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Published on: September 10, 2018
Eppin: an effective target for male contraception
M G O'Rand1, E E Widgren, Zengjun Wang
1Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. morand@unc.edu
Molecular and Cellular Endocrinology
|January 21, 2006
Summary
Epididymal protease inhibitor (Eppin) modulates semenogelin digestion by prostate-specific antigen (PSA). Antibodies targeting Eppin on sperm surfaces block semenogelin binding, impacting PSA activity.
Area of Science:
- Biochemistry
- Genetics
- Reproductive Biology
Background:
- Eppin (epididymal protease inhibitor) belongs to the WAP-type four-disulfide core (WFDC) gene family.
- This study focuses on Eppin and related genes in the Eppin cluster on human chromosome 20.
Purpose of the Study:
- To update information on Eppin and Eppin-like genes.
- To investigate the structural characteristics of Eppin.
- To explore the interaction of Eppin with human spermatozoa and semenogelin.
Main Methods:
- Virtual structural modeling of Eppin protein.
- Analysis of Eppin's interaction with human spermatozoa.
- Investigating the effect of Eppin on semenogelin digestion by prostate-specific antigen (PSA).
- Utilizing antibodies against Eppin to probe its function.
Main Results:
- Eppin's C-terminal shows homology to Kunitz-type trypsin inhibitors, while the N-terminal may resemble defensins.
- Human spermatozoa possess a receptor for Eppin.
- Eppin binding to semenogelin modulates PSA-mediated digestion.
- Antibodies against Eppin's C-terminal block PSA activity modulation.
Conclusions:
- Eppin plays a role in regulating semenogelin breakdown by PSA.
- Antibodies binding to Eppin on sperm surface inhibit semenogelin binding, suggesting a mechanism for PSA activity modulation.
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