Cui J J, Tian Y, Liu Y, Huang H L, Jin Y
Agricultural College of Yanbian University, Yanji, Jinlin, China.
Agricultural College of Yanbian University, Yanji, Jinlin, China
Genet Mol Res. 2014 Nov 27;13(4):9915-20. doi: 10.4238/2014.November.27.20.
The main objective of the current study was to explore the different activation mechanisms of capacitation and freeze-thawed spermatozoa. Using SDS-PAGE and Western blotting, the conversion process of boar proacrosin during freeze-thawing and capacitation of spermatozoa was analyzed. The results revealed that capacitated spermatozoa exhibited a greater fluorescence area than that of the freeze-thawed spermatozoa, which were smaller than those of the fresh group. Fresh spermatozoa displayed 45- and 35- kDa protein bands, while those of freeze-thawed andcapacitated spermatozoa displayed 45-, 35- and 28-kDa bands. In summary, these data indicate that proacrosin is activated, thus becoming α- and β-acrosins and a 28-kDa protein during capacitation and freeze-thawing.
本研究的主要目的是探索精子获能和冻融精子的不同激活机制。利用SDS-PAGE和蛋白质免疫印迹法，分析了公猪前顶体蛋白酶在精子冻融和获能过程中的转化过程。结果显示，获能精子的荧光面积比冻融精子大，而冻融精子的荧光面积又小于新鲜组精子。新鲜精子呈现出45 kDa和35 kDa的蛋白条带，而冻融精子和获能精子则呈现出45 kDa、35 kDa和28 kDa的条带。总之，这些数据表明前顶体蛋白酶在获能和冻融过程中被激活，从而转变为α-和β-顶体蛋白酶以及一种28 kDa的蛋白质。
