The protein tyrosine phosphorylation during in vitro capacitation and cryopreservation of mammalian spermatozoa.

Before the process of fertilization, spermatozoa necessitate a period of residence in the female reproductive environment, and undergo a sequence of physiological and biochemical changes collectively referred to as capacitation. Accumulated evidences from several laboratories indicated that the protein tyrosine phosphorylation (PTP) is one of the most important intracellular signaling events regulating sperm function, and is a meaningful indicator of capacitation. Different factors that affect PTP are cholesterol efflux, influx of HCO3(-), increased intracellular Ca(2+), cAMP and reactive oxygen species (ROS). cAMP/PKA and extracellular signal regulated kinases (ERKs) are the known important signaling pathways primarily involved in PTP. Advanced proteomics approaches have revealed several proteins that undergo tyrosine phosphorylation during capacitation. Semen cryopreservation subjects spermatozoa to frequent stressors, which result in capacitation like changes (cryo-capacitation). The cryo-capacitated spermatozoa usually show different patterns of PTP than the normal in vitro capacitated spermatozoa. In the current manuscript, we have summarized some information about the proteins undergoing tyrosine phosphorylation during capacitation and the effect of cryopreservation on PTP as well as the possibilities to reduce the changes associated with cryopreservation process.