Identification of Kallidin Degrading Enzymes in the Isolated Perfused Rat Heart | Zendy

Wolfrum Sebastian | Zendy; Dendorfer Andreas | Zendy; Dominiak Peter | Zendy

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Identification of Kallidin Degrading Enzymes in the Isolated Perfused Rat Heart

Author(s) -

Wolfrum Sebastian,

Dendorfer Andreas,

Dominiak Peter

Publication year - 1999

Publication title -

the 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.

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