アンジオテンシン変換酵素, ACE, CD143
WordNet
- any of several complex proteins that are produced by cells and act as catalysts in specific biochemical reactions
- any of several vasoconstrictor substances (trade name Hypertensin) that cause narrowing of blood vessels (同)angiotonin, Hypertensin
PrepTutorEJDIC
- 酵素
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2012/10/15 11:08:22」(JST)
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Angiotensin-converting enzyme |
Identifiers |
EC number |
3.4.15.1 |
CAS number |
9015-82-1 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Search |
PMC |
articles |
PubMed |
articles |
NCBI Protein |
search |
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Angiotensin I converting enzyme (peptidyl-dipeptidase A) 1 |
Rendering of ACE from PDB 1O86 |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1O86, 1O8A, 1UZE, 1UZF, 2C6F, 2C6N, 2IUL, 2IUX, 2OC2, 2XY9, 2XYD, 2YDM, 3BKK, 3BKL, 3L3N, 3NXQ
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Identifiers |
Symbols |
ACE; ACE1; CD143; DCP; DCP1; ICH; MVCD3 |
External IDs |
OMIM: 106180 MGI: 87874 HomoloGene: 37351 ChEMBL: 1808 GeneCards: ACE Gene |
EC number |
3.4.15.1 |
Gene Ontology |
Molecular function |
• actin binding
• endopeptidase activity
• carboxypeptidase activity
• protein binding
• drug binding
• metallopeptidase activity
• peptidyl-dipeptidase activity
• zinc ion binding
• chloride ion binding
• bradykinin receptor binding
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Cellular component |
• extracellular space
• endosome
• plasma membrane
• external side of plasma membrane
• integral to membrane
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Biological process |
• kidney development
• blood vessel remodeling
• angiotensin catabolic process in blood
• regulation of renal output by angiotensin
• regulation of systemic arterial blood pressure by renin-angiotensin
• proteolysis
• regulation of blood pressure
• regulation of smooth muscle cell migration
• regulation of vasoconstriction
• mononuclear cell proliferation
• regulation of vasodilation
• hormone catabolic process
• peptide catabolic process
• arachidonic acid secretion
• hemopoietic stem cell differentiation
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
1636 |
11421 |
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Ensembl |
ENSG00000159640 |
ENSMUSG00000020681 |
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UniProt |
P12821 |
P09470 |
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RefSeq (mRNA) |
NM_000789.3 |
NM_009598.2 |
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RefSeq (protein) |
NP_000780.1 |
NP_033728.1 |
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Location (UCSC) |
Chr 17:
61.55 – 61.6 Mb |
Chr 11:
105.97 – 105.99 Mb |
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PubMed search |
[1] |
[2] |
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Angiotensin-converting enzyme (ACE, EC 3.4.15.1), an exopeptidase, is a circulating enzyme that participates in the body's renin-angiotensin system (RAS), which mediates extracellular volume (i.e. that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. It is secreted by pulmonary and renal endothelial cells and catalyzes the conversion of decapeptide angiotensin I to octapeptide angiotensin II.[1]
Contents
- 1 Functions
- 2 Genetics and C and N domains function
- 3 Pathology
- 4 See also
- 5 References
- 6 Further reading
- 7 External links
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Functions
Schematic diagram of the renin-angiotensin-aldosterone system
Anatomical diagram of the renin-angiotensin system, showing the role of ACE at the lungs.
[2]
It has two primary functions:
- ACE catalyses the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor in a substrate concentration-dependent manner.[3]
- ACE degrades bradykinin, a potent vasodilator, and other vasoactive peptides,[4]
These two actions make ACE inhibition a goal in the treatment of conditions such as high blood pressure, heart failure, diabetic nephropathy, and type 2 diabetes mellitus. Inhibition of ACE (by ACE inhibitors) results in the decreased formation of angiotensin II and decreased metabolism of bradykinin, leading to systematic dilation of the arteries and veins and a decrease in arterial blood pressure. In addition, inhibiting angiotensin II formation diminishes angiotensin II-mediated aldosterone secretion from the adrenal cortex, leading to a decrease in water and sodium reabsorption and a reduction in extracellular volume.[5]
Genetics and C and N domains function
The ACE gene, ACE, encodes two isozymes. The somatic isozyme is expressed in many tissues, mainly in the lung, including vascular endothelial cells, epithelial kidney cells, and testicular Leydig cells, whereas the germinal is expressed only in sperm. Brain tissue has ACE enzyme, which takes part in local RAAS and converts Aβ42 (which aggregates into plaques) to Aβ40 (which is thought to be less toxic) forms of beta amyloid. The latter is predominantly a function of N domain portion on the ACE enzyme. ACE inhibitors that cross the blood–brain barrier and have preferentially select N terminal activity may, therefore, cause accumulation of Aβ42 and progression of dementia.[citation needed]
Pathology
Elevated levels of ACE are found in sarcoidosis, and are used in diagnosing and monitoring this disease.
See also
- Renin-angiotensin system
- ACE inhibitors
- Hypotensive transfusion reaction
- Angiotensin-converting enzyme 2
References
- ^ Kierszenbaum, Abraham L. (2007). Histology and cell biology: an introduction to pathology. Mosby Elsevier. ISBN 0-323-04527-8.
- ^ Page 866-867 (Integration of Salt and Water Balance) and 1059 (The Adrenal Gland) in: Walter F., PhD. Boron (2003). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. pp. 1300. ISBN 1-4160-2328-3.
- ^ Zhang R, Xu X, Chen T, Li L, Rao P (May 2000). "An assay for angiotensin-converting enzyme using capillary zone electrophoresis". Anal. Biochem. 280 (2): 286–90. doi:10.1006/abio.2000.4535. PMID 10790312.
- ^ Imig JD (March 2004). "ACE Inhibition and Bradykinin-Mediated Renal Vascular Responses: EDHF Involvement". Hypertension 43 (3): 533–5. doi:10.1161/01.HYP.0000118054.86193.ce. PMID 14757781.
- ^ Klabunde RE. "ACE-inhibitors". Cardiovascular Pharmacology Concepts. cvpharmacology.com. http://www.cvpharmacology.com/vasodilator/ACE.htm. Retrieved 2009-03-26.
Further reading
- Niu T, Chen X, Xu X (2002). "Angiotensin converting enzyme gene insertion/deletion polymorphism and cardiovascular disease: therapeutic implications". Drugs 62 (7): 977–93. doi:10.2165/00003495-200262070-00001. PMID 11985486.
- Roĭtberg GE, Tikhonravov AV, Dorosh ZhV (2004). "[Role of angiotensin-converting enzyme gene polymorphism in the development of metabolic syndrome]". Ter. Arkh. 75 (12): 72–7. PMID 14959477.
- Vynohradova SV (2005). "[The role of angiotensin-converting enzyme gene I/D polymorphism in development of metabolic disorders in patients with cardiovascular pathology]". Tsitol. Genet. 39 (1): 63–70. PMID 16018179.
- König S, Luger TA, Scholzen TE (2006). "Monitoring neuropeptide-specific proteases: processing of the proopiomelanocortin peptides adrenocorticotropin and alpha-melanocyte-stimulating hormone in the skin". Exp. Dermatol. 15 (10): 751–61. doi:10.1111/j.1600-0625.2006.00472.x. PMID 16984256.
- Sabbagh AS, Otrock ZK, Mahfoud ZR, et al. (2007). "Angiotensin-converting enzyme gene polymorphism and allele frequencies in the Lebanese population: prevalence and review of the literature". Mol. Biol. Rep. 34 (1): 47–52. doi:10.1007/s11033-006-9013-y. PMID 17103020.
- Castellon R, Hamdi HK (2007). "Demystifying the ACE polymorphism: from genetics to biology". Curr. Pharm. Des. 13 (12): 1191–8. doi:10.2174/138161207780618902. PMID 17504229.
- Lazartigues E, Feng Y, Lavoie JL (2007). "The two fACEs of the tissue renin-angiotensin systems: implication in cardiovascular diseases". Curr. Pharm. Des. 13 (12): 1231–45. doi:10.2174/138161207780618911. PMID 17504232.
External links
- Proteopedia Angiotensin-converting_enzyme - the Angiotensin-Converting Enzyme Structure in Interactive 3D
- Angiotensin+Converting+Enzyme at the US National Library of Medicine Medical Subject Headings (MeSH)
PDB gallery
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1o86: CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH LISINOPRIL.
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1o8a: CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME (NATIVE).
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1uze: COMPLEX OF THE ANTI-HYPERTENSIVE DRUG ENALAPRILAT AND THE HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME
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1uzf: COMPLEX OF THE ANTI-HYPERTENSIVE DRUG CAPTOPRIL AN THE HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME
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2c6f: STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN
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2c6n: STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN WITH LISINOPRIL
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2iul: HUMAN TACE G13 MUTANT
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2iux: HUMAN TACE MUTANT G1234
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2oc2: Structure of testis ACE with RXPA380
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Hydrolase: proteases (EC 3.4)
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3.4.11-19: Exopeptidase |
3.4.11 |
- Aminopeptidase
- Alanine
- Arginyl
- Aspartyl
- Cystinyl
- Leucyl
- Glutamyl
- Methionyl
- O
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3.4.13 |
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3.4.14 |
- Dipeptidyl peptidase
- Cathepsin C
- Dipeptidyl peptidase-4
- Tripeptidyl peptidase
- Tripeptidyl peptidase I
- Tripeptidyl peptidase II
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3.4.15 |
- Angiotensin-converting enzyme
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3.4.16 |
- Serine type carboxypeptidases: Cathepsin A
- DD-transpeptidase
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3.4.17 |
- Metallocarboxypeptidases: Carboxypeptidase
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Other/ungrouped |
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3.4.21-24: Endopeptidase |
- Serine proteases
- Cysteine protease
- Aspartic acid protease
- Metalloendopeptidases
- Other/ungrouped: Amyloid precursor protein secretase
- Alpha secretase
- Beta-secretase 1
- Beta-secretase 2
- Gamma secretase
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3.4.99: Unknown |
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Bioavailability of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from Virgibacillus halodenitrificans SK1-3-7 proteinases hydrolyzed tilapia muscle proteins.
- Toopcham T1, Mes JJ2, Wichers HJ2, Roytrakul S3, Yongsawatdigul J4.
- Food chemistry.Food Chem.2017 Apr 1;220:190-197. doi: 10.1016/j.foodchem.2016.09.183. Epub 2016 Sep 29.
- The angiotensin I-converting enzyme (ACE) inhibitory activity of protein hydrolysates from tilapia muscle fractions, namely mince (M), washed mince (WM), and sarcoplasmic protein (SP), were investigated. Each fraction was hydrolyzed by Virgibacillus halodenitrificans SK1-3-7 proteinases for up to 24
- PMID 27855889
- Bioactive peptides from Atlantic salmon (Salmo salar) with angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory, and antioxidant activities.
- Neves AC1, Harnedy PA1, O'Keeffe MB1, FitzGerald RJ2.
- Food chemistry.Food Chem.2017 Mar 1;218:396-405. doi: 10.1016/j.foodchem.2016.09.053. Epub 2016 Sep 9.
- The pH shift method was utilised for the recovery of proteins from salmon trimmings (ST), yielding 93% (w/w) protein. ST protein (STP) hydrolysates were generated with different enzyme preparations. STP incubated with Corolase PP for 1h (STP-C1) had the most potent angiotensin converting enzyme (ACE
- PMID 27719926
- Electrochemically reduced graphene and iridium oxide nanoparticles for inhibition-based angiotensin-converting enzyme inhibitor detection.
- Kurbanoglu S1, Rivas L2, Ozkan SA3, Merkoçi A4.
- Biosensors & bioelectronics.Biosens Bioelectron.2017 Feb 15;88:122-129. doi: 10.1016/j.bios.2016.07.109. Epub 2016 Jul 30.
- In this work, a novel biosensor based on electrochemically reduced graphene oxide and iridium oxide nanoparticles for the detection of angiotensin-converting enzyme inhibitor drug, captopril, is presented. For the preparation of the biosensor, tyrosinase is immobilized onto screen printed electrode
- PMID 27499381
Japanese Journal
- 加熱方法の違いによるサヤエンドウの色およびACE阻害活性の比較
- アンジオテンシン変換酵素を標的とした大豆由来内臓脂肪型肥満症改善物質の探索 (第16回研究報告会記録)
- マンネンタケ子実体の水抽出物に含まれるアンギオテンシン変換酵素阻害成分
- 熊倉 慧,小澤 好夫,五十嵐 圭日子,鮫島 正浩
- 日本きのこ学会誌 : mushroom science and biotechnology 22(1), 11-18, 2014-04-30
- 本研究ではマンネンタケ水抽出物中のACE阻害活性成分の同定を試みた.水抽出物をエタノール分画,限外ろ過,陽イオン交換クロマトグラフィーを用いて精製し,精製物(EU3C)を得た.EU3CのIC_<50>値は89μg/mL,K_i値は49μg/mLであった.さらにEU3Cを逆相クロマトグラフィーにより分画した結果,IC_<50>値およびK_i値は上昇した.一方,EU3Cは拮抗阻 …
- NAID 110009823292
Related Pictures
★リンクテーブル★
[★]
- 25歳の男性。職場の健康診断で胸部エックス線写真の異常を指摘され来院した。最近、目のかすみを自覚している。喫煙歴はない。胸部エックス線写真(別冊No. 20)を別に示す。
- この疾患の診断に有用な検査項目はどれか。
[正答]
※国試ナビ4※ [104I067]←[国試_104]→[104I069]
[★]
- 英
- angiotensin converting enzyme angiotensin-converting enzyme ACE
- 同
- キニナーゼII kininase II、アンジオテンシン転換酵素、CD143、 peptidyl dipeptidase A、ジペプチジルカルボキシペプチダーゼ dipeptidyl carboxypeptidase
- 関
- アンジオテンシン
概念
- 血中やその他の組織にも存在するが、肺で活性が強い (SPC.102)
- 実体は、dipeptidyl dipeptidaseのconverting enzyme (SPC.102)
検査
判別
[★]
- 関
- angiotensin-converting enzyme、peptidyl-dipeptidase A
[★]
ペプチジルジペプチダーゼA
- 関
- angiotensin I-converting enzyme、angiotensin-converting enzyme
[★]
アンジオテンシン変換酵素 angiotensin-converting enzyme
[★]
アンジオテンシン変換酵素阻害薬
[★]
アンジオテンシン変換酵素阻害薬
[★]
アンジオテンシン