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PubMed · 1460602

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

M P Fournet-Bourguignon·S Illiano·A Lenaers·B Teisseire
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Abstract

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.

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AnimalsHypercholesterolemiaHypertensionKidneyMembranesNeprilysinPeptidesRadioligand AssayRatsRats, Inbred SHRRats, Inbred WKYRats, Sprague-DawleyJournal Article

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M P Fournet-Bourguignon, S Illiano, A Lenaers, B Teisseire. 1992. Decrease in enkephalinase A number in kidney membranes from hypercholesterolemic and hypertensive rats.. https://doi.org/10.3109/10799899209074803

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