Angiotensin I-Converting Enzyme Modulates Neutral Endopeptidase Activity in the Rat
- 1 September 2001
- journal article
- Published by Wolters Kluwer Health in Hypertension
- Vol. 38 (3) , 650-654
- https://doi.org/10.1161/hy0901s1.095011
Abstract
Abstract — — Angiotensin I is a substrate for both ACE and for neutral endopeptidase 24.11 (NEP). We hypothesized that high ACE expression is related to low NEP activity. Accordingly, circulating and tissue NEP and ACE activities were measured by fluorometry in homozygous rats (F 0 and F 2 ) for the Lewis microsatellite allele (LL, low ACE) and for the Brown Norway microsatellite allele (BB, high ACE). Plasma, lung, and aortic ACE activities in F 0 and F 2 were higher in BB rats than in LL rats ( P 0 and F 2 homozygous ( P r =−0.6 and −0.598 in F 0 and F 2 , respectively; P r =−0.77 in F 0 and r =−0.59 in F 2 , P r =−0.696 and −0.584 in F 0 and F 2 , respectively; P <0.03). In conclusion, genetically determined high ACE expression in rats is inversely related to tissue NEP activity, which could determine lower angiotensin-(1-7) tissue levels.Keywords
This publication has 17 references indexed in Scilit:
- Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidasePublished by Elsevier ,2003
- A Highly Selective Assay for Neutral Endopeptidase Based on the Cleavage of a Fluorogenic Substrate Related to Leu-EnkephalinAnalytical Biochemistry, 1996
- Tissue-specific Expression of Rat Neutral Endopeptidase (Neprilysin) mRNAsPublished by Elsevier ,1995
- Inhibition of either angiotensin-converting enzyme or neutral endopeptidase induces both enzymesEuropean Journal of Pharmacology, 1994
- In vivo metabolism of angiotensin I by neutral endopeptidase (EC 3.4.24.11) in spontaneously hypertensive rats.Hypertension, 1992
- Chromosomal mapping of two genetic loci associated with blood-pressure regulation in hereditary hypertensive ratsNature, 1991
- Effect of chronic enalapril treatment on enzymes responsible for the catabolism of angiotensin I and formation of angiotensin IIBiochemical Pharmacology, 1990
- Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning.Proceedings of the National Academy of Sciences, 1988
- A highly sensitive fluorometric assay for “enkephalinase”, a neutral metalloendopeptidase that releases tyrosine-glycine-glycine from enkephalinsAnalytical Biochemistry, 1984
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976