Ferritin Overload Suppresses Male Fertility Via altered Acrosome Reaction
2015
Kwon, W.S., Department of Animal Science and Technology, Chung-Ang University, Anseong, Republic of Korea | Rahman, Md S., Department of Animal Science and Technology, Chung-Ang University, Anseong, Republic of Korea | Kim, Y.J., Department of Animal Science and Technology, Chung-Ang University, Anseong, Republic of Korea | Ryu, D.Y., Department of Animal Science and Technology, Chung-Ang University, Anseong, Republic of Korea | Kahtun, A., Department of Animal Science and Technology, Chung-Ang University, Anseong, Republic of Korea | Pang, M.G., Department of Animal Science and Technology, Chung-Ang University, Anseong, Republic of Korea
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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