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Related Experiment Videos

Endothelin-converting enzymes.

T J Opgenorth1, J R Wu-Wong, K Shiosaki

  • 1Pharmaceutical Products Division, Abbott Laboratories, Illinois 60064.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|June 1, 1992
PubMed
Summary
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Researchers are investigating endothelin-converting enzyme (ECE) inhibitors to block endothelin production in diseases. While a metalloprotease shows promise as the relevant enzyme, its direct impact on disease pathogenesis requires further proof.

Area of Science:

  • Biochemistry
  • Pharmacology
  • Molecular Biology

Background:

  • Endothelin-converting enzyme (ECE) is a target for therapeutic intervention.
  • Inhibiting ECE may prevent endothelin production in pathogenic conditions.
  • Two enzyme types, aspartic and metalloprotease, exhibit ECE characteristics.

Purpose of the Study:

  • To explore the role of ECE in endothelin-related diseases.
  • To identify the specific ECE enzyme responsible for endothelin production.
  • To evaluate the therapeutic potential of ECE inhibitors.

Main Methods:

  • Investigating aspartic and metalloprotease activities.
  • Utilizing phosphoramidon as an inhibitor of metalloprotease.
  • Assessing the impact of ECE inhibition on endogenous endothelin levels.

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Main Results:

  • A metalloprotease, inhibited by phosphoramidon, is suggested as the physiologically relevant ECE.
  • The precise ECE enzyme responsible for endothelin conversion remains under investigation.
  • Conclusive evidence linking ECE inhibitors to altered disease pathogenesis is still pending.

Conclusions:

  • The metalloprotease is a potential target for ECE inhibition.
  • Further studies are needed to confirm the role of ECE inhibitors in disease.
  • Directly demonstrating the therapeutic efficacy of ECE inhibitors in vivo is crucial.