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Cathepsin G binds to human lymphocytes

T Yamazaki1, Y Aoki

  • 1Department of Nutrition and Biochemistry, The Institute of Public Health, Tokyo, Japan.

Journal of Leukocyte Biology
|January 1, 1997
PubMed
Summary

Cathepsin G, a neutrophil serine protease, specifically binds to human lymphocytes including B cells, T cells, and NK cells. This binding, crucial for lymphocyte stimulation, involves both the active site and other regions of cathepsin G.

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Area of Science:

  • Immunology
  • Biochemistry
  • Cell Biology

Background:

  • Neutrophils play a critical role in the immune response.
  • Cathepsin G is a serine protease found in neutrophil azurophil granules.
  • Previous studies indicated cathepsin G stimulates human lymphocytes.

Purpose of the Study:

  • To investigate the specific binding characteristics of cathepsin G to human lymphocytes.
  • To determine the role of cathepsin G's active site in lymphocyte binding and stimulation.

Main Methods:

  • Flow cytometry was used to assess cathepsin G binding to lymphocyte subsets (B cells, CD4+ T cells, CD8+ T cells, NK cells).
  • Binding assays were performed using native and phenylmethylsulfonyl fluoride (PMSF)-inhibited cathepsin G.
  • Displacement assays were conducted to evaluate the interaction sites.

Main Results:

  • Cathepsin G demonstrated specific, saturable, and reversible binding to all tested lymphocyte types.
  • PMSF-inhibited cathepsin G showed reduced binding affinity and fewer binding sites compared to native cathepsin G.
  • Binding of native cathepsin G exhibited cooperativity, unlike the inhibited form.
  • Partially inhibited cathepsin G could displace bound native cathepsin G.

Conclusions:

  • Lymphocyte surface molecules recognize multiple sites on cathepsin G, including but not limited to the active site.
  • The active site of cathepsin G is essential for its binding to lymphocytes and subsequent stimulation.
  • Proteolytic activity of cathepsin G is required for effective lymphocyte activation.

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