Decrease in enkephalinase A number in kidney membranes from hypercholesterolemic and hypertensive rats

The variation of enkephalinase A number on the hypertensive and hypercholesterolemia rats kidney membranes is studied using the [3H]-acetorphan, a potent inhibitor of enkephalinase A to label the protease in rat kidney. The binding of [3H]-acetorphan to kidney membrane determined in vitro with both...

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Bibliographic Details
Published inJournal of receptor research Vol. 12; no. 4; p. 401
Main Authors Fournet-Bourguignon, M P, Illiano, S, Lenaers, A, Teisseire, B
Format Journal Article
LanguageEnglish
Published United States 1992
Subjects
Animals
Hypercholesterolemia - enzymology
Hypertension - enzymology
Kidney - enzymology
Membranes - enzymology
Neprilysin - metabolism
Peptides - metabolism
Radioligand Assay
Rats
Rats, Inbred SHR
Rats, Inbred WKY
Rats, Sprague-Dawley
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Summary:The variation of enkephalinase A number on the hypertensive and hypercholesterolemia rats kidney membranes is studied using the [3H]-acetorphan, a potent inhibitor of enkephalinase A to label the protease in rat kidney. The binding of [3H]-acetorphan to kidney membrane determined in vitro with both equilibrium and kinetic methods is saturable and reversible involving a single class of sites with a dissociation constant of 4-5.3 nM. The [3H]-acetorphan binding capacity is identical, Bmax approximately 51 pmoles per mg of proteins, for kidney membranes from Sprague Dawley and Wistar Kyoto rats. In contrast, the enkephalinase A number is decreased in the pathological states studied: 20% for hypertensive rats and 50% for hypercholesterolemic rats. Such pharmacological results provide a great deal of information about the modification appeared in the metabolism of peptidic substrates of enkephalinase A in hypercholesterolemia and hypertension.
ISSN:0197-5110
DOI:10.3109/10799899209074803