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A locus on chromosome 20 encompassing genes that are highly expressed in the epididymis

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Author

Summary, in English

During liquefaction of the ejaculate, the semen coagulum proteins semenogelin I (SEMG1) and semenogelin II (SEMG2) are degraded to low molecular mass fragments by kallikrein-related peptidase 3 (KLK3), also known as prostate-specific antigen. Semenogelin molecules initiate their own destruction by chelating Zn2+ that normally would completely inhibit the proteolytic activity of KLK3. In a similar way, semenogelins might regulate the activity of kallikrein-related peptidases in the epididymis, something that might be of importance for the maturation of spermatozoa or generation of anti-bacterial peptides. Studies on the evolution of semen coagulum proteins have revealed that most of them carry an exon that displays a rapid and unusual evolution. As a consequence, homologous proteins in rodents and primates show almost no conservation in primary structure. Further studies on their evolution suggest that the progenitor of the semen coagulum proteins probably was a protease inhibitor that might have displayed antimicrobial activity. The semenogelin locus on chromosome 20 contains at least 17 homologous genes encoding probable protease inhibitors with homology to semen coagulum proteins. All of these are highly expressed in the epididymis where they, similar to the semenogelins, could affect the maturation of spermatozoa or display antibacterial properties.

Publishing year

2007

Language

English

Pages

540-544

Publication/Series

Asian Journal of Andrology

Volume

9

Issue

4

Document type

Journal article review

Publisher

Nature Publishing Group

Topic

  • Medicinal Chemistry

Keywords

  • proteolysis
  • kunitz
  • antimicrobial
  • semenogelin
  • inhibitor
  • semen
  • whey acidic protein four disulphide core
  • zinc

Status

Published

Research group

  • Clinical Chemistry, Malmö

ISBN/ISSN/Other

  • ISSN: 1008-682X