• 제목/요약/키워드: Converting enzyme inhibitor

검색결과 146건 처리시간 0.022초

Angiotensin-Converting Enzyme Inhibitor(ACE Inhibitor)에 의해 유발된 안면부 맥관부종(angioedema) 치험례 (A Case of Angioedema Induced by Angiotensin-Converting Enzyme Inhibitor)

  • 하유군;정기용;백종우;김동우;박종형;전찬용;최유경
    • 대한한방내과학회지
    • /
    • 제28권2호
    • /
    • pp.399-407
    • /
    • 2007
  • Angioedema is a localized transient swelling of sudden onset that can occur in the face, lips, tongue, hand, feet, respiratory system and gastrointestinal system. Angioedema is classified as allergy, hereditary, idiopathic or induced by medication as like aspirin, nonsteroidal anti-inflammatory agents, opiates, antibiotics, and angiotensin-converting enzyme. Angiotensin-converting enzyme inhibitors are widely prescribed for hypertension and heart failure. This drug is commonly associated with angioedema which may be potentially life threatening. We experienced a case of angioedema induced by ACE inhibitor (angiotensin-converting enzyme inhibitor) in a 74-year-old patient who took ACE inhibitor to control hypertension during hospitalization. We thought the angioedema in the face had relation to myenzhong (面腫, mienjong) in oriental medicine. Weiling-tang (Wiryung-tang) was effective for angioedema in the face. As a result the symptoms disappeared rapidly. After 6 days, the patient's symptoms had notably improved.

  • PDF

Isolation of Angiotensin Converting Enzyme Inhibitory Peptide from Beef Bone Extract Hydrolysate

  • Park, Eun-Hee;Cho, Yong-Sik;Song, Kyung-Bin
    • Applied Biological Chemistry
    • /
    • 제41권4호
    • /
    • pp.270-272
    • /
    • 1998
  • Angiotensin converting enzyme (ACE) inhibitor was isolated from beef bone extract hydrolysate. After hydrolysis of beef bone extract with a commercial protease, ACE inhibitory peptide was purified by using ultrafiltration, gel permeation chromatography, and reverse-phase high pressure liquid chromatography. The purified ACE inhibitor was a pentapeptide, Gly-Pro-X-Gly-Pro.

  • PDF

Isolation of Angiotensin I Converting Enzyme (ACE) Inhibitor from fermented oyster, Crassostrea gigas

  • Park, Ji-Young;Je, Jae-Young;Park, Pyo-Jam;Kim, Se-Kwon
    • 한국어업기술학회:학술대회논문집
    • /
    • 한국어업기술학회 2002년도 추계 수산관련학회 공동학술대회발표요지집
    • /
    • pp.193-194
    • /
    • 2002
  • Angiotensin I converting enzyme (ACE) inhibitor was purified from Crassostrea gigas. The ACE belongs to the class of metalloprotease. This enzyme plays an important physiological role in regulating blood pressure of the rennin-angiotensin system by converting from angiotensin I to octapeptide angiotensin II, a potent vasoconstrictor and by inactivating bradykinin, which has depressor action. (omitted)

  • PDF

Production of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Malassezia pachydermatis G-14

  • Jeong, Seung-Chan;Kim, Jae-Ho;Kim, Na-Mi;Lee, Jong-Soo
    • Mycobiology
    • /
    • 제33권3호
    • /
    • pp.142-146
    • /
    • 2005
  • To produce a novel antihypertensive angiotensin I-converting enzyme (ACE) inhibitor from yeast, a yeast isolate, designated G-14 showing the highest ACE inhibitory activity was obtained and identified as Malassezia pachydermatis based on morphological, biochemical and cultural characteristics. The maximal extracellular ACE inhibitor production was obtained from M. pachydermatis G-14 when the strain was cultured in YEPD medium containing 0.5% yeast extract, 3.0% peptone and 2.0% glucose at $30^{\circ}C$ for 24 h and the final ACE inhibitory activity was 48.9% under the above condition.

Angiotensin Converting Enzyme(ACE) 저해제를 생성하는 방선균 분리주의 동정 및 최적 발효조건 (Identification and Culture Conditon of an Actionomycetes Stranin Producing an Angiotensin Converting Enzyme Inhibitor)

  • 문성훈;하상철;이동선;김종국;홍순덕
    • 한국미생물·생명공학회지
    • /
    • 제23권4호
    • /
    • pp.439-445
    • /
    • 1995
  • Identification of Actinomycetes isolate strain SH-8002, a producer of ACE inhibitor, based on procedures employed in the international Streptomyces project. The strain, designated as SH-8002, was identified as Streptomyces zoamyceticus SH-8002 based on its morphological, physiological, biochemical and chemotaxonomic characteristics. The ACE inhibitor produced by the strain was highly achieved in fermentation medium condition that was 1% soluble starch, 0.5% tryptone, 0.2% K$_{2}$HPO$_{4}$, 0.2% CaCO$_{3}$, 0.1% NaCl, pH 8.0 at 30$\circ$C for 144 hrs.

  • PDF

한국산 녹차로부터 분리한 Flavan-3-ol 화합물의 Angiotensin Converting Enzyme 저해 효과 (Inhibition Effect of Against Angiotensin Converting Enzyme of Flavan-3-ols isolated Korean Green Tea)

  • 조영제;안봉전;최청
    • 한국식품과학회지
    • /
    • 제25권3호
    • /
    • pp.238-242
    • /
    • 1993
  • 기능성 식품과 생약재로의 이용을 위한 연구의 일환으로 한국산 녹차로부터 탄닌을 분리하여 angiotensin converting enzyme 저해효과를 측정하였다. 녹차의 acetone 추출물에서 angiotensin converting enzyme 저해효과가 있음이 확인되었고 정제된 탄닌의 효소저해효과를 검토한 결과 angiotensin converting enzyme 저해는 galloyl tannin류가 nongalloyl tannin류 보다 활성이 더 우수하였고 구조적 이성체에서도 (+)-catechin류 보다 (-)-epicatechin류가 효소저해효과가 더 좋았으며, 각 물질 간 상승효과가 인정되었다. 녹차에서의 탄닌류는 angiotensin converting enzyme에 대해 비경쟁적 저해를 하는 것을 알 수 있다.

  • PDF

Tumor necrosis factor α-converting enzyme inhibitor attenuates lipopolysaccharide-induced reactive oxygen species and mitogen-activated protein kinase expression in human renal proximal tubule epithelial cells

  • Bae, Eun Hui;Kim, In Jin;Choi, Hong Sang;Kim, Ha Yeon;Kim, Chang Seong;Ma, Seong Kwon;Kim, In S.;Kim, Soo Wan
    • The Korean Journal of Physiology and Pharmacology
    • /
    • 제22권2호
    • /
    • pp.135-143
    • /
    • 2018
  • Tumor necrosis $factor-{\alpha}$ ($TNF{\alpha}$) and the angiotensin system are involved in inflammatory diseases and may contribute to acute kidney injury. We investigated the mechanisms by which $TNF{\alpha}$-converting enzyme (TACE) contributes to lipopolysaccharide (LPS)-induced renal inflammation and the effect of TACE inhibitor treatment on LPS-induced cellular injury in human renal proximal tubule epithelial (HK-2) cells. Mice were treated with LPS (10 mg/kg, i.p.) and HK-2 cells were cultured with or without LPS ($10{\mu}g/ml$) in the presence or absence of a type 1 TACE inhibitor ($1{\mu}M$) or type 2 TACE inhibitor ($10{\mu}M$). LPS treatment induced increased serum creatinine, $TNF{\alpha}$, and urinary neutrophil gelatinase-associated lipocalin. Angiotensin II type 1 receptor, mitogen activated protein kinase (MAPK), and TACE increased, while angiotensin-converting enzyme-2 (ACE2) expression decreased in LPS-induced acute kidney injury and LPS-treated HK-2 cells. LPS induced reactive oxygen species and the down-regulation of ACE2, and these responses were prevented by TACE inhibitors in HK-2 cells. TACE inhibitors increased cell viability in LPS-treated HK-2 cells and attenuated oxidative stress and inflammatory cytokines. Our findings indicate that LPS activates renin angiotensin system components via the activation of TACE. Furthermore, inhibitors of TACE are potential therapeutic agents for kidney injury.

Production and Characterization of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Pholiota adiposa

  • Koo Kyo-Chul;Lee Dae-Hyoung;Kim Jae-Ho;Yu Hyung-Eun;Park Jeong-Sik;Lee Jong-Soo
    • Journal of Microbiology and Biotechnology
    • /
    • 제16권5호
    • /
    • pp.757-763
    • /
    • 2006
  • Angiotensin I-converting enzyme (ACE) inhibitors have generally been very useful to remedy or prevent hypertension. This study describes the extraction and characterization of an ACE inhibitor from the fruiting body of Pholiota adiposa ASI 24012, which can be used as an antihypertensive drug. The maximal ACE inhibitory activity $(IC_{50};0.25mg)$ was obtained when the fruiting body of Pholiota adiposa ASI 24012 was extracted with distilled water at $30^{\circ}C$ for 12 h. After the purification of ACE inhibitor with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.044 mg was obtained. The purified ACE inhibitory peptide was a novel pentapeptide, showing very little similarity to other ACE inhibitory peptide sequences. The molecular mass of the purified ACE inhibitor was estimated to be 414 daltons with a sequence of Gly-Glu-Gly-Gly-Pro, and showed a clear antihypertensive effect on spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg.

재조합 대장균으로부터 항고혈압 Angiotensin I-Converting Enzyme 저해제의 특성연구 (Characterization of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Recombinant E. coli)

  • 김재호;정승찬;이대형;이종수
    • 자연과학논문집
    • /
    • 제16권1호
    • /
    • pp.1-13
    • /
    • 2005
  • 안지오텐신(ACE) 저해제는 항고혈 효과를 갖고 있으므로 오랫동안 고혈압의 예방이나 치료에 이용되어 왔다. 본 연구는 재조합 대장균으로부터 새로운 ACE 저해제를 생산하고 정제하며 나아가 이들이 구조-기능 관P를 규명하기 위해 수행되었다. Saccharomyces cerevisiae의 ACE 저해 펩타이드 유전자를 함유하고 있는 재조합 pGEX-4T-3을 대장균 BL21(DE3)로 형질전환 시켰다. 재조합 pGEX-4T-3을 갖고 있는 대장균 BL21(DE3)로부터 생산된 Glutathione-s 전이효소(GST) 융합 단백질을 얻어서 그중 ACE저해 펩타이드를 Sephadex G-25 컬럼 크로마토그래피로 정제하였다. 정제된 ACE 저해 펩타이드는 타이로신-아스파틱엑시드-그리신-글리신-발린-페닐알라린-아르기닌-발린-타이로신-트레오닌의 서열을 가진 새로운 decapeptide이었고 ACE에 대하여 경쟁적으로 저해하였다.

  • PDF

Characterization of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Saccharomyces cerevisiae

  • KIM, JAE-HO;LEE, DAE-HYOUNG;JEONG, SEOUNG-CHAN;CHUNG, KUN-SUB;LEE, JONG-SOO
    • Journal of Microbiology and Biotechnology
    • /
    • 제14권6호
    • /
    • pp.1318-1323
    • /
    • 2004
  • This study describes the purification and characterization of a novel antihypertensive angiotensin 1­converting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at $30^{\circ}C$ and its ACE inhibitory activity was increased by about 1.5 times after treatment of the cell-free extract with pepsin. After the purification of ACE inhibitory peptides with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.07 mg and $3.5\%$ yield was obtained. The purified peptide was a novel decapeptide, showing very low similarity to other ACE inhibitory peptide sequences, and its amino acid sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor competitively inhibited ACE and also showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg body weight.