Jpn. J. Pharmacol. 79 (1), 117-120 (1999)


Identification of Kallidin Degrading Enzymes in the Isolated Perfused Rat Heart

Sebastian Wolfrum, Andreas Dendorfer (*) and Peter Dominiak


Institute of Pharmacology, Medical University of Lubeck, Ratzeburger Allee 160, D-23538 Lubeck, Germany
(*) To whom correspondence should be addressed.

Abstract: 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 microM), amastatin (40 microM) and phosphoramidon (1 microM), 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.


Keywords: Kallidin, Kinin metabolism, Aminopeptidase M


Copyrightę The Japanese Pharmacological Society 1999

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