase in medium with or without catalase would allow in vitro fertilization.
키워드 : catalase, porcine IVF, sperm preincubation, xanthine, xanthine oxidase
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