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Protease nexin-1 complexes and inhibits T cell serine proteinase-1

D Gurwitz1, M M Simon, U Fruth

  • 1Department of Microbiology and Molecular Genetics, College of Medicine, University of California, Irvine 92717.

Insights

Protease nexin-1 (PN-1) irreversibly inhibits T cell serine proteinase-1 (TSP-1), a key player in cytotoxic T cell killing. PN-1 effectively complexes and inhibits both subunits of the TSP-1 homodimer.

Area of Science:

  • Biochemistry
  • Immunology

Background:

  • T cell serine proteinase-1 (TSP-1) is implicated in cytotoxic T cell-mediated killing.
  • Protease nexin-1 (PN-1) is an extravascular serine protease inhibitor.

Purpose of the Study:

  • To investigate the inhibitory mechanism of PN-1 on TSP-1.
  • To elucidate the interaction between PN-1 and TSP-1.

Main Methods:

  • SDS-PAGE analysis to detect protein complexes.
  • Kinetic analysis of the association rate constant.

Main Results:

  • PN-1 forms irreversible, SDS-stable complexes with TSP-1.
  • Two distinct complex species (91 and 122 kDa) indicate PN-1 inhibits both TSP-1 subunits.
  • Heparin significantly enhances the association rate constant between PN-1 and TSP-1.

Conclusions:

  • PN-1 is a potent inhibitor of TSP-1.
  • PN-1 likely functions as a primary extravascular regulator of TSP-1 released by cytotoxic T lymphocytes.

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