Oxidation-induced increase in activity of angiotensin converting enzyme in the rat kidney.
The activity of angiotensin converting enzyme(ACE) in crude extracts of the rat renal cortex was increased when the oxidizing agent diamide was added to the extract. The maximal activity was obtained at concentrations over 1 mM, and the value was twice or more the activity in the absence of the pretreatment. The activity of ACE was also increased by the diamide-pretreatment of the isolated membrane fraction of the renal cortex, thereby indicating that the increase in activity was not due to oxidation of endogenous glutathione (GSH) that may lower the ACE activity, but rather that ACE itself was oxidized. When O2 was included in the extract for 2 h, the ACE activity also increased to about twice the original activity. Lineweaver-Burk plots analysis demonstrated that, after oxidation with diamide and O2, the Vmax was increased but the Km remained unchanged. We conclude that the action of ACE in the kidney functions may differ in relation to oxidation of the tissue.
Ikemoto
F
F
Department of Pharmacology, Osaka City University Medical School, Japan.
Song
G
G
Tominaga
M
M
Yamamoto
K
K
D000818:Animals; D002216:Captopril / Q000494:pharmacology; D003958:Diamide / Q000494:pharmacology; D005978:Glutathione / Q000378:metabolism; D007672:Kidney Cortex / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D010084:Oxidation-Reduction; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D003958:Diamide; D002216:Captopril; D007703:Peptidyl-Dipeptidase A; D005978:Glutathione