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 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 language | English |
|---|---|
| Journal | Japanese Journal of Pharmacology |
| Volume | 79 |
| Issue number | 1 |
| Pages (from-to) | 117-120 |
| Number of pages | 4 |
| ISSN | 0021-5198 |
| DOIs | |
| Publication status | Published - 01.01.1999 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Research Areas and Centers
- Academic Focus: Center for Brain, Behavior and Metabolism (CBBM)
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