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Inhibition of lymphocyte protease granzyme A by antithrombin III.
Journal article

Inhibition of lymphocyte protease granzyme A by antithrombin III.

  • Masson D Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland.
  • Tschopp J
  • 1988-12-01
Published in:
  • Molecular immunology. - 1988
Animals
Antithrombin III
Blood
Cells, Cultured
Granzymes
Heparin
Kinetics
Mice
Serine Endopeptidases
Serine Proteinase Inhibitors
T-Lymphocytes, Cytotoxic
English T-lymphocytes contain a cytoplasmic granule associated homo-dimeric protease designated granzyme A. Upon T-cell target cell interaction, the granules undergo exocytosis and granzyme A, and other granule constituents, are released. Here we show that granzyme A secreted into plasma is immediately inactivated by antithrombin III. The rate of complex formation is enhanced 400-fold in the presence of heparin. Two different complexes are generated: granzyme A-antithrombin III and granzyme A-(antithrombin III)2, respectively, indicating that both active centers of granzyme A are functional. Thus, the proteolytic activity of lymphocyte protease granzyme A, whose physiologically relevant function is unknown, is well regulated in plasma.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/93676
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