Angiotensin-converting enzyme (EC18.104.22.168) 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.
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 testicularLeydig 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.
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.
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. 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.
^Kierszenbaum, Abraham L. (2007). Histology and cell biology: an introduction to pathology. Mosby Elsevier. ISBN0-323-04527-8.
^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. ISBN1-4160-2328-3.
^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. PMID10790312.
^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. PMID19458960.
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. PMID14959477.
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. PMID16018179.
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. PMID16984256.
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. PMID17103020.
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. PMID17504232.