Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0020538 (hypertension)
 170,190 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This paper evaluates the effect of the long-term intake of a hydrolysate of egg white with pepsin (HEW), with a potent angiotensin converting enzyme inhibitory activity, on the development of hypertension of spontaneously hypertensive rats (SHR). After being weaned, male 3-week-old SHR were randomly divided into five groups that were given until the 20th week of life the following drinking fluids: (1) tap water, (2) non-treated egg white 1 g/kg/day, (3) captopril 100 mg/kg/day, (4) HEW 0.5 g/kg/day, and (5) HEW 1 g/kg/day. From the 20th to 25th week of life, animals from all groups were given tap water. Systolic blood pressure (SBP) and diastolic blood pressure (DBP) were measured weekly in the rats, from the 6th to 25th week of life, by the tail cuff method. Development of hypertension was attenuated in the groups treated with captopril and HEW (P<0.001 vs. the group that drunk tap water). At the 20th week of life, the arterial blood pressure values of the different groups of rats were: tap water (SBP = 219.5 +/- 5.7, DBP = 167 +/- 3.7), non-treated egg white (SBP = 206.4 +/- 1.43, DBP = 166.4 +/- 4.9), captopril (SBP = 131.7 +/- 2.74, DBP = 91.5 +/- 1.62), HEW 0.5 g/kg/day (SBP = 182.9 +/- 4.64, DBP = 127.5 +/- 2.1) and HEW 1 g/kg/day (SBP = 177.7 +/- 4.72, DBP = 120.1 +/- 2.4). SBP and DBP increased in the treated SHR when the corresponding antihypertensive treatment was removed. In spite of this, SBP remained lower in the SHR that had received captopril and HEW than in the SHR of the control groups (P<0.05). The present results suggest that HEW could be used as a functional food with antihypertensive activity.
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PMID:Long-term intake of egg white hydrolysate attenuates the development of hypertension in spontaneously hypertensive rats. 1638 62

Food-derived bioactive peptides with ACE-inhibitory properties are receiving special attention due to their beneficial effects in the treatment of hypertension. In this work we evaluate the impact of a simulated gastrointestinal digestion on the stability and activity of two bioactive peptides that derive from ovalbumin by enzymatic hydrolysis, YAEERYPIL and RADHPFL. These peptides possess in vitro ACE-inhibitory activity and antihypertensive activity in spontaneously hypertensive rats (SHR). The results showed that YAEERYPIL and RADHPFL were susceptible to proteolytic degradation after incubation with pepsin and a pancreatic extract. In addition, their ACE-inhibitory activity in vitro decreased after the simulated digestion. The antihypertensive activity on SHR of the end products of the gastrointestinal hydrolysis, YAEER, YPI, and RADHP, was evaluated. The fragments YPI and RADHP significantly decreased blood pressure, 2 h after administration, at doses of 2 mg/kg, but they probably did not exert their antihypertensive effect through an ACE-inhibitory mechanism. It is likely that RADHP is also the active end product of the gastrointestinal digestion of the antihypertensive peptides FRADHPFL (ovokinin) and RADHPF (ovokinin 2-7).
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PMID:Effect of simulated gastrointestinal digestion on the antihypertensive properties of ACE-inhibitory peptides derived from ovalbumin. 1644 75

There have been studies of antihypertensive peptides derived from food proteins, but very few described the production of bioactive peptides from egg proteins. The first 2 antihypertensive peptides isolated in egg were obtained by enzymatic hydrolysis of ovalbumin. They correspond to the sequences Phe-Arg-Ala-Asp-His-Pro-Phe-Leu (ovokinin) and Arg-Ala-Asp-His-Phe-Leu (ovokinin 2-7). Both exhibited endothelium-dependent vasodilatory activity. Ovokinin (2-7) had higher antihypertensive potency than ovokinin in spontaneously hypertensive rats (SHR). Modifications in the sequence of ovokinin (2-7) improved the bioavailability of this peptide. It was also demonstrated that different ovalbumin hydrolysates can inhibit angiotensin I-converting enzyme (ACE). We recently obtained an egg white hydrolysate that inhibited the enzyme in vitro. It was obtained by treating egg white with pepsin and it exhibited antihypertensive activity in SHR. Some ACE-inhibitory peptides obtained from this hydrolysate (Tyr-Arg-Glu-Glu-Arg-Tyr-Pro-Ile-Leu, Arg-Ala-Asp-His-Pro-Phe-Leu, and Ile-Val-Phe) also showed antihypertensive activity in these rats. The egg products mentioned could be used as functional food ingredients with potential therapeutic benefit in the prevention and treatment of hypertension.
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PMID:Antihypertensive peptides derived from egg proteins. 1670 3

Angiotensin I converting enzyme (ACE) inhibitory peptide was isolated from tuna dark muscle hydrolysate prepared by alcalase, neutrase, pepsin, papain, alpha-chymotrypsin, and trypsin, respectively. Among hydrolysates, the pepsin-derived hydrolysate exhibited the highest ACE I inhibitory activity versus those of other enzyme hydrolysates. The structure of the peptide was identified to be Trp-Pro-Glu-Ala-Ala-Glu-Leu-Met-Met-Glu-Val-Asp-Pro (molecular weight 1581 Da) by time of flight mass spectrometry/mass spectrometry analysis, and the IC 50 value of the peptide was 21.6 microM. The Lineweaver-Burk plots revealed that the peptide acts as a noncompetitive inhibitor, and the inhibitor constant ( K i) was calculated as 26.6 microM using the secondary plots. The peptide had an antihypertensive effect according to the time-course measurement after oral administration to spontaneously hypertensive rats. Maximal reduction was detected 3 h after oral administration at a dose of 10 mg/kg of body weight. These results suggest that the peptide derived from tuna dark muscle would be a beneficial ingredient for functional food or pharmaceuticals against hypertension and its related diseases.
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PMID:Antihypertensive effect of angiotensin i converting enzyme-inhibitory peptide from hydrolysates of Bigeye tuna dark muscle, Thunnus obesus. 1789 58

Lyophylized antler powder was hydrolyzed by pepsin and trypsin separately and also simultaneously to give hydrolysates with special physical activities. Complete hydrolysis peptides with MW lower than 1 x 10(3) were collected for assay of angiotensin I-converting enzyme (ACE) inhibitory activity, antioxidant activity and proliferative activity toward UMR-106 osteoblast cells. The results of the experiments revealed that all hydrolysates exhibited potent hydroxyl radical scavenging activity with an IC50 value less than 1 mg/ml which was much lower than the value of 5.5 g x L(-1) for vitamin C. The peptic and peptic tryptic hydrolysates demonstrated strong angiotensin I-converting enzyme (ACE) inhibitory activity. The tryptic hydrolysate increased the proliferation of the UMR-106 cells by 73.43%. The results verified the traditional use of antler in bone-strengthening, anti-aging. The exploratory studies on the ACE inhibitory activity of antler hydrolysates indicated that the hydrolysates might be potentially useful in prevention and treatment of hypertension. Further purification of peptides contributing to the antioxidant activity, angiotensin I-converting enzyme-inhibitory activity and proliferative activity toward osteoblasts from antler hydrolysates is warranted.
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PMID:[Enzymatic hydrolysis of antler and properties of hydrolysates]. 2117 80

A peptide possessing antihypertensive activity was purified from Nile tilapia ( Oreochromis niloticus ) gelatin using alcalase, Pronase E, pepsin, and trypsin. Among them, the alcalase hydrolysate exhibited the highest angiotensin converting enzyme (ACE) inhibitory activity. Therefore, it was further analyzed, and a potent ACE inhibitory peptide of DPALATEPDPMPF (1382 Da) was separated and purified. In addition, the protective effect of the purified peptide against free radical-induced cellular and DNA damage in murine microglial cells (BV-2) was determined. These results suggest that the peptide isolated from Nile tilapia (O. niloticus) gelatin acts as a candidate against hypertension and oxidative stress and could be used in health-functional foods.
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PMID:An antihypertensive peptide from tilapia gelatin diminishes free radical formation in murine microglial cells. 2200 28

Peptides inhibiting angiotensin-I converting enzyme (ACE, EC. 3.4.15.1) are possible cures of hypertension. Food-derived ACE-inhibitory peptides are particularly attractive because of reduced side effects. Previously, we reported ACE-inhibitory activity of grass carp protein hydrolysates. In this work, we report steps for purifying the ACE-inhibitory peptide from the hydrolysate and its biochemical properties. Following steps of ultrafiltration, macroporous adsorption resin, and two steps of reversed phase high performance liquid chromatography (RE-HPLC), a single Val-Ala-Pro (VAP) tripeptide was identified. The tripeptide with excellent ACE-inhibitory activity (IC(50) value of 0.00534 mg/mL) was a competitive ACE inhibitor and stable against both ACE and gastrointestinal enzymes of pepsin and chymotrypsin. This is the first report of food-derived VAP. The identified unique biochemical properties of VAP may enable the application of grass carp protein hydrolysates as a functional food for treatments of hypertension. The developed purification conditions also allow the production of VAP for pharmaceutical applications.
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PMID:Purification and characterization of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide derived from enzymatic hydrolysate of grass carp protein. 2210 May 19

Angiotensin-converting enzyme (ACE) inhibitory, antihypertensive and antihyperlipidaemic activities of protein hydrolysates (RPH) from the jellyfish Rhopilema esculentum were investigated. R. esculentum was hydrolysed sequentially with pepsin and papain, and then the hydrolysate was ultrafiltered with a 2000 Da cut-off membrane. It was found that RPH contained high levels of Gly, Glu, Pro, Asp and Ala, having potential ACE inhibitory activity in vitro with an IC(50) of 1.28 mg/ml. It was also found that systolic blood pressure was reduced markedly in spontaneously hypertensive rats after single and chronic oral administration of RPH, indicating that RPH had an antihypertensive effect. In addition, oral administration of RPH decreased total serum cholesterol and triglyceride, and increased high-density lipoprotein cholesterol in rats fed with high-fat diet. These results indicate that RPH may prove to be a promising functional food for the prevention and treatment of hypertension and hyperlipidaemia.
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PMID:Angiotensin converting enzyme (ACE) inhibitory, antihypertensive and antihyperlipidaemic activities of protein hydrolysates from Rhopilema esculentum. 2344 66

Angiotensin-I-converting enzyme (ACE-I, EC 3.4.15.1), renin (EC 3.4.23.15), and dipeptidyl peptidase-IV (DPP-IV, EC 3.4.14.5) play key roles in the control of hypertension and the development of type-2 diabetes and other diseases associated with metabolic syndrome. The aim of this work was to utilize known in silico methodologies, peptide databases and software including ProtParam (http://web.expasy.org/protparam/), Basic Local Alignment Tool (BLAST), ExPASy PeptideCutter (http://web.expasy.org/peptide_cutter/) and BIOPEP (http://www.uwm.edu.pl/biochemia/index.php/pl/biopep) to assess the release of potentially bioactive DPP-IV, renin and ACE-I inhibitory peptides from bovine and porcine meat proteins including hemoglobin, collagen and serum albumin. These proteins were chosen as they are found commonly in meat by-products such as bone, blood and low-value meat cuts. In addition, the bioactivities of identified peptides were confirmed using chemical synthesis and in vitro bioassays. The concentration of peptide required to inhibit the activity of ACE-I and DPP-IV by 50% was determined for selected, active peptides. Novel ACE-I and DPP-IV inhibitory peptides were identified in this study using both in silico analysis and a literature search to streamline enzyme selection for peptide production. These novel peptides included the ACE-I inhibitory tri-peptide Ile-Ile-Tyr and the DPP-IV inhibitory tri-peptide Pro-Pro-Leu corresponding to sequences f (182-184) and f (326-328) of both porcine and bovine serum albumin which can be released following hydrolysis with the enzymes papain and pepsin, respectively. This work demonstrates that meat proteins are a suitable resource for the generation of bioactive peptides and further demonstrates the usefulness of in silico methodologies to streamline identification and generation of bioactive peptides.
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PMID:Identification of novel dipeptidyl peptidase-IV and angiotensin-I-converting enzyme inhibitory peptides from meat proteins using in silico analysis. 2502 Feb 48

Recent studies have investigated anti-hypertensive peptides derived from natural food products. In this work, we focus on Phascolosoma esculenta as a resource of anti-hypertensive peptides, which is also a seafood with high nutritive value. Compared with FAO/WHO requirements, P. esculenta was confirmed to contain high contents of amino acids and minerals. To investigate the anti-hypertensive activity of P. esculenta, water-soluble and insoluble proteins were extracted and hydrolysed by pepsin and trypsin, respectively. The hydrolysates of water-soluble proteins derived by pepsin and pepsin-trypsin exhibited angiotensin-converting enzyme (ACE) inhibitory activity with IC50 values of 0.67 and 0.24 mg ml(-1), respectively, and those of water-insoluble proteins presented IC50 values of 0.4 and 0.1 mg ml(-1), respectively. Experiments on 'spontaneously hypertensive rats' (SHRs) were carried out to test the anti-hypertension activity in vivo, which confirmed that the hydrolysates played a significant role in reducing both diastolic blood pressure (DBP) and systolic blood pressure (SBP). Consistently, the in vivo anti-hypertensive activity of the hydrolysis products of pepsin and trypsin used together was also higher than that by using pepsin hydrolysis products alone. As stated in both sets of results, we believe that P. esculenta is an excellent resource of antihypertensive peptides and warrants further investigation.
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PMID:The nutritional composition and anti-hypertensive activity on spontaneously hypertensive rats of sipuncula Phascolosoma esculenta. 2507 55


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