Abstract
Human seminal plasma spontaneously coagulates after ejaculation. The major component of this coagulum is semenogelin I, a 52-kDa protein expressed exclusively in the seminal vesicles. Recently, a sperm motility inhibitor has been found to be identical to semenogelin II suggesting that it may also be a physiological sperm motility inhibitor. The protein is rapidly cleaved after ejaculation by the chymotrypsin-like prostatic protease prostate-specific antigen, resulting in liquefaction of the semen coagulum and the progressive release of motile spermatozoa. Some of the cleavage products of Sg I may also have various biological functions. While the semenogelin I protein is unique to human and higher primates, it has recently been shown to belong to a gene family having a similar gene structure but encoding widely differing proteins. The recently elucidated characteristics of the semenogelin I gene as well as the biochemical and functional properties of the encoded protein are reviewed, and an attempt is made to integrate the various findings into a model for semen coagulation, sperm immobilization and potential other functions.
Original language | English |
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Pages (from-to) | 944-960 |
Number of pages | 17 |
Journal | Cellular and Molecular Life Sciences |
Volume | 55 |
Issue number | 6-7 |
Publication status | Published - 1999 Jul 12 |
Externally published | Yes |
Keywords
- Inhibin-like peptides
- Prostate-specific antigen
- REST gene
- Seminal plasma
- Seminal vesicle-specific antigen
- Sperm hyaluronidase
- Sperm motility inhibitor
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology
- Pharmacology
- Cellular and Molecular Neuroscience
- Cell Biology