ABSTRACT
The kallikrein-like serine protease, prostate-specific antigen (PSA), is mixed in
human seminal plasma with its protein substrates semenogelin (Sg) -I, Sg-II, and protein
C inhibitor (PCI), which are produced in seminal vesicles. In the seminal plasma,
PSA degrades Sg-I, and Sg-II, which are major components in insoluble coagula, and
PCI inhibits PSA by forming a PSA-PCI complex. Digestion of seminal coagula with PSA
releases PCI and PSA-PCI complex from the coagula into a soluble phase, suggesting
the presence of active PCI within the coagula. PCI forms a ternary complex with PSA
and Sg-II in the seminal plasma. The binding of Sg-II to PSA and PCI is influenced
by pH, ionic strength, heparin, negatively charged dextran sulfate, divalent cations,
and particularly by Zn2 +. These observations suggest that binding of PCI to Sg in seminal vesicles regulates
the PSA-catalyzed degradation of Sg in seminal plasma; the complex formation among
PCI, PSA, and Sg is modulated by several factors in seminal plasma.
KEYWORDS
Protein C inhibitor - prostate-specific antigen - semenogelins - seminal plasma -
male reproduction
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Professor Koji SuzukiPh.D.
Mie University Graduate School of Medicine
Edobashi 2-174, Tsu-city, Mie, 514-8507, Japan
eMail: suzuki@doc.medic.mie-u.ac.jp