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Tryptase from human mast cells does not activate purified human Hageman factor.
S C Alter1, B Lämmle, J H Griffin
1Department of Medicine, Virginia Commonwealth University, Medical College of Virginia, Richmond 23298.
Clinical Allergy
|March 1, 1988
Summary
Tryptase, released from mast cells, does not activate or degrade human Hageman Factor (Factor XII). This study found no change in Hageman Factor activity or molecular weight after tryptase incubation.
Area of Science:
- Biochemistry
- Immunology
- Hematology
Background:
- Tryptase is a protease released from human lung mast cells.
- Hageman Factor (Factor XII) is a key component of the intrinsic coagulation pathway.
- The interaction between mast cell mediators and coagulation factors is not fully understood.
Purpose of the Study:
- To investigate the effect of tryptase on the enzymatic activity and molecular integrity of purified human Hageman Factor.
- To determine if tryptase can activate or inactivate Hageman Factor.
Main Methods:
- Purified human Hageman Factor was incubated with human lung tryptase at 37°C.
- Hageman Factor enzymatic activity was measured.
- Activation of Hageman Factor by bovine trypsin was used as a positive control.
- Polyacrylamide gel electrophoresis (PAGE) was used to assess molecular weight changes.
Main Results:
- Incubation with tryptase did not increase Hageman Factor enzymatic activity.
- Pre-incubation with tryptase did not affect subsequent activation of Hageman Factor by trypsin.
- PAGE analysis showed no alteration in the molecular weight of Hageman Factor after tryptase incubation.
Conclusions:
- Tryptase does not activate human Hageman Factor.
- Tryptase does not enzymatically degrade or alter the molecular weight of human Hageman Factor.
- These findings suggest tryptase does not directly modulate Hageman Factor function in coagulation.