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During the capacitation process, spermatozoa acquire the ability to fertilize an oocyte, and upregulation of cAMP-dependent protein tyrosine phosphorylation occurs. Recently, Src family tyrosine kinase (SFK) has been involved in spermatozoa capacitation as a key PKA-dependent tyrosine kinase in several species. This work investigates the expression and role of SFK in porcine spermatozoa. SFK members Lyn and Yes are identified in porcine spermatozoa by western blotting as well as two proteins named SFK1 and SFK2 were also detected by their tyrosine 416 phosphorylation, a key residue for SFK activation. Spermatozoa with SFK1 and SFK2 increase their Y416 phosphorylation time-dependently under capacitating conditions compared with noncapacitating conditions. The specific SFK inhibitor SU6656 unaffected porcine spermatozoa motility or viability. Moreover, SFK inhibition in spermatozoa under capacitating conditions leads to a twofold increase in both nonstimulated and calcium-induced acrosome reaction. Our data show that capacitating conditions lead to a time-dependent increase in actin polymerization in boar spermatozoa and that long-term incubation with SFK inhibitor causes a reduction in the F-actin content. In summary, this work shows that the SFK members Lyn and Yes are expressed in porcine spermatozoa and that SFK1 and SFK2 are phosphorylated (activated) during capacitation. Our results point out the important role exerted by SFK in the acrosome reaction, likely mediated in part by its involvement in the actin polymerization process that accompanies capacitation, and rule out its involvement in porcine spermatozoa motility.

Src family tyrosine kinase regulates acrosome reaction but not motility in porcine spermatozoa