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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/04/11 05:54:25」(JST)

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Angiotensin-converting enzyme (EC 3.4.15.1) is known by the following names: ACE, dipeptidyl carboxypeptidase I, peptidase P, dipeptide hydrolase, peptidyl dipeptidase, angiotensin converting enzyme, kininase II, angiotensin I-converting enzyme, carboxycathepsin, dipeptidyl carboxypeptidase, "hypertensin converting enzyme" peptidyl dipeptidase I, peptidyl-dipeptide hydrolase, peptidyldipeptide hydrolase, endothelial cell peptidyl dipeptidase, peptidyl dipeptidase-4, PDH, peptidyl dipeptide hydrolase, and DCP. ACE indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels.

For this reason, drugs known as ACE inhibitors are used to lower blood pressure.

ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the inner layer of blood vessels.^[1]

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. Elevated levels of ACE are also found in leprosy, hyperthyroidism, acute hepatitis, primary biliary cirrhosis, diabetes mellitus, multiple myeloma, osteoarthritis, amyloidosis, Gaucher disease, pneumoconiosis, histoplasmosis, miliary tuberculosis. Serum levels are decreased in renal disease, obstructive pulmonary disease, and hypothyroidism.

Influence on athletic performance

ACE gene is a I/D polymorphism leading to the presence(I) or absence (D) the carriers of the ACE insertion allele of an alu repeat in intron 16 of the gene.^[6] With the insertion, observed higher maximum oxygen uptake (VO2max), increase in training, and increased muscle when paired with individuals carrying the deletion allele.
Individuals with the insertion are associated with long distance and endurance events this is seen in studies that suggest that its due to lower levels of angiotensin II. The other side is the deletion of the Alu that is increases angiotensin II that increases the vasoconstriction of blood vessels. This observed in short distance events and seen mostly in swimmers.^[7]

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. p. 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. Retrieved 2009-03-26.
^ Wang P, Fedoruk MN, Rupert JL (2008). "Keeping pace with ACE: are ACE inhibitors and angiotensin II type 1 receptor antagonists potential doping agents?". Sports Med 38 (12): 1065–79. doi:10.2165/00007256-200838120-00008. PMID 19026021.
^ Costa AM, Silva AJ, Garrido ND, Louro H, de Oliveira RJ, Breitenfeld L (August 2009). "Association between ACE D allele and elite short distance swimming". Eur. J. Appl. Physiol. 106 (6): 785–90. doi:10.1007/s00421-009-1080-z. PMID 19458960.

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)

UpToDate Contents

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1. サルコイドーシスの臨床症状および診断 clinical manifestations and diagnosis of sarcoidosis
2. ACE 阻害薬誘発性血管浮腫 ace inhibitor induced angioedema
3. アンギオテンシン変換酵素阻害剤とアンギオテンシン受容体拮抗剤との相違 differences between angiotensin converting enzyme inhibitors and receptor blockers
4. Chapter 2B：レニン－アンギオテンシン系 chapter 2b renin angiotensin system
5. アンギオテンシン変換酵素阻害剤およびアンギオテンシンⅡ受容体拮抗剤の主な副作用 major side effects of angiotensin converting enzyme inhibitors and angiotensin ii receptor blockers

English Journal

Angiotensin-(1-7): beyond the cardio-renal actions.

Passos-Silva DG, Verano-Braga T, Santos RA.SourceDepartment of Physiology and Biophysics, National Institute of Science and Technology in Nanobiopharmaceutics, Institute of Biological Sciences, Federal University of Minas Gerais, Belo Horizonte (MG), Brazil.
Clinical science (London, England : 1979).Clin Sci (Lond).2013 Apr;124(7):443-56. doi: 10.1042/CS20120461.
It is well known that the RAS (renin-angiotensin system) plays a key role in the modulation of many functions in the body. AngII (angiotensin II) acting on AT1R (type 1 AngII receptor) has a central role in mediating most of the actions of the RAS. However, over the past 10 years, several studies h
PMID 23249272

Angiotensin-converting enzyme inhibition curbs tyrosine nitration of mitochondrial proteins in the renal cortex during the early stage of diabetes mellitus in rats.

Ishii N, Carmines PK, Yokoba M, Imaizumi H, Ichikawa T, Ikenagasa H, Kodera Y, Oh-Ishi M, Aoki Y, Maeda T, Takenaka T, Katagiri M.SourceDepartment of Medical Laboratory Sciences, Kitasato University School of Allied Health Sciences, Kanagawa 252-0373, Japan.
Clinical science (London, England : 1979).Clin Sci (Lond).2013 Apr;124(8):543-52. doi: 10.1042/CS20120251.
Experiments were performed to evaluate the hypothesis that ACE (angiotensin-converting enzyme) inhibition (enalapril) suppresses 3-NT (3-nitrotyrosine) production in the renal cortex during the early stage of Type 1 DM (diabetes mellitus) in the rat. Enalapril was administered chronically for 2 week
PMID 23130652

Gestational Protein Restriction Increases Angiotensin II Production in Rat Lung.

Gao H, Yallampalli U, Yallampalli C.SourceDepartment of Obstetrics & Gynecology, the University of Texas Medical Branch, Galveston, Texas.
Biology of reproduction.Biol Reprod.2013 Mar 14;88(3):64. Print 2013.
Gestational protein restriction (PR) alters the renin-angiotensin system in uterine arteries and placentas and elevates plasma levels of angiotensin II in pregnant rats. To date, how PR increases maternal plasma levels of angiotensin II remains unknown. In this study, we hypothesize that the express
PMID 23365412

Japanese Journal

Role of Aminopeptidases in the Blood Pressure Regulation(Aminopeptidases in Health and Disease)

Mitsui Takashi,Nomura Seiji,Itakura Atsuo [他],MIZUTANI Shigehiko
Biological & pharmaceutical bulletin 27(6), 768-771, 2004-06-01
… This review describes the roles of aminopeptidase A, placental leucine aminopeptidase and kininase I, which are enzymes responsible for hydrolyzing angiotensin II (Angll), vasopressin (AVP) and bradykinin (BK), respectively, in BP regulation. …
NAID 110003608852

アンギオテンシン変換酵素阻害薬の血行動態

上地正実
動物の循環器 = Advances in animal cardiology 31(2), 53-58, 1998-12-01
NAID 10008287451

気道過敏性におけるキニンおよびタキキニンの関与

細川友和
日本薬理学雑誌 111(4), 243-248, 1998-04-01
… The O<SUB>3</SUB>-induced AHR was significantly enhanced by pretreatment with captopril, a kininase II inhibitor. …
NAID 10005085535

Related Pictures

Scheme showing the RAS and the KKS components contributing to CNV. Note Vasoactive Peptides - Basic and Clinical Pharmacology, 13th Ed. Frontiers | Kallikrein/K1, Kinins, and ACE/Kininase II in Homeostasis (PDF) Kallikrein/K1, Kinins, and ACE/Kininase II in Homeostasis and in ACE Polymorphisms | Circulation Research Biosynthesis and metabolism of kinins. Kininogen is converted by

★リンクテーブル★

リンク元	「アンジオテンシン変換酵素」
関連記事	「II」「I」

「アンジオテンシン変換酵素」

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, 4APH, 4APJ, 4BXK
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;
Cellular component	• extracellular region; • extracellular space; • endosome; • plasma membrane; • external side of plasma membrane; • integral to membrane;
Biological process	• kidney development; • blood vessel remodeling; • angiotensin maturation; • 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; • cellular protein metabolic process; • arachidonic acid secretion; • hematopoietic stem cell differentiation;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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PMC	articles
PubMed	articles
NCBI	proteins

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
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PMC	articles
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NCBI	proteins

　　[★]

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

肺の血管内皮細胞に局在 (SPC.102)

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

高値：肉芽腫を形成する疾患(サルコイドーシス、過敏性肺臓炎、ベリリウム肺、珪肺)

「II」

　　[★]

「I」

　　[★]

[isbn0-323-04527-8-1] Kierszenbaum, Abraham L. (2007). Histology and cell biology: an introduction to pathology. Mosby Elsevier. ISBN 0-323-04527-8.

[2] 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. p. 1300. ISBN 1-4160-2328-3.

[pmid10790312-3] 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.

[pmid14757781-4] 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.

[urlACE-inhibitors-5] Klabunde RE. "ACE-inhibitors". Cardiovascular Pharmacology Concepts. cvpharmacology.com. Retrieved 2009-03-26.

[pmid19026021-6] Wang P, Fedoruk MN, Rupert JL (2008). "Keeping pace with ACE: are ACE inhibitors and angiotensin II type 1 receptor antagonists potential doping agents?". Sports Med 38 (12): 1065–79. doi:10.2165/00007256-200838120-00008. PMID 19026021.

[pmid19458960-7] Costa AM, Silva AJ, Garrido ND, Louro H, de Oliveira RJ, Breitenfeld L (August 2009). "Association between ACE D allele and elite short distance swimming". Eur. J. Appl. Physiol. 106 (6): 785–90. doi:10.1007/s00421-009-1080-z. PMID 19458960.

匿名

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案内

案内

kininase II