Identification of kallidin degrading enzymes in the isolated perfused rat heart

Sebastian Wolfrum; Andreas Dendorfer; Peter Dominiak

doi:10.1254/jjp.79.117

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)

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	https://doi.org/10.1254/jjp.79.117
Publication status	Published - 01.01.1999

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

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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.",

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AU - Wolfrum, Sebastian

AU - Dendorfer, Andreas

AU - Dominiak, Peter

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N2 - 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.

AB - 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.

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M3 - Journal articles

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AN - SCOPUS:0033005640

SN - 0021-5198

VL - 79

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EP - 120

JO - Japanese Journal of Pharmacology

JF - Japanese Journal of Pharmacology

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ER -

Identification of kallidin degrading enzymes in the isolated perfused rat heart

Abstract

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