Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/12224
Title: Tissue angiotensin converting enzyme (ACE) during changes in the renin-angiotensin system.
Authors: Jackson, B;Cubela, R B;Johnston, Colin I
Affiliation: University of Melbourne, Department of Medicine, Austin Hospital, Heidelberg, Victoria, Australia.
Issue Date: 16-May-1987
Citation: Journal of Cardiovascular Pharmacology; 10 Suppl 7(): S137-40
Abstract: To establish if physiological manipulations of the renin-angiotensin system modulates tissue angiotensin converting enzyme (ACE), rats were fed low, normal, or high salt diets, or high salt and DOCA, for 3 weeks, and then plasma and tissue ACE levels were determined by radioinhibitor binding studies. Urinary sodium excretion (mmol/24 h) was 0.03 +/- 0.01 (low salt), 0.58 +/- 0.09 (normal salt), and 10.4 +/- 1.3 (high salt), and plasma angiotensin II (pg/ml) was 73.5 +/- 8.6 (low salt), 49.3 +/- 8.5 (normal salt), 32.2 +/- 8.5 (high salt), and 6.9 +/- 0.6 (high salt plus DOCA) in the third week of dietary treatment. ACE was studied by Scatchard analysis of radioinhibitor binding in plasma and tissue homogenates. [125I]MK351A bound to ACE was measured under standardized conditions in the presence of MK351A (10(-13) to 10(-5) M) and MK351A binding sites and equilibrium dissociation constant calculated. There were no significant changes in binding site concentration in plasma, lung, aorta, epididymus, brain, or kidney preparations across the range of salt states studied. The equilibrium dissociation constant appeared uniform within organs, but varied between organs. Further studies were undertaken with captopril, enalapril, and cilazoprilic acid in kidney and lung preparations. Concentration of inhibitor required for equal displacement of bound [125I]MK351A was consistently greater for kidney than for lung. Binding studies of rat ACE using [125I]MK351A showed that manipulation of salt status did not influence rat tissue ACE. Binding data suggest ACE from different tissues may have variations at the active site.
Internal ID Number: 2485049
URI: http://ahro.austin.org.au/austinjspui/handle/1/12224
URL: http://www.ncbi.nlm.nih.gov/pubmed/2485049
Type: Journal Article
Subjects: Animals
Male
Peptidyl-Dipeptidase A.metabolism
Radioligand Assay
Rats
Rats, Inbred Strains
Renin-Angiotensin System.physiology
Salts
Appears in Collections:Journal articles

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