Literature DB >> 14504185

Angiotensin-(1-7) formation in the intact human heart: in vivo dependence on angiotensin II as substrate.

Lawrence S Zisman1, Glenn E Meixell, Michael R Bristow, Charles C Canver.   

Abstract

BACKGROUND: Several enzymes that hydrolyze angiotensin I (Ang I) and Ang II to Ang-(1-7) have been identified, but their relative importance in the intact human heart is not known. METHODS AND
RESULTS: Intracoronary (IC) 123I-Ang I was administered to 4 heart transplantation recipients. Arterial and coronary sinus (CS) samples were taken before and after coadministration of IC enalaprilat. 123I-Ang metabolites were separated by high-pressure liquid chromatography, and 123I-Ang-(1-7) and 123I-Ang II were quantified across the myocardial circulation. 123I-Ang II formation (as measured by fractional conversion) at steady state was 0.43+/-0.05 and was reduced to 0.042+/-0.02 after IC enalaprilat (P<0.01). The fractional conversion of 123I-Ang-(1-7) was 0.198+/-0.032 but was reduced to 0.06+/-0.01 during IC enalaprilat (P<0.01). Net Ang II production at steady state was 2720+/-704 pg/min. Ang-(1-7) production was 3489+/-768 pg/min. After IC enalaprilat, Ang II production fell to 436+/-66.8 pg/min (P<0.05 versus Ang II production). After suppression of Ang II production with enalaprilat, there was net uptake of Ang-(1-7): -289+/-144 pg/min (P<0.05).
CONCLUSIONS: Ang-(1-7) was formed in the intact human myocardial circulation and was decreased when Ang II formation was suppressed. These data indicate that the major pathway for Ang-(1-7) generation in the intact human heart was dependent on substrate availability of Ang II. Ang-(1-7)-forming enzymes that demonstrate substrate preference for Ang II are likely to play an important role in the regulation of Ang-(1-7) formation in the intact human heart.

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Year:  2003        PMID: 14504185     DOI: 10.1161/01.CIR.0000094733.61689.D4

Source DB:  PubMed          Journal:  Circulation        ISSN: 0009-7322            Impact factor:   29.690


  28 in total

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