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Dipeptide processing activates recombinant human prochymase

H Urata1, S S Karnik, R M Graham

  • 1Department of Cardiovascular Biology, Cleveland Clinic Foundation, Ohio 44195-5069.

The Journal of Biological Chemistry
|November 15, 1993
PubMed
Summary
This summary is machine-generated.

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Human chymase (h-chymase) activation requires processing of its dipeptide pro-segment. This enzymatic step is necessary and sufficient for generating active h-chymase, crucial for angiotensin II production.

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Human chymase (h-chymase) is a serine protease involved in angiotensin II formation.
  • Its structure suggests synthesis as an inactive zymogen requiring proteolytic processing for activation.

Purpose of the Study:

  • To investigate the maturational processing and activation mechanism of human chymase.
  • To determine the role of the signal peptide and dipeptide pro-segment in h-chymase activation.

Main Methods:

  • Expression of wild-type and modified h-chymase cDNA constructs in COS-1 cells.
  • Biochemical characterization, purification, and N-terminal sequencing of recombinant proteins.
  • Activation assays using B-cell lymphoma homogenate and protease inhibitors.

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Main Results:

  • Recombinant proteins lacking signal peptide or pro-segment were inactive.
  • Wild-type protein processing yielded the proenzyme.
  • Activation by B-cell lymphoma homogenate led to pro-segment cleavage, generating catalytically active h-chymase identical to the native enzyme.
  • Activation was inhibited by thiol protease inhibitors.

Conclusions:

  • Processing of the dipeptide pro-segment is both necessary and sufficient for human chymase activation.
  • This processing mechanism is likely conserved in related serine proteases like cathepsin G.