The rapid rise of proteomics has been driven by technological developments in high-throughput mass spectrometry that make protein sequencing feasible at a scale not remotely possible only a decade ago. Coupled with enhanced methods for protein prefractionation, such developments have enabled characterization of complex proteomes from various cell types, including the spermatozoa of a number of species. These studies have generated inventories consisting of thousands of sperm proteins and paved the way for significant advances that will now be driven by parallel improvements in our capacity to turn these protein inventories into meaningful functional insights. Specifically, there is a need to quantitatively compare proteomic profiles from spermatozoa in different functional states (immature vs. mature, uncapacitated vs. capacitated, fertile vs. infertile). Such comparisons will enable us to define which specific elements of the proteome are of functional significance and understand the cascade of posttranslational modifications (e.g., phosphorylation, glycosylation, proteolytic cleavage) involved in generating a functional spermatozoon. This fundamental information will then create a basis for identifying key points in the posttesticular maturation of spermatozoa that might be targeted for contraceptive purposes or implicated in the defective sperm function observed in a significant proportion of infertile males.
Immune Infertility: The Impact of Immune Reactions on Human Infertility p. 3-12