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Institute of Experimental and Clinical Pharmacology and Toxicology, Medical University of Lübeck, D-23538 Lübeck, Germany
Kinins are vasoactive peptide hormones
that can confer protection against the development of hypertension.
Because their efficacy is greatly influenced by the rate of enzymatic
degradation, the activities of various kininases in plasma and blood of
spontaneously hypertensive rats (SHR) were compared with those in
normotensive Wistar-Kyoto rats (WKY) to identify pathogenic
alterations. Either plasma or whole blood was incubated with bradykinin
(10 µM). Bradykinin and kinin metabolites were measured by
high-performance liquid chromatography. Kininase activities were
determined by cumulative inhibition of angiotensin I-converting enzyme
(ACE), carboxypeptidase N (CPN), and aminopeptidase P (APP), using
selective inhibitors. Plasma of WKY rats degraded bradykinin at a rate
of 13.3 ± 0.94 µmol · min
1 · l1. The
enzymes ACE, APP, and CPN represented 92% of this kininase activity,
with relative contributions of 52, 25, and 16%, respectively. Inclusion of blood cells at physiological concentrations did not extend
the activities of these plasma kininases further. No differences of
kinin degradation were found between WKY and SHR. The identical conditions of kinin degradation in WKY and SHR suggest no pathogenic role of kininases in the SHR model of genetic hypertension.
kinins; metabolism; angiotensin I-converting enzyme; aminopeptidase P; carboxypeptidase N
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