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Related Experiment Videos

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
PubMed
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.

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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.

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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.