Scientific article

Protease-nexin I as an androgen-dependent secretory product of the murine seminal vesicle

Published inEMBO journal, vol. 12, no. 5, p. 1871-1878
Publication date1993

A search for inhibitors of urokinase-type plasminogen activator (uPA) in the male and female murine genital tracts revealed high levels of a uPA ligand in the seminal vesicle. This ligand is functionally, biochemically and immunologically indistinguishable from protease-nexin I (PN-I), a serpin ligand of thrombin and uPA previously detected only in mesenchymal cells and astrocytes. A survey of murine tissues indicates that PN-I mRNA is most abundant in seminal vesicles, where it represents 0.2-0.4% of the mRNAs. PN-I is synthesized in the epithelium of the seminal vesicle, as determined by in situ hybridization, and is secreted in the lumen of the gland. PN-I levels are much lower in immature animals, and strongly decreased upon castration. Testosterone treatment of castrated males rapidly restores PN-I mRNA levels, indicating that PN-I gene expression is under androgen control.

  • Amyloid beta-Protein Precursor
  • Animals
  • Base Sequence
  • Carrier Proteins/genetics/ secretion
  • Cells, Cultured
  • Dna
  • Female
  • Humans
  • Male
  • Mice
  • Molecular Sequence Data
  • Plasminogen Inactivators/genetics/ secretion
  • RNA, Messenger/genetics
  • Rats
  • Receptors, Cell Surface
  • Seminal Vesicles/ secretion
  • Sequence Homology, Nucleic Acid
  • Serpins/ secretion
  • Testosterone/physiology
  • Tumor Cells, Cultured
  • Urokinase-Type Plasminogen Activator/antagonists & inhibitors
Citation (ISO format)
VASSALLI, Jean-Dominique et al. Protease-nexin I as an androgen-dependent secretory product of the murine seminal vesicle. In: EMBO journal, 1993, vol. 12, n° 5, p. 1871–1878.
Main files (1)
ISSN of the journal0261-4189

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