Semenogelin, the main protein of the human semen coagulum, regulates sperm function.

Semenogelin (Sg), the main component of the human semen coagulum, is an important and versatile protein acting on several sperm parameters, both as intact or degraded Sg. Sg originates mostly from seminal vesicle and probably is responsible for sperm immobilization in the seminal coagulum. Purified Sg can be cross-linked by transglutaminase or phosphorylated by kinases, but the actual occurrence of these reactions in reproductive physiology is not clear. Experimental evidence demonstrates that prostate-specific antigen (PSA) rapidly cleaves Sg, an event temporally associated with semen liquefaction and initiation of sperm motility. Sg and its degradation peptides participate in various processes including Zn +2 shuttling, antibacterial activity, hyaluronidase activation, and so on. Sg inhibits sperm motility at the concentration found in the coagulum, but the rapid processing by PSA allows initiation of movement. The mechanism of Sg action and its targets are not known, but improper Sg degradation decreases fertility. Sg and its degradation peptides block sperm capacitation and associated events at concentrations much lower than those of seminal plasma and could play important role in preventing premature capacitation. The effects of Sg are dependent on time and proteolysis due to PSA, and any imbalance may affect sperm physiology and fertility.