A TRH-like peptide, fertilization-promoting peptide (FPP), is present in high concentrations in mammalian prostate and semen and enhances the fertilization potential of spermatozoa. In this study, we have examined the properties of the enzyme that degrades TRH and FPP in rabbit seminal plasma. The enzyme responsible had a pH optimum of approximately 7·0, was inhibited by serine (di-isopropyl flurophosphate) and thiol (N-ethylmaleimide) protease inhibitors, bacitracin and concentrations of Zn2+ naturally present in seminal plasma: these functional reagents are all known to be potent inhibitors of prolyl endopeptidase. The major product after incubation of [3H]TRH in seminal plasma for 100 min was acid TRH (deamidated TRH) which is also the product after incubation of TRH with prolyl endopeptidase. Our results are consistent with the enzyme responsible for degradation of TRH and FPP in seminal plasma being similar to prolyl endopeptidase. The enzyme identified in this study is secreted and is therefore likely to be different from prolyl endopeptidase characterized from porcine brain, because the latter enzyme is known to be located in the cytosolic compartment of the cell.
Journal of Endocrinology (1995) 144, 61–66
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