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