ACE2 entsyymi on dipeptidyylikarboksypeptidaasien perhettä, kardioprotektiivinen

https://www.ncbi.nlm.nih.gov/gene/59272

Official Symbol

ACE2provided by

Official Full Name

angiotensin I converting enzyme 2

Also known as

ACEH

Summary

The protein encoded by this gene belongs to the angiotensin-converting enzyme family of dipeptidyl carboxydipeptidases and has considerable homology to human angiotensin 1 converting enzyme. This secreted protein catalyzes the cleavage of angiotensin I into angiotensin 1-9, and angiotensin II into the vasodilator angiotensin 1-7. The organ- and cell-specific expression of this gene suggests that it may play a role in the regulation of cardiovascular and renal function, as well as fertility. In addition, the encoded protein is a functional receptor for the spike glycoprotein of the human coronaviruses SARS and HCoV-NL63. [provided by RefSeq, Jul 2008]

Expression

Biased expression in small intestine (RPKM 93.7), duodenum (RPKM 69.0) and 5 other tissues See more

Orthologs

 

1. Hypertension and hypertensive left ventricular hypertrophy are associated with ACE2 genetic polymorphism. Fan Z, et al. Life Sci, 2019 May 15. PMID 30917908
2. RhoA-Rho associated kinase signaling leads to renin-angiotensin system imbalance and angiotensin converting enzyme 2 has a protective role in acute pulmonary embolism. Xu X, et al. Thromb Res, 2019 Apr. PMID 30784777
3. Degradation of Lung Protective Angiotensin Converting Enzyme-2 by Meconium in Human Alveolar Epithelial Cells: A Potential Pathogenic Mechanism in Meconium Aspiration Syndrome. Gandhi CK, et al. Lung, 2019 Apr. PMID 30759273
4. A review of urinary angiotensin converting enzyme 2 in diabetes and diabetic nephropathy. Gilbert A, et al. Biochem Med (Zagreb), 2019 Feb 15. PMID 30591810, Free PMC Article
5. Evidence for a role of angiotensin converting enzyme 2 in proteinuria of idiopathic nephrotic syndrome. Filha RDS, et al. Biosci Rep, 2019 Jan 31. PMID 30514826, Free PMC Article

See all (266) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

What's a GeneRIF?

1. Meconium causes degradation of lung protective ACE-2 by proteolytic enzymes present in meconium, leading to meconium aspiration syndrome.
2. A strong association of circulating miR-421 with decreased transcripts of ACE2 may contribute to the low expression of the enzyme in leukocytes of chronic kidney disease patients
3. RhoA-ROCK signaling leads to renin-angiotensin system imbalance in acute pulmonary embolism patients, and ACE2 activation might be a novel therapeutic target in acute pulmonary embolism treatment.
4. Our findings suggest that ACE2, as a potential resister to breast cancer, might inhibit breast cancer angiogenesis through the VEGFa/VEGFR2/ERK pathway.
5. We have hypothesized the mechanism that reverses the downregulation of the ACE2-angiotensin 1-7/Mas receptor axis path and the upregulation of angiotensin receptor type 1-mediated signaling. Thus, we posit that ACE2, Ang-(1-7), and the Mas receptor could be novel therapeutic targets for treating benign prostatic hyperplasia
6. Evidence for a role of ACE2 in pediatric proteinuria of idiopathic nephrotic syndrome has been presented.
7. Urinary ACE2, neprilysin, and ADAM17 are increased in patients with diabetes and could be used as early biomarkers to predict the incidence or progression of CKD at early stages among individuals with type 2 diabetes.Abstract
   Angiotensin converting enzyme 2 (ACE2) and neprilysin (NEP) are metalloproteases that are highly expressed in the renal proximal tubules. ACE2 and NEP generate renoprotective angiotensin (1-7) from angiotensin II and angiotensin I, respectively, and therefore could have a major role in chronic kidney disease (CKD). Recent data demonstrated increased urinary ACE2 in patients with diabetes with CKD and kidney transplants. We tested the hypothesis that urinary ACE2, NEP, and a disintegrin and metalloproteinase 17 (ADAM17) are increased and could be risk predictors of CKD in patients with diabetes. ACE2, NEP, and ADAM17 were investigated in 20 nondiabetics (ND) and 40 patients with diabetes with normoalbuminuria (Dnormo), microalbuminuria (Dmicro), and macroalbuminuria (Dmacro) using ELISA, Western blot, and fluorogenic and mass spectrometric-based enzyme assays. Logistic regression model was applied to predict the risk prediction. Receiver operating characteristic curves were drawn, and prediction accuracies were calculated to explore the effectiveness of ACE2 and NEP in predicting diabetes and CKD. Results demonstrated that there is no evidence of urinary ACE2 and ADAM17 in ND subjects, but both enzymes were increased in patients with diabetes, including Dnormo. Although there was no detectable plasma ACE2 activity, there was evidence of urinary and plasma NEP in all the subjects, and urinary NEP was significantly increased in Dmicro patients. NEP and ACE2 showed significant correlations with metabolic and renal characteristics. In summary, urinary ACE2, NEP, and ADAM17 are increased in patients with diabetes and could be used as early biomarkers to predict the incidence or progression of CKD at early stages among individuals with type 2 diabetes.
8. ACE2 genetic polymorphisms are associated with hypertension and hypertensive left ventricular hypertrophy.
9. REVIEW: recent findings on expression of urinary ACE2, examination of its relationship with clinical parameters and highlights possible applications in management of diabetic nephropathy

 

1. down-regulation of lncRNA GAS5 decreases ACE2 expression through increasing miR-200c-3p to promote the apoptosis of A549 cells, thus to promote the progression of acute respiratory distress syndrome (ARDS)

 

ACE2 entsyymin tarkempi rakenne: https://www.ncbi.nlm.nih.gov/protein/NP_068576.1
Siinä on aminohappoja 1..805.
Se on metallopeptidaasi ja sitoo sinkkiä aminohapoilla 374, 378 ja 402 .


https://www.biorxiv.org/content/10.1101/2020.02.17.951848v
 Abstract

Angiotensin-converting enzyme 2 (ACE2) is the surface receptor for SARS coronavirus (SARS-CoV), directly interacting with the spike glycoprotein (S protein). ACE2 is also suggested to be the receptor for the new coronavirus (2019-nCoV), which is causing a serious epidemic in China manifested with severe respiratory syndrome. B⁰AT1 (SLC6A19) is a neutral amino acid transporter whose surface expression in intestinal cells requires ACE2. Here we present the 2.9 Å resolution cryo-EM structure of full-length human ACE2 in complex with B⁰AT1. The complex, assembled as a dimer of ACE2-B⁰AT1 heterodimers, exhibits open and closed conformations due to the shifts of the peptidase domains (PDs) of ACE2. A newly resolved Collectrin-like domain (CLD) on ACE2 mediates homo-dimerization. Structural modelling suggests that the ACE2-B⁰AT1 complex can bind two S proteins simultaneously, providing important clues to the molecular basis for coronavirus recognition and infection.