Keywords

Sp32, Preacrosomal Protein, Acrosome Protein, Activation, Tyrosine Phosphorylation

Abstract

? In order to explore the relationship between the expression of pig sperm protein 32 (sp32) and the regulation of tyrosine phosphorylation on the activation of pig sperm acrosome protein, this study conducted experiments on pigs treated with different treatments (fresh sperm, freeze-thaw, capacitation, and acrosome reaction). Sperm acrosome membrane proteins were separated, detected and analyzed by Coomassie brilliant blue staining, sds-page electrophoresis and western blot. The results show that after porcine sperm undergoes capacitation, freezing-thawing and acrosome reaction, the expression of sp32 is different during the transformation process of proacrosin and acrosin, and capacitation and acrosin are different. The expression level of sp32 in the somatic reaction treatment group was slightly higher than that in the freeze-thaw treatment group, but significantly higher than that in the fresh semen treatment group. Compared with other treatment groups, the frozen-thawed sperm treatment group produced significant differences in sp32 tyrosine phosphorylation levels. However, in sds-page electrophoresis, the protein expression bands in the protein molecular weight range of 38 to 170 ku in the pig fresh semen treatment group were more obvious than those in other comparison groups, which indicates the capacitation and acrosome reaction processes that pig sperm must undergo before fertilization. , acrosome membrane proteins accompany protein modification and degradation of macromolecules. Conclusion: As a preacrosomal protein-binding protein, sp32¡¯s expression level and tyrosine phosphorylation level are increased during the activation of preacrosomal protein.

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Original research done by Sun Peiliang, Cui Mingxun, Jiang Yuanyuan, Cao Lipeng, Jin Yi

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