Monoamine Oxidase and Semicarbazide-Sensitive Amine Oxidase Activities in Isolated Cardiomyocytes of Spontaneously Hypertensive Rats
Authors: Pino, R.; Failli, P.; Mazzetti, L.; Buffoni, F.
Source: Biochemical and Molecular Medicine, Volume 62, Number 2, December 1997 , pp. 188-196(9)
Publisher: Academic Press
Abstract:In the isolated cardiomyocytes of spontaneously hypertensive rats (SHR, 3 months old) MAO A and B activities were significantly increased compared to the myocytes in the hearts of age-matched Wistar-Kyoto rats. This increase was not associated with cardiac hypertrophy in these young animals, but might represent an early event in the development of hypertrophy. A semicarbazide-sensitive amine oxidase (SSAO) activity was found in cardiomyocytes. This activity showed a high affinity for benzylamine (Km 5-6 muM) and was not inhibited by 10-4 M pargyline and 10-5 M deprenyl, but was largely inhibited by 10-4 M B24 (3,5-diethoxy-4-aminomethylpyridine), a specific inhibitor of semicarbazide-sensitive amine oxidase with high affinity for benzylamine. The SSAO enzyme of rat cardiomyocytes is a copper-amine oxidase and has a cross-reactivity with the antibodies raised against pure pig plasma benzylamine oxidase. In the cardiomyocytes of 3-month-old SHR rats the level of this enzymic activity is not significantly increased. Copyright 1997 Academic Press.
Document Type: Research Article
Affiliations: Department of Pharmacology, University of Florence, Florence, 50134, Italy
Publication date: December 1, 1997