• 제목/요약/키워드: Angiotensin converting enzyme 2

검색결과 472건 처리시간 0.024초

Upregulation of Renal Renin-Angiotensin System in Rats with Adriamycin-Induced Nephrosis

  • Kim, Soo-Wan;Lee, Jong-Un;Han, Sang-Woong;Ryu, Jun-Ho;Oh, Yoon-Wha;Kim, Nam-Ho;Choi, Ki-Chul;Kim, Ho-Jung
    • The Korean Journal of Physiology and Pharmacology
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    • 제6권2호
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    • pp.127-130
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    • 2002
  • The present study was aimed to investigate whether the adriamycin-induced nephrosis is associated with an altered regulation of local renin-angiotensin system (RAS) in the kidney. Rats were subjected to a single injection of adriamycin (2 mg/kg body weight, IV) and kept for 6 weeks to allow the development of nephrosis. They were then divided into two groups, and supplied with and without cilazapril, an angiotensin converting enzyme (ACE) inhibitor, in drinking water (100 mg/l) for additional 6 weeks. Another group without adriamycin-treatment served as control. The mRNA expression of renin, ACE, type 1 and type 2 angiotensin II receptors (AT1R, AT2R), and transforming growth factor $(TGF)-{\beta}1$ was determined in the cortex of the kidney by reverse transcription-polymerase chain reaction. Adriamycin treatment resulted in heavy proteinuria. Accordingly, the mRNA expression of renin, ACE, and AT1R was increased in the renal cortex, while that of AT2R was decreased. Co-treatment with cilazapril attenuated the degree of proteinuria. While not affecting the altered expression of renin, cilazapril decreased the expression of ACE to the control level. Cilazapril further increased the expression of AT1R, while it restored the decreased expression of AT2R. The expression of $(TGF)-{\beta}1$ was increased by the treatment with adriamycin, which was abolished by cilazapril. An altered expression of local RAS components may be causally related with the development of adriamycin-induced nephrosis, in which AT1R is for and AT2R is against the development of nephrosis.

김 가수분해물로부터 Angiotensin-I Converting Enzyme저해 Peptide의 분리$\cdot$정제 (Separation and Purification of Angiotensin-I Converting Enzyme Inhibitory Peptides from Layer Hydrolysate)

  • 이헌옥;김동수;도정룡;권대영
    • 한국수산과학회지
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    • 제34권2호
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    • pp.164-172
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    • 2001
  • 본 연구는 김의 Maxazyme NNP 가수분해물로부터 여러 단계의 column chromatography 및 HPLC를 통해 ACE 저해 peptide를 분리, 정제하여 이의 분자량과 amino acid sequence를 분석하였다. ACE 저해 효과가 큰 저분자 peptide의 함량이 많은 가수분해물을 얻기 위한 최적의 단백질 가수분해 효소를 선정하기 위하여 시험한 결과, Maxazyme NNP에 의한 가수분해물의 ACE 저해효과가 $37.2\%$로 가장 높게 나타났다 김의 효소 가수분해물로부터ACE 저해 peptide만을 효율적으로 분리하기 위한 추출 조건 시험에서, 색소 제거를 위해서는 diethylether 처리가, 다당류 및 고분자 단백질 제거를 위해서는 $70\%$ ethanol 처리가 각각 선정되었다. 김 가수분해물로부터 ACE 저해 peptide를 분리, 정제하기 위한 첫 단계로 ultrafiltration을 한 결과, 분자량 3,000 이하 분획물의 ACE 저해 효과가 $69.4\%$로 가장 높았으며, 이 분획물을 gel filtration chromatography (Sephadex G-25) , reverse-phase HPLC (ODS & Vydac C-18) 및 gel permeation chromatography (Superdex Peptide HR)와 같은 단계별 column chromatography를 행하여 최종적으로 단일 peptide peak들을 분리하였다. 이들 단일 peptide peak들의 분자량을 Electrospray-Mass Spectrometer로 측정한 결과, 각각 413.48 (S1O2V2V1P),346.86 (S1O2V2V2P) 그리고 320.32 (S2O6V3V1P) dalton이었으며, 이들 peptide의 amino acid sequence는 N-말단으로부터 아미노산 잔기를 분석한 결과, 각각 Val-Gln-Gly-Asn, Thr-Glu-Thr 및 Phe-Arg으로 확인되었다.

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Antioxidant and Angiotensin I Converting Enzyme Inhibitory Activities of Red Snow Crab Chionoecetes japonicas Shell Hydrolysate by Enzymatic Hydrolysis

  • Yoon, Na Young;Shim, Kil-Bo;Lim, Chi-Won;Kim, Sang-Bo
    • Fisheries and Aquatic Sciences
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    • 제16권4호
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    • pp.237-242
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    • 2013
  • We investigated the antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of red snow crab Chionoecetes japonicas shell (RSCS) hydrolysate by enzymatic hydrolysis and its molecular weight cut-off fractions. The RSCS hydrolysate was fractionated through two ultrafiltration membranes of 3 and 10 kDa cut-offs. Three fractions (<3 kDa, 3-10 kDa, and >10 kDa) were evaluated for total amino acid composition, antioxidant activities using 2'-azino-bis[3-ethylbenzthiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities and reducing power assays, and ACE inhibitory activity using Hou's method. Although all fractions showed activity, the <3 kDa fraction of RSCS hydrolysate exhibited the greatest $ABTS^+$ radical scavenging, SOD-like and ACE inhibitory activities. However, these fractions exhibited low reducing power. These results suggest that the low-molecular-weight enzymatic hydrolysate of RSCS could be used as a functional ingredient to control oxidative stress and ACE activity.

Hypoglycemic and Angiotension Converting Enzyme Inhibitory Effect of Water and Ethanol Extracts from Haesongi Mushroom (Hypsizigus marmoreus)

  • Jung, Eun-Bong;Jo, Jin-Ho;Cho, Seung-Mock
    • Food Science and Biotechnology
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    • 제18권2호
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    • pp.541-545
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    • 2009
  • Water and ethanol extracts were prepared from the haesongi mushroom (Hypsizigus marmoreus) to measure functional components. The ability of the extracts to inhibit angiotensin-converting enzyme (ACE) and their hypoglycemic effects were also determined; the latter was measured by $\alpha$-amylase and glucosidase inhibition. Extraction yield, protein content, total phenol, and $\beta$-glucan in the water extracts were 55.86, 17.71, 1.89, and 21.93%, respectively. The respective values for the ethanol extracts were lower than those for water extracts. Both water and ethanol extracts showed dosedependent ACE inhibition, the effect of the former being greater. The water extract inhibited ACE activity by 95.34% at 40 mg/mL. The $IC_{50}$ values of the water extracts were 63.32 and 0.41 mg/mL for $\alpha$-amylase and glucosidase, respectively. Thus, the water extracts had a greater hypoglycemic effect than the ethanol extracts. From these results, water is a better solvent than ethanol to extract from the haesongi mushroom functional components that show ACE inhibition and have hypoglycemic effects.

Biological Activities of Non-saponin Compounds Isolated from Korean Red Ginseng

  • Okuda, Hiromichi;Lee, Sung-Dong;Matsuura, Yukinaga;Zheng, Yinan;Sekiya, Keizo;Takeshi, Takaku;Kameda, Kenji;Hirose, Kumi;Ohtani, Kazuhiro;Tanaka, Osamu;Sakata, Toshiie
    • 고려인삼학회:학술대회논문집
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    • 고려인삼학회 1990년도 Proceedings of International Symposium on Korean Ginseng, 1990, Seoul, Korea
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    • pp.15-19
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    • 1990
  • We have been isolating various physiologically active substances from non-saponin fraction of Korean Red Ginseng These are adenosine, gyro-glutamic acid, dencichine and acidic polysaccharide. Adenosine and gyro-glutamic acid are loom to inhibit epinephrine-induced lipolysis in fat cells and stimulate the insulin-mediated lipogenesis. In addition to these actions, adenosine was found to inhibit both norepinephrine- and histamine-induced aorta constriction, and pyre·glutamic acid inhibits angiotensin-converting enzyme. Dencichine stimulated histamine-induced aorta constriction. Finally, acidic polysaccharide was found to inhibit both lipolytic and anorexigenic actions of Toxohormone-L. Based on these experimental results, I presented a brief review on these compounds isolated from non- saponin fraction of Korea Red Ginseng. Keywords Panax ginseng, Korean red ginseng, adenosine, pyroglutamic acid, dencichine, acidic polysac- charide, lipolysis, lipogenesis, angiotensin-converting enzyme, toxohormone-L.

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Assessment of the Inhibitory Activity of Peptide Extracts from Hanwoo Musculus Longissimus on Angiotensin I-Converting Enzyme

  • Seol, Kuk-Hwan;Song, Ji-Hye;Prayad, Thirawong;Kim, Hyoun-Wook;Jang, Ae-Ra;Ham, Jun-Sang;Oh, Mi-Hwa;Kim, Dong-Hun;Lee, Moo-Ha
    • 한국축산식품학회지
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    • 제31권5호
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    • pp.663-667
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    • 2011
  • This study was performed to measure the angiotensin I-converting enzyme (ACE) inhibitory activity of peptide extracts derived from the enzymatic proteolysis of Hanwoo Musculus longissimus (M. longissimus) during cold storage. Thermolysin (80 ppm, w/w) and protease type XIII (100 ppm, w/w) were injected separately or in combination for the enzymatic proteolysis of sarcoplasmic and myofibrillar proteins prior to storage at $5^{\circ}C$ (T1) or at $-1^{\circ}C$ (T2) in a chilling room for 9 days. Beef injected with thermolysin (E2) and thermolysin+protease type XIII (E3) showed a significantly higher degree of hydrolysis at both storage temperatures (p<0.05). During the storage period, T1E2 at day 6 and T1E3 at day 9 showed the strongest ACE inhibitory activity with sarcoplasmic and myofibrillar protein proteolysates. Macromolecules greater than 10,000 Da were removed by ultra filtration, and the filtrates were separated into fractions using gel filtration. Five and three major fractions were collected from S-T1E2-6 and M-T1E3-9 extracts, respectively, and the $4^{th}$ fraction of the S-T1E2-6 extracts showed the highest ACE inhibitory rate of $61.96{\pm}7.41%$.

국산 홍합과 뉴질랜드 초록입 홍합 열수 추출물의 알코올분해효소 활성에 미치는 영향 및 DPPH 라디칼 소거능과 Angiotensin Converting Enzyme 저해 활성 (Effects of Hot Water Extracts of Domestic Blue Mussel and New Zealand Green Lipped Mussel on Alcohol Metabolizing Enzymatic, DPPH Radical Scavenging, and Angiotensin Converting Enzyme Inhibitory Activities)

  • 김시경;옥둘이;박은주;이승철
    • 한국식품영양과학회지
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    • 제43권9호
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    • pp.1363-1368
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    • 2014
  • 우리나라 남해안 연안에서 주로 양식되는 진주담치(국산 홍합)와 세계적으로 기능성이 잘 알려진 뉴질랜드 초록입 홍합의 열수 추출물을 제조하여 생리활성을 비교하였다. 모든 홍합 추출물들은 알코올대사와 관련한 alcohol dehydrogenase(ADH)와 acetaldehyde dehydrogenase(ALDH)의 활성을 상승시켰으며, 특히 ADH의 활성을 크게 향상시켰다. 국산 홍합의 육질 추출물은 초록입 홍합의 육질 추출물에 비하여 ADH 상승 효과는 비슷하였으며, ALDH 상승 효과는 약간 낮았다. DPPH 라디칼 소거능으로 조사한 항산화능은 국산 홍합의 육질 추출물이 초록입 홍합의 육질 추출물 보다 높았다. 항고혈압과 관련한 ACE 저해능의 경우에는 국산 홍합 육질 추출물이 초록입 홍합의 육질 추출물에 비해 10 mg/mL 농도에서는 낮았으나 20 mg/mL 이상의 농도에서는 유의차(P<0.05)를 보이지 않았다. 이상의 결과는 국내에서 양식되고 있는 홍합도 세계적으로 초록입 홍합에 못지않은 생리활성을 가지고 있음을 시사한다.

Epoxyalkanoyls as Novel ACE Inhibitors

  • P. Choo, Hea-Young;Yoon, Hea-Ran;Park, Hwha-Soon;Kim, Dong-Hyun;Park, Jong-Sei;Kim, Dong-H.
    • Archives of Pharmacal Research
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    • 제21권2호
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    • pp.168-173
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    • 1998
  • The epoxyalkanoyl derivatives were designed and synthesized as ACE inhibitors. Coupling of unsaturated carboxylic acids with amino acids and following epoxidation with dimethyldioxirane gave the epoxyalkanoyls with high yield. The inhibitory activity of synthesized compounds on angiotensin converting enzyme was $IC_{50}$ values of 0.06~5.5 ${\mu}M$.

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장내 가수분해조건에 의한 Casein 가수분해물의 Angiotensin Converting Enzyme 저해 효과

  • 황유진;양희진;도정룡;이수원
    • 한국축산식품학회:학술대회논문집
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    • 한국축산식품학회 2005년도 제36차 추계 학술발표대회
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    • pp.290-293
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    • 2005
  • 장내 단백질 가수분해효소에 의한 casein 분해산물들의 ACE 저해 활성을 비교하기 위하여 인공위액, 인공장액 및 인공위액과 장액 연속처리를 각각 반응조건으로 일정시간 casein을 가수분해한 후 각 효소 가수분해물이 혈압상승 peptide 생성효소인 Angiotensin converting enzyme(ACE)에 대한 저해활성을 측정하였다. 각 소화액에 따른 가수분해물은 모두 ACE 저해활성을 나타내었으며, 2시간 효소처리를 하였을 때, 인공위액, 인공장액, 인공위액과 장액 가수분해물은 각각 69%, 80% 및 88%로 최대 ACE 저해활성을 보였다. 그리고 casein의 가수분해 정도를 확인하기 위한 SDS-PAGE에서는 인공위액으로 처리한 군보다 인공장액으로 처리한 군이 더 작은 분자량으로 분해되는 것을 확인할 수 있었고, 인공위액과 장액을 함께 처리한 군에서는 1시간 안에 대부분의 분해가 이루지는 것을 관찰할 수 있었다.

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