Human seminal vesicle-specific antigen is a substrate for prostate-specific antigen (or P-30).

Human seminal vesicle and prostatic fluids were obtained separately and reconstituted in vitro to test the hypothesis that proteolytic enzymes of prostatic origin would degrade seminal vesicle-specific antigen (SVSA). Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblot analysis to follow the fate of SVSA over time, we found that upon mixing the two secretions, SVSA was converted to forms of intermediate and low molecular weight identical to transformations seen in normal liquefied ejaculates. Diisoproprylfluorophophate, a serine protease inhibitor, prevented this degradation, indicating serine protease involvement in the proteolysis of SVSA. Prostate-specific antigen (PSA; also known as P-30), recently identified as a serine protease, was examined for its ability to mimic the effects of prostatic fluid on SVSA. Purified PSA catalyzed degradation of SVSA to produce proteolytic fragments that comigrated and were immunologically related to SVSA fragments produced by prostatic fluid. Purified PSA in the presence of serine protease inhibitors was unable to degrade SVSA. These results demonstrate that SVSA is a substrate for PSA during human semen liquefaction.