Identification of kallidin degrading enzymes in the isolated perfused rat heart

Sebastian Wolfrum, Andreas Dendorfer*, Peter Dominiak

*Corresponding author for this work
5 Citations (Scopus)


Kallidin (KD) is an important vasoactive kinin whose physiological effects are strongly dependent on its degradation through local kininases. In the present study, we examined the spectrum of these enzymes and their contribution to KD degradation in isolated perfused rat hearts. By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 μM), amastatin (40 μM) and phosphoramidon (1 μM), respectively, relative kininase activities were obtained. APM (44%) and ACE (35%) are the main KD degrading enzymes in rat heart; NEP (7%) plays a minor role. A participation of carboxypeptidase N (CPN) could not be found.

Original languageEnglish
JournalJapanese Journal of Pharmacology
Issue number1
Pages (from-to)117-120
Number of pages4
Publication statusPublished - 01.01.1999

Research Areas and Centers

  • Academic Focus: Center for Brain, Behavior and Metabolism (CBBM)


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