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

  • David Gurwitz*
  • , Markus M. Simon
  • , Ulli Fruth
  • , Dennis D. Cunningham
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

The T cell serine proteinase-1 (TSP-1) which most probably is involved in cell killing by cytotoxic T cells is inhibited by protease nexin-1 (PN-1), an extravascular serine protease inhibitor. The inhibition is irreversible and correlates with formation of SDS-stable complexes between the two proteins. Two distinct species of complexes (91 and 122 kDa) are observed upon SDS-PAGE analysis of the reacted proteins, indicating that PN-1 is capable of complexing and inhibiting both subunits of the homodimeric TSP-1 molecule. Heparin (2 ug/ml) increases the association rate constant from 4.2×104 M-1 sec-1 to 4.8×105 M-1 sec-1. These observations suggest that PN-1 may function as a major extravascular inhibitor of TSP-1 released from cytotoxic T lymphocytes.

Original languageEnglish
Pages (from-to)300-304
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume161
Issue number1
DOIs
StatePublished - 30 May 1989
Externally publishedYes

Funding

FundersFunder number
DeutscheF orschungsgemeinschaGftSi 214/5-4/5
National Institute of General Medical SciencesR01GM031609

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