scholarly journals The Chemical Compounds of Flacourtia rukam Leaves and Their Inhibition of Angiotensin-converting Enzyme (ACE) Activity

Molekul ◽  
2021 ◽  
Vol 16 (3) ◽  
pp. 219
Author(s):  
Muharni Muharni ◽  
Heni Yohandini ◽  
Elfita Elfita ◽  
Fitrya Fitrya ◽  
Ani Sarah ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Antihypertensive Agent ◽  
Ace Inhibitor ◽  
Chemical Compounds ◽  
Antihypertensive Activity ◽  
Converting Enzyme ◽  
Isolation And Identification ◽  
Ace Activity ◽  
Reported Data ◽  
Ace Inhibitory

Flacourtia  rukam is a plant popular among people to treat hypertension, especially the Musi Banyuasin of south Sumatera, Indonesia. Isolation and identification of chemical compounds from F. rukam leaves and evaluation of their effects on antihypertensive activity have been conducted. Isolation of chemical compounds using chromatographic methods and identification using spectroscopic methods were compared with the reported data. The drug’s effects on antihypertension were determined using the  angiotensin converting enzyme (ACE) inhibitory method. Two compounds were first reported and isolated from the leaves of F. rukam and identified as apigenin (1) and lupeol (2). These compounds were demonstrated to be effective in treating antihypertension with IC50 656.51 ± 1.55 µg/mL for apigenin and 15.12 ± 0.72 µg/mL for lupeol. It can be concluded that  F. rukam leaves is a potential ACE inhibitor can be explored further as an effective antihypertensive agent.

scholarly journals The Potential of Hydrolysate from Rabbit Meat Protein as an Angiotensin Converting Enzyme Inhibitor

2019 ◽  
Vol 43 (1) ◽  
Author(s):  
Edy Permadi ◽  
Jamhari Jamhari ◽  
Edi Suryanto ◽  
Zaenal Bachruddin ◽  
Yuny Erwanto
Keyword(s):  
Molecular Weight ◽  
Angiotensin Converting Enzyme ◽  
Soluble Protein ◽  
Ace Inhibitor ◽  
Water Soluble ◽  
Converting Enzyme ◽  
Soluble Protein Content ◽  
Water Soluble Protein ◽  
Rabbit Meat ◽  
Ace Inhibitory

This research aimed to investigate the rabbit meat hydrolysate potential as an angiotensin-converting enzyme (ACE) inhibitor. Indonesian local rabbit meats were used in this study. The research was conducted in Department of Animal Product Technology, Faculty of Animal Science, Universitas Gadjah Mada, from August 2016 to February 2017. The local rabbit meats were hydrolyzed by pepsin, trypsin, and pancreatic. The obtained hydrolysates were then analyzed to identify the water-soluble protein content. The molecular weight of the hydrolysates were also confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The ACE inhibitory properties of the hydrolysates were analyzed in vitro. The results showed that pepsin, trypsin, and pancreatic hydrolysis showed a significant effect on the water-soluble protein content of rabbit meat (p<0.05). The water-soluble protein of rabbit meat hydrolysed by pepsin, trypsin, and pancreatic were 9.41, 7.66, and 9.75 mg/mL respectively. The molecular weight of the rabbit meat hydrolysate were increased from 10 to 43 kDa; 17 to 43 kDa; and 10 to 43 kDa, after hydrolysed by by pepsin, trypsin, and pancreatic respectively. Furthermore, the ACE inhibitory properties ) of the hydrolysed rabbit meat by pepsin, trypsin, and pancreatic were 439, 170, and 380 μg/mL, respectively. The rabbit meat hydrolysate showed a potential to be ACE inhibitor after hydrolyzed with pepsin, trypsin and pancreatic. Moreover, it also showed a promising potential to be used as bioactive components in different pharmaceutical applications. The highest ACE inhibitory capability was showed on trypsin hydrolysis with the total of 65.45% and 170 μg/mL ACE inhibition

scholarly journals Characterization of angiotensin-converting enzyme in canine testis

Reproduction ◽  
2001 ◽  
pp. 139-146 ◽  
Author(s):  
K Sabeur ◽  
AT Vo ◽  
BA Ball
Keyword(s):  
Enzyme Activity ◽  
Angiotensin Converting Enzyme ◽  
Affinity Chromatography ◽  
Ace Inhibitor ◽  
Specific Activity ◽  
Normal Activity ◽  
Seminiferous Tubules ◽  
Affinity Column ◽  
Converting Enzyme ◽  
Ace Activity

The aim of this study was to characterize angiotensin-converting enzyme (ACE) in canine testis. Detergent-extracted canine testes were sonicated in the presence of protease inhibitors and purified on an affinity column with the ACE inhibitor, lisinopril, as an affinity ligand for ACE. The fractions recovered were assessed for ACE enzyme activity via an enzyme kinetic microplate assay (at 330 nm) based on the hydrolysis of Fa-Phe-Gly-Gly (FAPGG) at pH 7.5 during an 8 min incubation. The specific activity of ACE in the starting testicular extracts was 3.53 +/- 0.99 mU mg(-1) protein with a 1588 times enrichment in ACE activity after lisinopril affinity chromatography (4239 +/- 2600 mU mg(-1) protein). The recovery efficiency of ACE after lisinopril affinity chromatography was 71.2%. The ACE activity in the detergent extracts and the purified fractions was inhibited significantly by 10 micromol captopril l(-1), a specific ACE inhibitor, and was restored to 88% of normal activity by the addition of the thiol-alkylating agent N-ethylmaleimide (0.5 mmol l(-1)) in the detergent extracts and the purified fractions incubated with captopril. The treatment of testicular extracts with 10 mmol EDTA l(-1) reduced the ACE activity significantly (5.40 +/- 1.26 versus 0.58 +/- 0.23 mU mg(-1)). The ACE activity was restored fully in the presence of zinc (5.28 +/- 0.70 mU mg(-1)). The anti-ACE antibody (raised against a 70 kDa protein from the periacrosomal plasma membrane of equine spermatozoa) recognized a 65-70 kDa protein in the detergent-extracted testes as well as in the affinity-purified fractions. This antibody also recognized a protein of similar molecular mass in ejaculated spermatozoa. ACE was localized in the periacrosomal area of the ejaculated spermatozoa and in spermatids in the seminiferous tubules. The results of this study demonstrate that ACE is present in canine testis and retains its enzyme activity after purification with lisinopril affinity chromatography. Activity of canine ACE is inhibited by captopril and EDTA and is restored in the presence of N-ethylmaleimide and zinc.

Antihypertensive effect of an angiotensin converting enzyme inhibitory peptide from enzyme modified cheese

2008 ◽  
Vol 75 (3) ◽  
pp. 284-290 ◽  
Author(s):  
Hidekazu Tonouchi ◽  
Masayuki Suzuki ◽  
Masayuki Uchida ◽  
Munehiro Oda
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Amino Acid Sequences ◽  
Antihypertensive Activity ◽  
Converting Enzyme ◽  
Inhibitory Peptide ◽  
Spontaneously Hypertensive ◽  
Inhibitory Peptides ◽  
Single Oral Administration ◽  
First Time ◽  
Ace Inhibitory

Two angiotensin converting enzyme (ACE)-inhibitory peptides were isolated from enzyme modified cheese (EMC) and their amino acid sequences were identified as Leu-Gln-Pro and Met-Ala-Pro. The EMC was prepared by a combination of Protease N, Umamizyme, and Flavourzyme 500L. Both peptides were derived from β-casein, f 88-90 and f 102-104, respectively. Met-Ala-Pro showed strong ACE inhibitory activity (IC50=0·8 μm) and antihypertensive activity in spontaneously hypertensive rats (SHR) after single oral administration. The IC50 value of Met-Ala-Pro was not affected by pre-incubation with ACE, suggesting that this peptide was a true ACE-inhibitory peptide. We report here, for the first time antihypertensive peptides from EMC.

scholarly journals Spent Hen Protein Hydrolysate with Good Gastrointestinal Stability and Permeability in Caco-2 Cells Shows Antihypertensive Activity in SHR

Foods ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 1384 ◽  
Author(s):  
Hongbing Fan ◽  
Wenlin Yu ◽  
Wang Liao ◽  
Jianping Wu
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Antihypertensive Activity ◽  
Converting Enzyme ◽  
Muscle Proteins ◽  
Ace Inhibitory Activity ◽  
Spent Hen ◽  
Anti Inflammatory ◽  
Ace Inhibitory

Spent hens are a major byproduct of the egg industry but are rich in muscle proteins that can be enzymatically transformed into bioactive peptides. The present study aimed to develop a spent hen muscle protein hydrolysate (SPH) with antihypertensive activity. Spent hen muscle proteins were hydrolyzed by nine enzymes, either individually or in combination; 18 SPHs were assessed initially for their in vitro angiotensin-converting enzyme (ACE) inhibitory activity, and three SPHs, prepared by Protex 26L (SPH-26L), pepsin (SPH-P), and thermoase (SPH-T), showed promising activity and peptide yield. These three hydrolysates were further assessed for their angiotensin-converting enzyme 2 (ACE2) upregulating, antioxidant, and anti-inflammatory activities; only SPH-T upregulated ACE2 expression, while all three SPHs showed antioxidant and anti-inflammatory activities. During simulated gastrointestinal digestion, ACE2 upregulating, ACE inhibitory and antioxidant activities of SPH-T were not affected, but those of SPH-26L and SPH-P were reduced. ACE inhibitory activity of gastrointestinal-digested SPH-T was not affected after the permeability study in Caco-2 cells, while ACE2 upregulating, antioxidant and anti-inflammatory activities were improved; nine novel peptides with five–eight amino acid residues were identified from the Caco-2 permeate. Among these three hydrolysates, only SPH-T reduced blood pressure significantly when given orally at a daily dose of 1000 mg/kg body weight to spontaneously hypertensive rats. SPH-T can be developed into a promising functional food ingredient against hypertension, contributing to a more sustainable utilization for spent hens while generating extra revenue for the egg industry.

scholarly journals Antihypertensive Effects of Corn Silk Extract and Its Novel Bioactive Constituent in Spontaneously Hypertensive Rats: The Involvement of Angiotensin-Converting Enzyme Inhibition

Molecules ◽  
2019 ◽  
Vol 24 (10) ◽  
pp. 1886 ◽  
Author(s):  
Chia-Cheng Li ◽  
Yu-Chen Lee ◽  
Hsin-Yi Lo ◽  
Yu-Wen Huang ◽  
Chien-Yun Hsiang ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Angiotensin Converting Enzyme ◽  
Spontaneously Hypertensive Rats ◽  
Angiotensin Converting Enzyme Inhibition ◽  
Converting Enzyme ◽  
Hypertensive Rats ◽  
Spontaneously Hypertensive ◽  
Corn Silk ◽  
Ace Activity ◽  
Ace Inhibitory

Corn silk tea has been used in folk medicine for anti-hypertensive healthcare. Angiotensin-converting enzyme (ACE) plays a crucial role on the homeostasis of blood pressure. However, effects of corn silk tea on ACE activity and the presence of ACE inhibitory constituents in corn silk are still unknown. Here we applied proteomics and bioinformatics approaches to identify corn silk bioactive peptides (CSBps) that target ACE from the boiling water extract of corn silk (CSE). CSE significantly reduced systolic blood pressure (SBP) levels in spontaneously hypertensive rats and inhibited the ACE activity. By proteomics coupled with bioinformatics analyses, we identified a novel ACE inhibitory peptide CSBp5 in CSE. CSBp5 significantly inhibited the ACE activity and decreased SBP levels in a dose-dependent manner. Docking analysis showed that CSBp5 occupied the substrate-binding channel of ACE and interacted with ACE via hydrogen bonds. In conclusion, we identified that CSE exhibited anti-hypertensive effects in SHRs via the inhibition of ACE, the target of most anti-hypertensive drugs. In addition, an ACE inhibitory phytopeptide CSBp5 that decreased SBP levels in rats was newly identified. Our findings supported the ethnomedical use of corn silk tea on hypertension. Moreover, the identification of ACE inhibitory phytopeptide in corn silk further strengthened our findings.

scholarly journals A clinical dose of angiotensin-converting enzyme (ACE) inhibitor and heterozygous ACE deletion exacerbate Alzheimer's disease pathology in mice

2019 ◽  
Vol 294 (25) ◽  
pp. 9760-9770 ◽  
Author(s):  
Shuyu Liu ◽  
Fujiko Ando ◽  
Yu Fujita ◽  
Junjun Liu ◽  
Tomoji Maeda ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Angiotensin Converting Enzyme ◽  
Amyloid Precursor Protein ◽  
Ace Inhibitors ◽  
Ace Inhibitor ◽  
Precursor Protein ◽  
Causative Role ◽  
Converting Enzyme ◽  
Clinical Dose

Inhibition of angiotensin-converting enzyme (ACE) is a strategy used worldwide for managing hypertension. In addition to converting angiotensin I to angiotensin II, ACE also converts neurotoxic β-amyloid protein 42 (Aβ42) to Aβ40. Because of its neurotoxicity, Aβ42 is believed to play a causative role in the development of Alzheimer's disease (AD), whereas Aβ40 has neuroprotective effects against Aβ42 aggregation and also against metal-induced oxidative damage. Whether ACE inhibition enhances Aβ42 aggregation or impairs human cognitive ability are very important issues for preventing AD onset and for optimal hypertension management. In an 8-year longitudinal study, we found here that the mean intelligence quotient of male, but not female, hypertensive patients taking ACE inhibitors declined more rapidly than that of others taking no ACE inhibitors. Moreover, the sera of all AD patients exhibited a decrease in Aβ42-to-Aβ40–converting activity compared with sera from age-matched healthy individuals. Using human amyloid precursor protein transgenic mice, we found that a clinical dose of an ACE inhibitor was sufficient to increase brain amyloid deposition. We also generated human amyloid precursor protein/ACE+/− mice and found that a decrease in ACE levels promoted Aβ42 deposition and increased the number of apoptotic neurons. These results suggest that inhibition of ACE activity is a risk factor for impaired human cognition and for triggering AD onset.

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