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Angiotensin-converting enzyme: Wikis

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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 GeneCards: ACE Gene
RNA expression pattern
PBB GE ACE 209749 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1636 11421
Ensembl ENSG00000159640 ENSMUSG00000020681
UniProt P12821 Q3TU20
RefSeq (mRNA) NM_000789 NM_009598
RefSeq (protein) NP_000780 NP_033728
Location (UCSC) 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

Schematic diagram of the renin-angiotensin-aldosterone system
Anatomical diagram of the renin-angiotensin system, showing role of ACE at the lungs.[2]

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.[5]

Genetics & C and N Domains With Important Functional Difference

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. Brain has ACE enzyme which takes part in local RAAS and converts Aβ42 ( plaquogenic ) to Aβ40( more soluble and removal ) forms of Beta amyloid ; latter is prdominentally a function of N domain portion on the ACE enzyme; Inhibition of ACE with ACE Inhibitors, especially Blood Brain Barrier crossing and with preferentially select N terminal activity would cause accumulation of Aβ42 which is plaquogenic causing progression of dementia; preferential C domain active BBB crossing ACE would likely have less of this latter effect.

See also

References

  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. pp. 1300. ISBN 1-4160-2328-3.  
  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.  
  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.  
  5. ^ 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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