Inhibitor binding assay for angiotensin-converting enzyme.

Fyhrquist, Frej; Tikkanen, I.; Grönhagen-Riska, C; Hortling, Lars; Hichens, Martin

doi:10.1093/clinchem/30.5.696

Cited by 67 publications

(15 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The present method of ACE estimation by radioinhibitor binding was developed at the same time as that reported by Fyhrquist et al (1984). Differences between the assay systems include the presence of sulphate and the use of Dextran T70 charcoal for separation of bound from free counts.…”

Section: Discussionmentioning

confidence: 99%

Angiotensin‐converting Enzyme (Ace) Measurement in Human Serum Using Radioinhibitor Ligand Binding

Jackson

Cubela

Johnston

1986

Aust J Exp Biol Med

View full text Add to dashboard Cite

Summary. MK315A, a tyrosyl analogue of enalaprilic acid (MK422) is a potent inhibitor of angiotensin-converting enzyme (ACE). MK351A was radioiodinated with '"i and used to develop a radioinhibitor binding assay for human serum ACE.'^'i MK351A associated rapidly and reversibly with human serum ACE (TVi = Vi h). Bound '"i MK351A was displaced by an excess of cold MK351A, to give non-specific binding of <1%. Scatchard analysis of binding was linear (r= -0-99, n = 6, p<0 001), indicating a single class of binding site.ACE was estimated in serum from normal patients and patients with sarcoid by the radio inhibitor binding assay and by enzyme kinetic assay using Hip-His-Leu as substrate. The two methods for ACE estimation correlated closely (r = 0-87, n«82, p< 0-001).The radioinhibitor binding assay for human serum ACE is a simple, sensitive and specific assay which utilizes novel assay methodology.

show abstract

Section: Discussionmentioning

confidence: 99%

Angiotensin‐converting Enzyme (Ace) Measurement in Human Serum Using Radioinhibitor Ligand Binding

Jackson

Cubela

Johnston

1986

Aust J Exp Biol Med

View full text Add to dashboard Cite

show abstract

“…Care was taken to minimize irritation of the eye. Serum ACE concentration was determined in all patients, using the inhibitor-binding assay (Fyhrquist et al 1984). Tear ACE was determined using the same method on a micro scale.…”

Section: Methodsmentioning

confidence: 99%

Concentration of angiotensin‐converting enzyme in tears of patients with sarcoidosis

Immonen

Friberg

Sorsila

et al. 1987

Acta Ophthalmologica

View full text Add to dashboard Cite

The concentration of angiotensin-converting enzyme (ACE) was studied in 39 patients with sarcoidosis, 6 of whom had active uveitis, 7 patients with non-sarcoid uveitis and 36 healthy controls. ACE concentration in tears was also compared with total protein concentration in tears in order to exclude the effect of varying dilution of tears at sampling. Mean tear ACE concentration and ACE/protein ratio were higher in patients with sarcoidosis than in controls. There were no significant differences in tear ACE concentration or ACE/protein ratio between sarcoidosis patients with uveitis and those with no eye involvement. Tear ACE concentration and ACE/protein ratio did not correlate significantly with serum ACE concentration. It is concluded that the mean concentration of tear ACE and ACE/protein ratio are elevated in sarcoidosis, but that this elevation is independent of any eye involvement.

show abstract

“…ACE amount in intact endothelial cells was measured by an inhibitor-binding assay developed and characterized in our laboratory (21). Briefly, a lisinopril analog, p-hydroxybenzamidine derivative of N-(1-carboxy-3-phenylpropyl)-L-lysyl-L-proline (351A; Merck, Sharp and Dohme; Rahway, NJ), was labeled with 125 iodine (IMS 30; Amersham; Buckinghamshire, UK) using the chloramine T method, as described elsewhere (8). 125 I-labeled 351A is specifically bound to ACE (8,11).…”

Section: Ace Inhibitor Binding Assaymentioning

confidence: 99%

Atorvastatin completely inhibits VEGF-induced ACE upregulation in human endothelial cells

Saijonmaa

Nyman²,

Stewen³

et al. 2004

American Journal of Physiology-Heart and Circulatory Physiology

View full text Add to dashboard Cite

Angiotensin-converting enzyme (ACE) plays an important role in the pathophysiology of cardiovascular disease. We investigated whether atorvastatin, a powerful agent for the prevention and treatment of cardiovascular disease, influences ACE production in endothelial cells. Human umbilical cord vein endothelial cells were treated with VEGF (476 pM), which induced ACE upregulation. Cotreatment with atorvastatin (0.1-10 microM) dose dependently inhibited VEGF-induced ACE upregulation. In the presence of mevalonate (100 microM), atorvastatin failed to downregulate VEGF-induced ACE production. Cotreatment of the cells with either farnesylpyrophosphate (FPP; 5 microM) or geranylgeranylpyrophosphate (GGPP; 5 microM) partially inhibited the suppressive effect of atorvastatin. Pretreatment of the cells with Rho-associated protein kinase inhibitor, Y-27632 (10 microM), partially inhibited VEGF-induced ACE upregulation. VEGF (476 pM) caused PKC phosphorylation, which was inhibited by cotreatment of the cells with atorvastatin. Atorvastatin inhibited VEGF-induced ACE upregulation probably by inhibiting PKC phosphorylation. This effect was mediated via inhibition of the mevalonate pathway. ACE downregulation may be an additional beneficial effect of statins in the treatment of cardiovascular disease.

show abstract

Inhibitor binding assay for angiotensin-converting enzyme.

Cited by 67 publications

References 0 publications

Angiotensin‐converting Enzyme (Ace) Measurement in Human Serum Using Radioinhibitor Ligand Binding

Angiotensin‐converting Enzyme (Ace) Measurement in Human Serum Using Radioinhibitor Ligand Binding

Concentration of angiotensin‐converting enzyme in tears of patients with sarcoidosis

Atorvastatin completely inhibits VEGF-induced ACE upregulation in human endothelial cells

Contact Info

Product

Resources

About