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 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.
Fournet-Bourguignon
M P
MP
Groupe de Recherches Servier, FONDAX ACTAM et CIE, Puteaux, France.
Illiano
S
S
Lenaers
A
A
Teisseire
B
B
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
D010455:Peptides; D015260:Neprilysin