Angiotensin I-converting enzyme in isolated human glomeruli.
Angiotensin I-converting enzyme (ACE) activity was measured with hippurylhistidylleucine as a substrate in isolated human glomeruli. The mean level was 2.2 +/- 0.47 mIU/mg glomerular protein. S9780, a newly designed competitive inhibitor of ACE, inhibited this activity by 85% at 0.3 microM. [3H]S9780 specifically bound to isolated human glomeruli. The Kd value and the number of sites were 23 nM and 83 fmol/mg, respectively. The prodrug, S9490, and Captopril were less potent than S9780 in displacing [3H]S9780 from its binding sites. Angiotensin I had no effect. Binding of [3H]S9780 was inhibited after preincubation of the glomeruli with a specific polyclonal anti-human ACE antibody. These results demonstrate that ACE is present in human adult glomeruli.
D000806:Angiotensin-Converting Enzyme Inhibitors; D001665:Binding Sites / Q000187:drug effects; D001667:Binding, Competitive; D002216:Captopril / Q000494:pharmacology; D006801:Humans; D007211:Indoles / Q000494:pharmacology; D007678:Kidney Glomerulus / Q000201:enzymology*; D007703:Peptidyl-Dipeptidase A / Q000302:isolation & purification*; D020913:Perindopril; D013997:Time Factors
D000806:Angiotensin-Converting Enzyme Inhibitors; D007211:Indoles; D002216:Captopril; D007703:Peptidyl-Dipeptidase A; D020913:Perindopril