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

Sappino, N.
Velardi, A.
Erno, H.
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Published in EMBO journal. 1993, vol. 12, no. 5, p. 1871-1878
Abstract 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.
Keywords Amyloid beta-Protein PrecursorAnimalsBase SequenceCarrier Proteins/genetics/ secretionCells, CulturedDnaFemaleHumansMaleMiceMolecular Sequence DataPlasminogen Inactivators/genetics/ secretionRNA, Messenger/geneticsRatsReceptors, Cell SurfaceSeminal Vesicles/ secretionSequence Homology, Nucleic AcidSerpins/ secretionTestosterone/physiologyTumor Cells, CulturedUrokinase-Type Plasminogen Activator/antagonists & inhibitors
PMID: 8491179
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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. https://archive-ouverte.unige.ch/unige:9070

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Deposited on : 2010-07-12

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