Drugs online research references
J Biol Chem. 1985 Dec 5;260(28):14938-44.
Angiotensin-converting enzyme from human tissues. Physicochemical, catalytic, and immunological properties.
Lanzillo JJ, Stevens J, Dasarathy Y, Yotsumoto H, Fanburg BL.
Angiotensin-converting enzyme was purified from human lung, kidney, testis, blood plasma, and seminal plasma using a facile two-step protocol which included affinity chromatography on Sepharose-bound lisinopril followed by either gel filtration or hydroxylapatite chromatography. Molecular mass for converting enzyme from all sources except testis was 140 kDa. That from testis consisted of both a 90- and a 140-kDa form in a 4:1 ratio. Detergent-extracted membrane-bound converting enzyme aggregated on gel filtration chromatography, while trypsin-extracted and soluble converting enzyme did not. Comparison of detergent-extracted and trypsin-extracted membrane-bound converting enzyme by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing indicated that the membrane binding sequence contributed minimally to the size and charge of the enzyme. Catalytic and kinetic properties assessed by interaction with substrates, inhibitors, and anti-converting enzyme immunoglobulin were similar for all forms and sources of converting enzyme. Enzyme-linked immunosorbent assay revealed only partial homology between the 90- and 140-kDa forms of the enzyme.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2999099&dopt=Abstract
Clin Exp Hypertens A. 1987;9(2-3):307-21.
Angiotensin converting enzyme inhibition in plasma and tissues.
Johnston CI, Cubela R, Sakaguchi K, Jackson B.
Angiotensin converting enzyme (ACE) and the ACE inhibitor lisinopril were measured in patients with renal impairment, by both radioinhibitor 125I MK351A binding studies, and by radioimmunoassay. Plasma concentration of lisinopril estimated by radioinhibitor binding displacement correlated closely with that measured by radioimmunoassay. Plateau lisinopril concentration in 8 patients with varying degrees of renal failure treated with 5 mg lisinopril per day for 1 week, was inversely related to renal function. Plasma lisinopril concentrations of 30-70 ng/ml were required for 50% inhibition of plasma ACE activity in vivo. Acute studies in the rat showed inhibition of ACE in different tissues had different time courses. These observations suggest that 125I MK351A binding studies in tissues will be useful in establishing the pharmacokinetic and pharmacodynamic profiles of newer ACE inhibitors, and may help delineate the contribution of ACE in different tissues to cardiovascular homeostasis.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3038391&dopt=Abstract
J Lab Clin Med. 1994 Mar;123(3):372-7.
Angiotensin-converting enzyme, bradykinin, and angiotensin II receptor binding in rat skin, tendon, and heart valves: an in vitro, quantitative autoradiographic study.
Sun Y, Diaz-Arias AA, Weber KT.
Department of Internal Medicine, University of Missouri-Columbia 65212.
Angiotensin converting enzyme (ACE), an ectoenzyme bound to vascular endothelial cells, is also found at tissue sites (TACE) normally composed of fibrillar collagen and fibroblasts. For example, TACE is present in the adventitia of intramural coronary arteries and matrix of heart valves, as well as the fibrous tissue that follows the chronic administration of angiotensin II (AII) or aldosterone. At these sites bradykinin (BK) receptor but not AII receptor binding has been observed, suggesting that in fibrous tissue TACE uses BK as substrate. Dermis, subcutaneous tissue, and skeletal muscle tendon likewise are sites that are rich in fibrillar collagen but are different in their cellularity. Accordingly, we tested the hypothesis that TACE is normally present at sites of fibrous tissue and that BK--not AIK--receptor binding is anatomically coincident with TACE in keeping with its role as a kininase II. TACE and receptors for BK and AII were localized by quantitative in vitro autoradiography with [125I]351A, 125I[Tyr8]BK, and 125I[Sar1, Ile8]AII, respectively. Skin morphology was examined in serial full thickness sections obtained from the dorsum of Sprague-Dawley rats. We found the following: (1) high TACE binding occurred in subcutaneous connective tissue and heart valves that was displaced by lisinopril or 351A in a dose-dependent manner; (2) BK receptor binding and low density AII receptor binding were seen at these sites, where AII receptor binding was totally displaced by a type 1 (DuP753) but not a type 2 (PD123177) receptor antagonist; (3) ACE, BK, and AII receptor binding was not evident in epidermis, dermis, skeletal muscle, or tendon.(ABSTRACT TRUNCATED AT 250 WORDS)
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8133148&dopt=Abstract
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