Open AccessIdentification of Kallidin Degrading Enzymes in the Isolated Perfused Rat Heart
Author(s) -
Sebastian Wolfrum,
Andreas Dendorfer,
Peter Dominiak
Publication year - 1999
Publication title -
japanese journal of pharmacology/japanese journal of pharmacology
Language(s) - English
Resource type - Journals
eISSN - 1347-3506
pISSN - 0021-5198
DOI - 10.1254/jjp.79.117
Subject(s) - kallidin , neprilysin , bradykinin , enkephalinase , enzyme , chemistry , aminopeptidase , endocrinology , phosphoramidon , medicine , renin–angiotensin system , carboxypeptidase , kinin , biochemistry , biology , enkephalin , amino acid , leucine , receptor , opioid , blood pressure
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.