Insulin-like growth factor binding protein-3 (IGFBP-3), the major serum carrier protein for the IGFs, is absent from Western ligand blots of seminal plasma, but is detectable by RIA. IGFBP-3 protease activity has recently been described in pregnancy serum. We investigated the possibility that seminal plasma contains an IGFBP-3 protease, by incubating seminal plasma with 125I-labeled human IGFBP-3. Seminal plasma was found to have potent IGFBP-3 protease activity with a cleavage pattern different from that of pregnancy serum. Prostate-specific antigen (PSA) is a serine protease found in semen. Autonidi-ographs measuring IGFBP-3 protease activity demonstrated that purified PSA cleaved IGFBP-3. yielding a cleavage pattern identical to that of seminal plasma. IGFBP-2 and -4 in seminal plasma were not degraded by PSA. Cleavage of IGFBP-3 by PSA resulted in a marked reduction in the binding affinity of the fragments to IGF-I, but not IGF-II. We speculate that PSA may serve to modulate IGF function within the reproductive system or in prostate cancer bv altering IGF IGFBP-3 interactions.
|Original language||English (US)|
|Number of pages||8|
|Journal||Journal of Clinical Endocrinology and Metabolism|
|Publication status||Published - 1992|
ASJC Scopus subject areas
- Endocrinology, Diabetes and Metabolism