scholarly journals Aronia melanocarpa ElliotReduces the Activity of Angiotensin I-Converting Enzyme—In VitroandEx VivoStudies

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Joanna Sikora ◽  
Marlena Broncel ◽  
Elżbieta Mikiciuk-Olasik
Keyword(s):  
Ace Inhibition ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Hypotensive Action ◽  
Aronia Melanocarpa ◽  
Clinical Observations ◽  
Angiotensin I Converting Enzyme ◽  
Ace Activity ◽  
Positive Correlations

Purpose. The aim of the study was to analyze the effects of two-month supplementation with chokeberry preparation on the activity of angiotensin I-converting enzyme (ACE) in patients with metabolic syndrome (MS). During thein vitrostage of the study, we determined the concentration of chokeberry extract, which inhibited the activity of ACE by 50% (IC50).Methods. The participants (n=70) were divided into three groups: I—patients with MS who received chokeberry extract supplements, II—healthy controls, and III—patients with MS treated with ACE inhibitors.Results. After one and two months of the experiment, a decrease in ACE activity corresponded to 25% and 30%, respectively. We documented significant positive correlations between the ACE activity and the systolic (r=0.459,P=0.048) and diastolic blood pressure, (r=0.603,P=0.005) and CRP. The IC50of chokeberry extract and captopril amounted to155.4±12.1 μg/mL and0.52±0.18 μg/mL, respectively.Conclusions. Ourin vitrostudy revealed that chokeberry extract is a relatively weak ACE inhibitor. However, the results of clinical observations suggest that the favorable hypotensive action of chokeberry polyphenols may be an outcome of both ACE inhibition and other pleotropic effects, for example, antioxidative effect.

scholarly journals Camel Hemorphins Exhibit a More Potent Angiotensin-I Converting Enzyme Inhibitory Activity than Other Mammalian Hemorphins: An In Silico and In Vitro Study

Biomolecules ◽  
2020 ◽  
Vol 10 (3) ◽  
pp. 486 ◽  
Author(s):  
Amanat Ali ◽  
Seham Abdullah Rashed Alzeyoudi ◽  
Shamma Abdulla Almutawa ◽  
Alya Nasir Alnajjar ◽  
Yusra Al Dhaheri ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Active Site ◽  
Inhibitory Activity ◽  
In Vitro Study ◽  
Ace Inhibition ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Dynamics Simulations

Angiotensin-I converting enzyme (ACE) is a zinc metallopeptidase that has an important role in regulating the renin-angiotensin-aldosterone system (RAAS). It is also an important drug target for the management of cardiovascular diseases. Hemorphins are endogenous peptides that are produced by proteolytic cleavage of beta hemoglobin. A number of studies have reported various therapeutic activities of hemorphins. Previous reports have shown antihypertensive action of hemorphins via the inhibition of ACE. The sequence of hemorphins is highly conserved among mammals, except in camels, which harbors a unique Q>R variation in the peptide. Here, we studied the ACE inhibitory activity of camel hemorphins (LVVYPWTRRF and YPWTRRF) and non-camel hemorphins (LVVYPWTQRF and YPWTQRF). Computational methods were used to determine the most likely binding pose and binding affinity of both camel and non-camel hemorphins within the active site of ACE. Molecular dynamics simulations showed that the peptides interacted with critical residues in the active site of ACE. Notably, camel hemorphins showed higher binding affinity and sustained interactions with all three subsites of the ACE active site. An in vitro ACE inhibition assay showed that the IC50 of camel hemorphins were significantly lower than the IC50 of non-camel hemorphins.

scholarly journals Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Peptides Isolated from Carabao Mango (Mangifera indica) Flesh

KIMIKA ◽  
2021 ◽  
Vol 32 (1) ◽  
pp. 1-18
Author(s):  
Trisha Rojas ◽  
Jherome Co ◽  
Mia Clare Marie Bercansil ◽  
Lory Jane Dela Cruz ◽  
Lawrence Yves Uy ◽  
...  
Keyword(s):  
Mangifera Indica ◽  
Ace Inhibition ◽  
The Philippines ◽  
Antihypertensive Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Hypertension has been reported as the second major cause of morbidity in the Philippines. One of the mechanisms to control blood pressure is through the inhibition of the angiotensin I-converting enzyme (ACE). This study specifically focused on the determination of ACE inhibitory activities of peptides from ‘Carabao’ mango flesh of three shell colors (SC1, SC3, SC5). The bioactive peptides were obtained upon a series of extraction, purification, and enzymatic hydrolysis steps. Among the undigested and digested crude and purified samples, the highest in vitro ACE inhibition was exhibited by the three-hour digest of SC3 (83.28 ± 0.83%). The most prominent peak from the fractionation of the mixture of peptides in SC3 digest was evaluated for ACE inhibition, and the decrease in activity inferred the synergistic effect of the peptides in exhibiting the inhibitory function. This selected bioactive peptide was revealed to have alanine and phenylalanine as the components, which can possibly be AF – an ACE inhibitory peptide determined from in silico analyses. Meanwhile, assessment of the in vivo antihypertensive activity showed no significant results due to insufficiently administered doses of the samples. Overall, the measured activity of the ACE inhibitory peptides inferred the potential of mango as a functional food in dealing with hypertension.  

scholarly journals Investigation of Chlorella pyrenoidosa Protein as a Source of Novel Angiotensin I-Converting Enzyme (ACE) and Dipeptidyl Peptidase-IV (DPP-IV) Inhibitory Peptides

Nutrients ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 1624
Author(s):  
Yuchen Li ◽  
Gilda Aiello ◽  
Enrico Mario Alessandro Fassi ◽  
Giovanna Boschin ◽  
Martina Bartolomei ◽  
...  
Keyword(s):  
Chlorella Pyrenoidosa ◽  
Cellular Level ◽  
Potential Interaction ◽  
Converting Enzyme ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Dpp Iv ◽  
Ace Activity ◽  
The Stability

Chlorella pyrenoidosa (C. pyrenoidosa) is a microalgae species with a remarkably high protein content that may potentially become a source of hypotensive and hypoglycemic peptides. In this study, C. pyrenoidosa proteins were extracted and hydrolyzed overnight with pepsin and trypsin with final degrees of hydrolysis of 18.7% and 35.5%, respectively. By LC-MS/MS, 47 valid peptides were identified in the peptic hydrolysate (CP) and 66 in the tryptic one (CT). At the concentration of 1.0 mg/mL, CP and CT hydrolysates inhibit in vitro the angiotensin-converting enzyme (ACE) activity by 84.2 ± 0.37% and 78.6 ± 1.7%, respectively, whereas, tested at cellular level at the concentration of 5.0 mg/mL, they reduce the ACE activity by 61.5 ± 7.7% and 69.9 ± 0.8%, respectively. At the concentration of 5.0 mg/mL, they decrease in vitro the DPP-IV activity by 63.7% and 69.6% and in Caco-2 cells by 38.4% and 42.5%, respectively. Short peptides (≤10 amino acids) were selected for investigating the potential interaction with ACE and DPP-IV by using molecular modeling approaches and four peptides were predicted to block both enzymes. Finally, the stability of these peptides was investigated against gastrointestinal digestion.

Effect of enalapril (MK-421), an orally active angiotensin I converting enzyme inhibitor, on blood pressure, active and inactive plasma renin, urinary prostaglandin E2, and kallikrein excretion in conscious rats

1984 ◽  
Vol 62 (1) ◽  
pp. 116-123 ◽  
Author(s):  
Ernesto L. Schiffrin ◽  
Jolanta Gutkowska ◽  
Gaétan Thibault ◽  
Jacques Genest
Keyword(s):  
Blood Pressure ◽  
Angiotensin Ii ◽  
Plasma Renin Activity ◽  
Plasma Renin ◽  
Ace Inhibition ◽  
Renin Activity ◽  
Prostaglandin E ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme

The angiotensin I converting enzyme (ACE) inhibitor enalapril (MK-421), at a dose of 1 mg/kg or more by gavage twice daily, effectively inhibited the pressor response to angiotensin I for more than 12 h and less than 24 h. Plasma renin activity (PRA) did not change after 2 or 4 days of treatment at 1 mg/kg twice daily despite effective ACE inhibition, whereas it rose significantly at 10 mg/kg twice daily. Blood pressure fell significantly and heart rate increased in rats treated with 10 mg/kg of enalapril twice daily, a response which was abolished by concomitant angiotensin II infusion. However, infusion of angiotensin II did not prevent the rise in plasma renin. Enalapril treatment did not change urinary immunorcactive prostaglandin E2 (PGE2) excretion and indomethacin did not modify plasma renin activity of enalapril-treated rats. Propranolol significantly reduced the rise in plasma renin in rats receiving enalapril. None of these findings could be explained by changes in the ratio of active and inactive renin. Water diuresis, without natriuresis and with a decrease in potassium urinary excretion, occurred with the higher dose of enalapril. Enalapril did not potentiate the elevation of PRA in two-kidney one-clip Goldblatt hypertensive rats. In conclusion, enalapril produced renin secretion, which was in part β-adrenergically mediated. The negative short feedback loop of angiotensin II and prostaglandins did not appear to be involved. A vasodilator effect, apparently independent of ACE inhibition, was found in intact conscious sodium-replete rats.

scholarly journals A novel peptide-processing activity of insect peptidyl-dipeptidase A (angiotensin I-converting enzyme): the hydrolysis of lysyl-arginine and arginyl-arginine from the C-terminus of an insect prohormone peptide

1998 ◽  
Vol 330 (1) ◽  
pp. 61-65 ◽  
Author(s):  
R. Elwyn ISAAC ◽  
Liliane SCHOOFS ◽  
A. Tracy WILLIAMS ◽  
Dirk VEELAERT ◽  
Mohammed SAJID ◽  
...  
Keyword(s):  
Neurosecretory Cells ◽  
Single Domain ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Recognition Sequence ◽  
Angiotensin I Converting Enzyme ◽  
C Terminus ◽  
Processing Activity ◽  
Hydrolysis Of

Insect peptidyl-dipeptidase A [angiotensin I-converting enzyme (ACE)] is a soluble single-domain peptidyl-dipeptidase that has many properties in common with the C-domain of mammalian somatic ACE and with the single-domain mammalian germinal ACE. Mammalian somatic ACE is important in blood homoeostasis, but the role of ACE in insects is not known. Immunocytochemistry has been used to localize ACE in the neuroendocrine system of the locust, Locusta migratoria. Staining was observed in five groups of neurosecretory cells in the brain and suboesophageal ganglion, in the nervi corpori cardiaci, the storage part of the corpora cardiaca and in the nervi corpori allati. In three groups of neurosecretory cells, ACE co-localized with locustamyotropins, suggesting a possible role for the enzyme in the metabolism of these neuropeptides. We demonstrate in vitro a novel activity of ACE that removes pairs of basic amino acid residues from a locustamyotropin peptide extended at the C-terminus with either Gly-Lys-Arg or Gly-Arg-Arg, corresponding to a consensus recognition sequence for endoproteolysis of prohormone proteins by prohormone convertases. The low Km and high kcat values (Km 7.3 and 5.0 μM, kcat 226 and 207 s-1 for the hydrolysis of Phe-Ser-Pro-Arg-Leu-Gly-Lys-Arg and Phe-Ser-Pro-Arg-Leu-Gly-Arg-Arg, respectively) obtained for the hydrolysis of these two peptides by insect ACE means that these peptides, along with mammalian bradykinin, are the most favoured in vitro ACE substrates so far identified. The discovery of this in vitro prohormone-processing activity of insect ACE provides a possible explanation for the intracellular co-localization of the enzyme with locustamyotropin peptides, and provides evidence for a new role for ACE in the biosynthesis of peptide hormones and transmitters.

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