| Background | Angiotensin-converting enzyme (CD143/ACE) is a ~150 kDa protein. Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity. Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates. Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response. Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins. 1. Kessler, SP. et al. (2002) The Journal of biological chemistry 277, 4271-6. PMID: 117231292. Kessler, SP. et al. (2003) The Journal of biological chemistry 278, 21105-12. PMID: 127774433. Fuchs, S. et al. (2004) The Journal of biological chemistry 279, 15946-53. PMID: 147577574. Fuchs, S. et al. (2005) Nature medicine 11, 1140-2; author reply 1142-3. PMID: 162700635. Trieu, BH. et al. (2022) Science (New York, N.Y.) 375, 1177-1182. PMID: 352018987. Esther, CR. et al. (1996) Laboratory investigation; a journal of technical methods and pathology 74, 953-65. PMID: 86427908. Tian, B. et al. (1997) Hypertension (Dallas, Tex. : 1979) 30, 128-33. PMID: 92318329. Junot, C. et al. (2001) The Journal of pharmacology and experimental therapeutics 297, 606-11. PMID: 11303049 |
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