title: Decrease in enkephalinase A number in kidney membranes from hypercholesterolemic and hypertensive rats.
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.
authors.affiliation: Groupe de Recherches Servier, FONDAX ACTAM et CIE, Puteaux, France.
authors.forename: M P
authors.initials: MP
authors.lastname: Fournet-Bourguignon
authors.forename: S
authors.initials: S
authors.lastname: Illiano
authors.forename: A
authors.initials: A
authors.lastname: Lenaers
authors.forename: B
authors.initials: B
authors.lastname: Teisseire
mesh_terms: D000818:Animals; D006937:Hypercholesterolemia / Q000201:enzymology*; D006973:Hypertension / Q000201:enzymology*; D007668:Kidney / Q000201:enzymology*; D008566:Membranes / Q000201:enzymology; D015260:Neprilysin / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism; D011869:Radioligand Assay; D051381:Rats; D011918:Rats, Inbred SHR; D011921:Rats, Inbred WKY; D017207:Rats, Sprague-Dawley
chemical_list: D010455:Peptides; D015260:Neprilysin