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Rat mast cell tryptase.

D Lagunoff1, A Rickard, C Marquardt

  • 1Department of Pathology, St. Louis University School of Medicine, Missouri 63104.

Archives of Biochemistry and Biophysics
|November 15, 1991
PubMed
Summary
This summary is machine-generated.

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Rat mast cell tryptase, unlike chymase, is poorly bound to granules and unstable extracellularly. This suggests distinct roles for these enzymes after mast cell secretion.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Immunology

Background:

  • Rat mast cell tryptase is primarily localized within secretory granules.
  • Understanding the extracellular behavior of tryptase is crucial for elucidating its function.

Purpose of the Study:

  • To investigate the granule binding, release kinetics, and extracellular stability of rat mast cell tryptase.
  • To compare the properties of rat tryptase with rat chymase and tryptases from other species.

Main Methods:

  • Active site labeling using [3H]diisopropyl fluorophosphate to determine tryptase:chymase ratios.
  • Induction of mast cell secretion to observe tryptase release.
  • Hypotonic treatment of isolated granules to assess tryptase binding to the granule matrix.
  • Stability assays of tryptase at different pH levels.

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Main Results:

  • The ratio of tryptase to chymase active sites in rat mast cells was found to be 0.05.
  • Rat tryptase exhibited poor binding to the granule matrix, releasing parallel to histamine.
  • Tryptase was found in the supernatant after hypotonic stripping of granule membranes.
  • Rat tryptase showed moderate stability at pH 5.0 but was unstable at pH 7.5.

Conclusions:

  • Rat mast cell tryptase is less integrated into the granule matrix compared to chymase.
  • The extracellular instability of tryptase at physiological pH suggests a transient extracellular role.
  • The distinct properties of rat tryptase indicate a functional divergence from chymase in the extracellular environment.