angiotensin converting enzyme 2 (ACE2)
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Function
- carboxypeptidase
- converts angiotensin 1 to angiotensin 1-9
- converts angiotensin 2 to angiotensin 1-7
- hydrolyzes apelin-13 & dynorphin-13 with high efficiency
- regulator of heart function
- interacts with ITGB1, HCOV-SARS, HCOV-NL63 S protein
- processing by ADAM17 may lead to a secreted protein
- binds 1 Zn+2 & 1 Cl- per subunit
- may hydrolyze bradykinin
Inhibition:
- inhibited by MLN-4760, cFP-Leu, EDTA
- NOT inhibited by benzylsuccinate, a carboxypeptidase A inhibitor or ACE inhibitors
- KM=6.9 uM for angiotensin 1
- KM=2 uM for angiotensin 2
- KM=6.8 uM for apelin-13
- KM=5.5 uM for dynorphin-13
- pH dependence:
Compartment
- membrane protein
- processing by ADAM17 may lead to a secreted protein
Expression
- endothelial cells* from
- small & large arteries
- arterial smooth muscle cells
- lung alveolar epithelial cells (pneumocytes)*
- myofiber membrane of the diaphragm muscle[6]
- enterocytes of the small intestine*
- Leydig cells
- Sertoli cells
- heart*, up-regulated in failing heart
- kidney*
- testis*
- gastrointestinal system
* high levels of expression
* expression upregulated by the farnesyl X receptor (FXR)[7]
Pathology
- functional receptor for human coronaviruses, SARS & NL63 including SARS CoV2[5]
- SARS CoV spike glyxoprotein receptor is ACE2
- cell entry of SARS CoV2 also requires proteolysis of spike glycoprotein by cell surface serine protease TMPRSS2 expressed on type II pneumocytes
- N-glycosylation on Asn-90 may limit SARS infectivity[2]
- SARS CoV spike glyxoprotein receptor is ACE2
More general terms
Additional terms
- angiotensin I
- angiotensin II (Giapreza)
- angiotensin-converting enzyme (ACE) in serum/plasma/blood
- SARS-CoV
References
- ↑ OMIM https://mirror.omim.org/entry/300335
- ↑ 2.0 2.1 Li W, Moore MJ, Vasilieva N, Sui J, Wong SK, Berne MA et al Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature. 2003 Nov 27;426(6965):450-4. PMID: https://www.ncbi.nlm.nih.gov/pubmed/14647384
- ↑ SeattleSNPs http://pga.gs.washington.edu/data/ace2/
- ↑ UniProt http://www.uniprot.org/uniprot/Q9BYF1.html
- ↑ 5.0 5.1 Hoffmann M, Kleine-Weber H, Schroeder S SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell. 2020 Mar 4. pii: S0092-8674(20)30229-4. PMID: https://www.ncbi.nlm.nih.gov/pubmed/32142651
- ↑ 6.0 6.1 Shi Z, de Vries HJ, Vlaar APJ et al Diaphragm Pathology in Critically Ill Patients With COVID-19 and Postmortem Findings From 3 Medical Centers. JAMA Intern Med. Published online November 16, 2020. PMID: https://www.ncbi.nlm.nih.gov/pubmed/33196760 PMCID: PMC7670391 Free PMC article https://jamanetwork.com/journals/jamainternalmedicine/fullarticle/2773060
- ↑ 7.0 7.1 Brevini T, Maes M, Webb GJ et al FXR inhibition may protect from SARS-CoV-2 infection by reducing ACE2. Nature 2022. Dec 5. PMID: https://www.ncbi.nlm.nih.gov/pubmed/36470304 https://www.nature.com/articles/s41586-022-05594-0