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Angiotensin-converting enzyme

 
Sports Science and Medicine: angiotensin-converting enzyme

ACE

An enzyme that catalyses the conversion of angiotensin I to angiotensin II. Two forms of the enzyme are coded for by two ACE alleles of different length. Individuals with two copies of the longer allele have been found to gain more muscle mass and lose more body fat during intensive physical training than those with two copies of the shorter allele or one copy of each.

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Medical Dictionary: di·pep·ti·dyl carboxypeptidase
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(dī-pĕp'tĭ-dĭl')
n.

A proteolytic enzyme that catalyzes the removal of dipeptides from a variety of compounds, as from angiotensin I as it is converted to angiotensin II. Also called angiotensin-converting enzyme.

WordNet: angiotensin converting enzyme
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Note: click on a word meaning below to see its connections and related words.

The noun has one meaning:

Meaning #1: proteolytic enzyme that converts angiotensin I into angiotensin II


Wikipedia: Angiotensin-converting enzyme
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Angiotensin I converting enzyme (peptidyl-dipeptidase A) 1
Available structures: 1o86, 1o8a, 1uze, 1uzf, 2c6f, 2c6n, 2iul, 2iux, 2oc2
Identifiers
Symbols ACE; ACE1; CD143; DCP; DCP1; MGC26566
External IDs OMIM106180 MGI87874 HomoloGene37351
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 1636 11421
Ensembl ENSG00000159640 ENSMUSG00000020681
Uniprot P12821 Q3TU20
Refseq NM_000789 (mRNA)
NP_000780 (protein)
NM_009598 (mRNA)
NP_033728 (protein)
Location Chr 17: 58.91 - 58.94 Mb Chr 11: 105.78 - 105.81 Mb
Pubmed search [1] [2]

Angiotensin I-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

Functions

It has two primary functions:

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 angiotension 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.[4]

Genetics

The ACE gene, ACE, encodes 2 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.

See also

References

  1. ^ Kierszenbaum, Abraham L. (2007). Histology and cell biology: an introduction to pathology. Mosby Elsevier. ISBN 0-323-04527-8. 
  2. ^ 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. 
  3. ^ 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. 
  4. ^ 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. 

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Sports Science and Medicine. The Oxford Dictionary of Sports Science & Medicine. Copyright © Michael Kent 1998, 2006, 2007. All rights reserved.  Read more
Medical Dictionary. The American Heritage® Stedman's Medical Dictionary Copyright © 2002, 2001, 1995 by Houghton Mifflin Company Read more
WordNet. WordNet 1.7.1 Copyright © 2001 by Princeton University. All rights reserved.  Read more
Wikipedia. This article is licensed under the Creative Commons Attribution/Share-Alike License. It uses material from the Wikipedia article "Angiotensin-converting enzyme" Read more