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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/04/12 13:56:37」(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)

English Journal

Gaucher Disease-Induced Pluripotent Stem Cells Display Decreased Erythroid Potential and Aberrant Myelopoiesis.

Sgambato JA1, Park TS1, Miller D1, Panicker LM1, Sidransky E1, Lun Y1, Awad O1, Bentzen SM1, Zambidis ET1, Feldman RA2.
Stem cells translational medicine.Stem Cells Transl Med.2015 Aug;4(8):878-86. doi: 10.5966/sctm.2014-0213. Epub 2015 Jun 10.
Gaucher disease (GD) is the most common lysosomal storage disease resulting from mutations in the lysosomal enzyme glucocerebrosidase (GCase). The hematopoietic abnormalities in GD include the presence of characteristic Gaucher macrophages that infiltrate patient tissues and cytopenias. At present,
PMID 26062980

The cell-surface proteome of cultured adipose stromal cells.

Donnenberg AD1,2,3, Meyer EM2, Rubin JP3,4, Donnenberg VS2,3,5.
Cytometry. Part A : the journal of the International Society for Analytical Cytology.Cytometry A.2015 Jul;87(7):665-74. doi: 10.1002/cyto.a.22682. Epub 2015 Apr 30.
In this technical note we describe a method to evaluate the cell surface proteome of human primary cell cultures and cell lines. The method utilizes the BD Biosciences lyoplate, a system covering 242 surface proteins, glycoproteins, and glycosphingolipids plus relevant isotype controls, automated pl
PMID 25929697

Genetic Association Between CD143 rs4340 Polymorphism and Pneumonia risk: A Meta Analysis.

Wang H1, Zhang K, Qin H, Yang L, Zhang L, Cao Y.
Medicine.Medicine (Baltimore).2015 Jul;94(30):e883. doi: 10.1097/MD.0000000000000883.
rs4340 polymorphism at intron 16 of the angiotensin-converting enzyme (CD143) gene was reported to repress cough reflex by reducing bradykinin and substance P levels, thus increasing the likelihood to develop pneumonia. There have been different reports regarding the correlation of CD143 rs4340 geno
PMID 26222869

Related Pictures

Mazda Mazda5 2,0 CD143 GTA * Superausstattung* add to cart model cd143 manufactured by crissy armstrong collection Flow Cytometry with anti-CD143 / Angiotensin Converting Enzyme 1 Details about CD143 Canadian Pacific -Yellow Green ace cd143 in human kidney angiotensin i converting enzyme ace cd143 IHC/ICC: ACE/CD143 Mazda, 5 CD143 GTA Navi, 19.600,-

★リンクテーブル★

リンク元	「アンジオテンシン変換酵素」「angiotensin-converting enzyme」「kininase II」
関連記事	「CD14」「CD1」

「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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Search
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
Search
PMC	articles
PubMed	articles
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)

「angiotensin-converting enzyme」

　　[★] アンジオテンシン変換酵素, ACE, CD143

「kininase II」

　　[★] アンジオテンシン変換酵素, CD143

「CD14」

　　[★]

同？: リポ多糖受容体 LPS受容体 lipopolysaccharide receptor, LPS receptor

単球、マクロファージ、好中球の細胞膜上に存在し、LPS-LBP複合体をTLRを共役して受容し、TNF-α、IL-1を産生するシグナルを伝達するらしい

LPSの受容 (SMB.117)

LPSはマクロファージ、単球、顆粒球、Bリンパ球と反応し、多彩な生物活性を発現する。この反応には細胞表面のToll-like receptor。TLR-4がLPSのレセブタ-としてはたらき, LPSのシグナルを細胞内へと伝達する。このTLR-4の機能不全はLPSに対する応答性を失わせる。 TLR-4のほかに, CD14やMD-2と呼ばれる分子もLPSの認識に関与している。このTLRは分子群を形成し,ペプチドグリカン,リポタンパク質DNAなどの菌体成分を認識し,感染防御に重要なシグナルを伝達する。

発現細胞

骨髄性単球細胞

機能

LPSの直接の受容体であり、Toll-like receptorとともに細胞内へのシグナル伝達に関わる。
LPS-LBP複合体の受容体　←　日本語がよく分かりません

「CD1」

　　[★]

同: leucine-6, CD1A through E

種類

CD1a, CD1b, CD1c, CD1d

発現組織

胸腺皮質、ランゲルハンス細胞、樹状細胞、B細胞(CD1c)、腸上皮、平滑筋、血管上皮(CD1d)

分子量

43-49

機能

MHC class I-like molecule, associated with β2-microgloulin. Has specialized role in presentation of lipid antigens

[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

検索

案内

案内

CD143