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Semenogelin I and semenogelin II, the major gel-forming proteins in human semen, are substrates for transglutaminase

In English

Författare

Summary, in English

The major seminal vesicle secreted proteins in human semen, semenogelin I and semenogelin II, interact non-covalently and via disulphide bridges to instantly form a coagulum upon ejaculation. The coagulum is liquefied after a few minutes due to the action of a prostatic serine protease, prostate-specific antigen (PSA). In contrast to rat semen, which forms an insoluble plug within minutes of expulsion, no transglutaminase-mediated cross-linking has been demonstrated in ejaculated human semen. However, we here show that semenogelin I and semenogelin II, both in seminal vesicle fluid and purified from semen, are substrates for factor XIIIa, the fibrin cross-linking transglutaminase. The cross-linking of the semenogelins, which was conformation-dependent, and the incorporation of a fluorescence-labelled amine, were visualised by SDS/PAGE and Western blot. Purified semenogelin I and semenogelin II could be cross-linked separately into complexes. Moreover, digestion of semenogelin with PSA produced fragments, some of which were cross-linked into complexes by factor XIIIa. We also found that PSA was unable to release any semenogelin fragments during exposure of the high molecular-mass complexes of cross-linked semenogelin to active PSA.

Publiceringsår

1998

Språk

Engelska

Sidor

21-216

Publikation/Tidskrift/Serie

Eur J Biochem

Volym

252

Issue

2

Dokumenttyp

Artikel i tidskrift

Förlag

Wiley-Blackwell

Ämne

  • Medicinal Chemistry

Nyckelord

  • Non-U.S. Gov't
  • Research Support
  • Recombinant Proteins/metabolism
  • Prostate-Specific Antigen/metabolism
  • Peptide Fragments/metabolism
  • Male
  • Humans
  • Gonadal Steroid Hormones/*metabolism
  • Fluorescent Dyes/metabolism
  • Dithiothreitol/pharmacology
  • Disulfides/metabolism
  • Cross-Linking Reagents/metabolism
  • Cadaverine/analogs & derivatives/metabolism
  • Calcium/pharmacology
  • Semen/*chemistry
  • *Seminal Vesicle Secretory Proteins
  • Solubility
  • Substrate Specificity
  • Transglutaminases/*metabolism
  • Urea/pharmacology

Status

Published

Forskningsgrupp

  • Clinical Chemistry, Malmö