• Journal of Veterinary Science
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• v.24 no.2
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• pp.26.1-26.11
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• 2023

Background: Angiotensin-converting enzyme inhibitor (ACEi) inhibits the catalysis of angiotensin I to angiotensin II and the degradation of substance P (SP) and bradykinin (BK). While the possible relationship between ACEi and SP in nociceptive mice was recently suggested, the effect of ACEi on signal transduction in astrocytes remains unclear. Objectives: This study examined whether ACE inhibition with captopril or enalapril modulates the levels of SP and BK in primary cultured astrocytes and whether this change modulates PKC isoforms (PKCα, PKCβI, and PKCε) expression in cultured astrocytes. Methods: Immunocytochemistry and Western blot analysis were performed to examine the changes in the levels of SP and BK and the expression of the PKC isoforms in primary cultured astrocytes, respectively. Results: The treatment of captopril or enalapril increased the immunoreactivity of SP and BK significantly in glial fibrillary acidic protein-positive cultured astrocytes. These increases were suppressed by a pretreatment with an angiotensin-converting enzyme. In addition, treatment with captopril increased the expression of the PKCβI isoform in cultured astrocytes, while there were no changes in the expression of the PKCα and PKCε isoforms after the captopril treatment. The captopril-induced increased expression of the PKCβI isoform was inhibited by a pretreatment with the neurokinin-1 receptor antagonist, L-733,060, the BK B1 receptor antagonist, R 715, or the BK B₂ receptor antagonist, HOE 140. Conclusions: These results suggest that ACE inhibition with captopril or enalapril increases the levels of SP and BK in cultured astrocytes and that the activation of SP and BK receptors mediates the captopril-induced increase in the expression of the PKCβI isoform.

• Journal of Microbiology and Biotechnology
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• v.12 no.1
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• pp.59-64
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• 2002

An angiotensin I-converting enzyme (EC 3.4.15.1) (ACE), which can convert inactive angiotensin I into angiotensin II, a vasoconstrictor, is one of the key enzymes in controlling hypertension. It is suggested that the inhibition of ACE prevents hypertension, and many inhibitory peptides have already been reported. In the current study, oligonucleotides encoding ACE inhibitory peptides (IY, VKY) were chemically synthesized and designed to be multimerised due to isoschizomer sites (BamHI, BglII). The cloned gene named AP3 was multimerised up to 6 times in pBluescript and expressed in BL2l containing pGEX-KG. The fusion protein (GST-AP3) was easily purified with a high recovery by an affinity resin, yielding 38 mg of synthetic AP3 from a 1-1 culture. The digestion of AP3 by chymotrypsin exhibited an $IC_50$ value of $18.53{\mu}M$. In conclusion, the present experiment indicated that AP3 could be used as a dietary antihypertensive drug, since the potent ACE inhibitory activity of AP3 could be activated by chymotrypsin in human intestine.

• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.4
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• pp.719-725
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• 2000

This study focused on the purification and characterization of ACE inhibitor from Porphyra yezoensis. The dried Porphyra yezoensis was ground and hydrolyzed with 2.5 N HCl, followed by neutralization and centrifugation. Then, the subsequential purification of ACE inhibitor was carried out by Amberlite XAD 8, DEAE-Toyopearl 650C, Sephadex LH-20 column chromatography and reverse phase HPLC with C18 column. The purified ACE inhibitor was peptide which consisted of glycine (24.5%), arginine (56.8%) and proline (18.8%). Also, it showed the competitive inhibition pattern to ACE. The apparent molecular mass of purified peptide was 580 dalton, and an IC50 value of ACE inhibitor was 10.6 $\mu\textrm{g}$.

• Journal of Physiology & Pathology in Korean Medicine
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• v.23 no.1
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• pp.93-96
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• 2009

This study was attempted to investigate the anti-hypertensive activity of Solanum tuberosum, cv. Gui valley. Ethanol extract of Gui vally (EGV) increased free radical scarvenge activity up to 91.6% of control at $200{\mu}g/m{\ell}$. It's anti-oxidant activity is similar to 10 uM of ascorbic acid, well known as antioxidant. EGV inhibited Angiotensin-I-converting enzyme (ACE) activity in vitro. ACE plays a important role in regulation of blood pressure and ACE inhibitors are important for the treatment of hypertension. Anti-hypertensive activity of EGV in vivo was assessed in lead acetate (LAT)-induced hypertensive rats for 8 weeks. Elevated blood pressure in control group was significantly decreased by EGV at 200 mg/kg. Also, ACE activity in blood was also suppressed by EGV treatment. Taken together, these results suggest that EGV has an anti-hypersive activity via inhibition of ACE and can be used for the treatment or prevention of hypertension.

• Food Science and Biotechnology
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• v.17 no.4
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• pp.873-877
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• 2008

Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.

• The Korean Journal of Food And Nutrition
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• v.33 no.2
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• pp.167-173
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• 2020

To increase the functional material content of soybean, a repetitive steaming and drying process was used. We investigated the changes in the total polyphenol content, the antioxidant activity, and the angiotensin-I converting enzyme (ACE) inhibition in soybean following nine rounds of steaming and drying. Soybean was steamed 9 times for 2 h and then dried 9 times from 55℃ to 73℃ for 3 h. The total polyphenol content in the soybean reached a maximum value of 60.47 mg GAE eq./100 g at 73℃ while the total polyphenol content in the raw soybean reached 25.17 mg GAE eq./100 g. In the raw soybean samples, the DPPH radical scavenging activity (5 mg/mL) was 8.04% but it increased by 43.29% after drying 9 times to 73℃. ABTS radical scavenging activity also improved following 9 rounds of steaming and drying. ACE inhibitory activity of the soybean dried 9 times at 73℃ was 58.94% at 10 mg/mL. These results showed that steaming and drying soybean 9 times enhanced the antioxidant activity and the ACE inhibitory activity of soybean. Therefore, more research on the biological and anti-hypertensive activity of soybean using this steaming and drying method is necessary.

• Fisheries and Aquatic Sciences
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• v.14 no.4
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• pp.283-288
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• 2011

The jellyfish Nemopilema nomurai was hydrolyzed with papain and a novel dipeptide purified via ultrafiltration, gel filtration chromatography with Sephadex LH-20, and reverse phase chromatography using $C_{18}$ and $C_{12}$ columns. The IR, 1H NMR, 13C NMR, and MS spectrometer analyses showed that the dipeptide comprised tyrosine-isoleucine (Tyr-Ile). The $IC_{50}$ and $K_i$ values were $6.56{\pm}1.12$ and $3.10{\pm}0.28\;{\mu}M$, respectively, indicating competitive inhibition of angiotensin-I-converting enzyme (ACE). As a novel ACE-inhibitory active peptide, Tyr-Ile may have potential for use in antihypertensive therapy.

• Journal of Microbiology and Biotechnology
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• v.25 no.8
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• pp.1315-1320
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• 2015

To enhance the γ-aminobutyric acid (GABA) content, the optimized fermentation of soybean with added sea tangle extract was evaluated at 30℃ and pH 5.0. The medium was first inoculated with Aspergillus oryzae strain FMB S46471 and fermented for 3 days, followed by the subsequent inoculation with Lactobacillus brevis GABA 100. After fermentation for 7 days, the fermented soybean showed approximately 1.9 g/kg GABA and exhibited higher ACE inhibitory activity than the traditional soybean product. Furthermore, several peptides in the fraction containing the highest ACE inhibitory activity were identified. The novel fermented soybean enriched with GABA and ACE inhibitory components has great pharmaceutical and functional food values.

• Korean Journal of Food Science and Technology
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• v.27 no.6
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• pp.978-984
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• 1995

This study was conducted to investigate the physiological functionality of the hot water and 70% acetone extracts obtained from the pine needle and mugwort. Flavanol tannin content was above 60% of the total polyphenol in pine needle extracts. 70% Acetone extract from pine needle exhibited inhibition percentage of about 82.2% on the mutagenicity of Trp-P-1. Angiotensin I converting enzyme(ACE) inhibition activity was 61% and 50% in the hot water extract and in the 70% acetone extract respectively. Electron donating ability(EDA) of the hot water and 70% acetone extracts obtained from the pine needle was significantly good above 80%. 70% Acetone extract from pine needle showed inhibitary effect against the polyphenol oxidase(PPO) of water dropwort. The nitrite scavenging ability was appeared in all the extracts examined and it showed $80{\sim}90%$ at pH 3.0. The oxidative stability was determined by POV. Results showed that ethyl acetate fraction is better antioxidants than chloroform and butanol fractions in the soybean oil. Then, in the mugwort extracts, antimutagenicity of 70% acetone extract was similar to that of pine needle. Ratio of ACE inhibition activity was higher than that of pine needle extracts. EDA of hot water and 70% acetone extracts was 45%. Extracts from the mugwort were lower in nitrite scavenging ability about $20{\sim}30%$ than extracts from pine needle.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.1
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• pp.8-13
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• 2010

The angiotensin converting enzyme (ACE) inhibition effect of soybean protein isolate hydrolysate was studied using protease. Soybean protein isolate was hydrolysed by seven enzymes (Alcalase 2.4 L, Flavourzyme 500 MG, GC 106, Multifect Neutral, Neutrase 0.8 L, Papain 30,000 and Protamex), enzyme concentrations (0, 0.5, 1.0 and 1.5%), at various hydrolysis times (0, 1, 2, 3, 4, 5 and 6 hr) and suspension concentrations (1, 5, 7, 10 and 15%). Absorbance at 280 nm, brix and ACE inhibitory activity of soybean protein isolate hydrolysates were investigated. Absorbance at 280 nm and brix of Alcalase 2.4 L treatment were higher than other enzyme treatments. The optimum condition of hydrolysis was Alcalase 2.4 L, 1% enzyme concentration, 5% suspension concentration for 4 hr. $IC_{50}$ value of ACE inhibitory activity of soybean protein isolate hydrolysate was $79.94 {\mu}g/mL$. These results suggest that soybean isolate protein hydrolysate from Alcalase 2.4 L may be of benefit for developing antihypertensive therapeutics.