The Effect Of The Phosphorylation Of Sp32and Heat Shock Protein On The Activation Of Acrosome Protein In Boar Sperm

Tyrosine phosphorylation of proteins in sperm shows regional distribution, and head construction of sperm is highly polarized, not only the tyrosine phosphorylation of acrosin related to the acrosomal reaction during capacitation, but also is closely related to sperm-egg binding which made sperm tthrough the transparent tape. Tyrosine phosphorylation of proteins plays an important role in capacitation, acrosome reaction and activation movement in sperm, which is regarded as an important symbol of capacitation. There is a kind of highly conserved protein that the molecular weight is about32000at boar acrosome. This kind of mammalian proteins is translated and modified from its precursor,the molecular weight of precursor is61000. Because of its specific combination with acrosin raw (also called proacrosin) and intermediates of acrosome, then transformed both into acrosin, it is called sperm protein32(sp32).To investigate the mechanism of capacitation like sperm cann’ treally capacitation, this rearch explored the effect of different treatments on the phosphorytyrsine that temperature dependency and sp32, the eight groups were fresh semen sperm, frozen-thawed sperm, capacitation sperm, the early acrosome reaction sperm, non-capacitation medium of cold shock, non-capacitation medium of cold shock for rewarming, capaci tation medium of cold shock, capacitation medium of cold shock for rewarming. Commassie Blue Staining and the detection of boar sperm were used, acrosin was extracted and analysed by SDS-PAGE and Western blot.The results are as follows:1. The expression level of sp32in the early acrosome reaction sperm was the highest (fresh semen sperm, capacitation sperm, thawed sperm, the early acrosome reaction sperm), followed by capacitation sperm, frozen-thawed sperm and fresh semen sperm;2. The expression extent of sp32, sp38tyrosine phosphorylation would be up regulation with the activation of boar sperm;3. The expression of sp38, sp40and sp53presented some particularity due to sperm cryopreservation by cold shock during tyrosine phosphorylation of acrosin. Sperm motility would increase when there were more low molecular weight during tyrosine phosphorylation of acrosin;4. A higher expression level of tyrosine phosphorylation sp35in frozen-thawed sperm was closely related with the mechanism of sperm cryopreservation.In conclusion, the expression level of tyrosine phosphorylation protein in boar acrosome presented certain regularity, which would provide theoretical reference for the follow-up text of spern actication and cold shock, especially play a role in sperm cold shock and cryopreservation. In addation, this study may have certain significance for the preservation and breeding of other precious special economic animals.