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자료유형
학술저널
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Kwon, Woo-Sung (Department of Animal Science and Technology, Chung-Ang University) Rahman, Md Saidur (Department of Animal Science and Technology, Chung-Ang University) Kim, Ye-Ji (Department of Animal Science and Technology, Chung-Ang University) Ryu, Do-Yeol (Department of Animal Science and Technology, Chung-Ang University) Kahtun, Amena (Department of Animal Science and Technology, Chung-Ang University) Pang, Myung-Geol (Department of Animal Science and Technology, Chung-Ang University)
저널정보
한국동물번식학회 한국동물번식학회지 한국동물번식학회지 제39권 제4호
발행연도
2015.1
수록면
117 - 125 (9page)

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Iron is required for cell viability but is toxic in excess. While the iron-mediated malfunction of testicular cells is well appreciated, the underlying mechanism(s) of this effect and its relationship with fertility are poorly understood. Ferritin is a ubiquitous intracellular protein that controls iron storage, ferroxidase activity, immune response, and stress response in cells. Ferritin light chain protein (FTL) is the light subunit of the Ferritin. Previously, we had identified the FTL in bovine spermatozoa following capacitation. In present study, to investigate the role of Ferritin in sperm function, mice spermatozoa were incubated with multiple doses (1, 10 and $100{\mu}M$) of sodium nitroprusside (SNP), an iron donor. SNP was increased Ferritin levels in a dose-dependent manner. The Ferritin was detected on the acrosome in spermatozoa by immunocytochemistry. Short-term exposure of spermatozoa to SNP increased tyrosine phosphorylation and the acrosome reaction (AR). Finally, SNP affected a significant decrease in the rate of fertilization as well as blastocyst formation during early embryonic development. On the basis of these results, we propose that the effects of Ferritin on the AR may reduce overall sperm function leads to poor fertility in males and compromised embryonic development.

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