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Angiotensin-Converting Enzyme 2 (ACE2, SARS Receptor )

By EST database searching for sequences showing homology to the zinc metalloprotease angiotensin-I converting enzyme, a full-length ACE2 cDNA, originally called ACEH, was isolated, which encoded a deduced 805-amino acid protein that shares approximately 40% identity with the N- and C-terminal domains of ACE. ACE2 contains a potential 17-amino acid N-terminal signal peptide and a putative 22-amino acid C-terminal membrane anchor. Northern blot analysis detected high expression of ACE2 in kidney, testis, and heart, and moderate expression in colon, small intestine, and ovary. Tipnis et al. expressed a soluble, truncated form of ACE2 lacking transmembrane and cytosolic domains in CHO cells and found that it produced a glycosylated protein that was able to cleave angiotensin I and angiotensin II , but not bradykinin. Boehm and Nabel showed whereas ACE converts angiotensin I to angiotensin II, which has 8 amino acids, ACE2 converts angiotensin I to angiotensin 1–9, which has 9 amino acids. This can then further be converted by ACE to a shorter peptide, angiotensin 1–7, which is a blood vessel dilator. Using ACE2 null mice, Crackower et al. showed that ACE2 was critically involved in a cardiac contractility. Li et al. identified ACE2, isolated from SARS coronavirus-permissive Vero E6 cells, that efficiently binds the S1 domain of the SARS coronavirus S protein. It was shown that when ACE2 was engaged with S protein ACE2 surface expression was downregulated, increasing lung levels of angiotensin II, which was proposed to give rise to a severe lung injury. Since ACE2 is detected in urine, measurement of shedded ACE2 may provide a novel clue to renal & cardiovascular function of ACE2.



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