Angiotensin-Converting Enzyme 2

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Gavin Y. Oudit - One of the best experts on this subject based on the ideXlab platform.

  • angiotensin converting Enzyme 2 sars cov 2 receptor and regulator of the renin angiotensin system celebrating the 20th anniversary of the discovery of ace2
    Circulation Research, 2020
    Co-Authors: Mahmoud Gheblawi, Anthony J. Turner, Jiu-chang Zhong, Kaiming Wang, Anissa Viveiros, Quynh Nguyen, Mohan K Raizada, Maria B Grant, Gavin Y. Oudit
    Abstract:

    ACE2 (Angiotensin-Converting Enzyme 2) has a multiplicity of physiological roles that revolve around its trivalent function: a negative regulator of the renin-angiotensin system, facilitator of ami...

  • murine recombinant angiotensin converting Enzyme 2 attenuates kidney injury in experimental alport syndrome
    Kidney International, 2017
    Co-Authors: Fei Fang, Vaibhav B Patel, Ana Konvalinka, Vanessa Williams, Xuewen Song, Rohan John, Xiaohua Zhou, Gavin Y. Oudit, James W. Scholey
    Abstract:

    Angiotensin-Converting Enzyme 2 (ACE2) is a monocarboxypeptidase in the renin-angiotensin system that catalyzes the breakdown of angiotensin II to angiotensin 1-7. We have reported that ACE2 expression in the kidney is reduced in experimental Alport syndrome but the impact of this finding on disease progression has not been studied. Accordingly, we evaluated effects of murine recombinant ACE2 treatment in Col4a3 knockout mice, a model of Alport syndrome characterized by proteinuria and progressive renal injury. Murine recombinant ACE2 (0.5 mg/kg/day) was administered from four to seven weeks of age via osmotic mini-pump. Pathological changes were attenuated by murine recombinant ACE2 treatment which ameliorated kidney fibrosis as shown by decreased expression of COL1α1 mRNA, less accumulation of extracellular matrix proteins, and inhibition of transforming growth factor-β signaling. Further, increases in proinflammatory cytokine expression, macrophage infiltration, inflammatory signaling pathway activation, and heme oxygenase-1 levels in Col4a3 knockout mice were also reduced by murine recombinant ACE2 treatment. Lastly, murine recombinant ACE2 influenced the turnover of renal ACE2, as it suppressed the expression of tumor necrosis factor-α converting Enzyme, a negative regulator of ACE2. Thus, treatment with exogenous ACE2 alters angiotensin peptide metabolism in the kidneys of Col4a3 knockout mice and attenuates the progression of Alport syndrome nephropathy.

  • Targeting Angiotensin-Converting Enzyme 2 as a new therapeutic target for cardiovascular diseases.
    Canadian Journal of Physiology and Pharmacology, 2014
    Co-Authors: Nirmal Parajuli, Vaibhav B Patel, Wang Da-wang, Tharmarajan Ramprasath, Brendan N. Putko, Jun Mori, Gavin Y. Oudit
    Abstract:

    Angiotensin-Converting Enzyme 2 (ACE2) is a monocarboxypeptidase that metabolizes several vasoactive peptides, including angiotensin II (Ang-II; a vasoconstrictive/proliferative peptide), which it converts to Ang-(1–7). Ang-(1–7) acts through the Mas receptor to mediate vasodilatory/antiproliferative actions. The renin–angiotensin system involving the ACE–Ang-II–Ang-II type-1 receptor (AT1R) axis is antagonized by the ACE2–Ang-(1–7)–Mas receptor axis. Loss of ACE2 enhances adverse remodeling and susceptibility to pressure and volume overload. Human recombinant ACE2 may act to suppress myocardial hypertrophy, fibrosis, inflammation, and diastolic dysfunction in heart failure patients. The ACE2–Ang-(1–7)–Mas axis may present a new therapeutic target for the treatment of heart failure patients. This review is mainly focused on the analysis of ACE2, including its influence and potentially positive effects, as well as the potential use of human recombinant ACE2 as a novel therapy for the treatment cardiovascul...

  • cardiac protective effects of irbesartan via the ppar gamma signaling pathway in angiotensin converting Enzyme 2 deficient mice
    Journal of Translational Medicine, 2013
    Co-Authors: Zhen-zhou Zhang, Gavin Y. Oudit, Josef M. Penninger, Ying-le Xu, Bei Song, Qianhui Shang, Lin Lu, Tong Zhou, Jiu-chang Zhong
    Abstract:

    Background Angiotensin-Converting Enzyme 2 (ACE2), a monocarboxypeptidase which metabolizes angiotensin II (Ang II) to generate Ang-(1–7), has been shown to prevent cardiac hypertrophy and injury but the mechanism remains elusive. Irbesartan has the dual actions of angiotensin receptor blockade and peroxisome proliferator-activated receptor-γ (PPARγ) activation. We hypothesized that irbesartan would exert its protective effects on ACE2 deficiency-mediated myocardial fibrosis and cardiac injury via the PPARγ signaling.

  • Angiotensin-Converting Enzyme 2 is an essential regulator of heart function
    Nature, 2002
    Co-Authors: Michael A. Crackower, Gavin Y. Oudit, Renu Sarao, Chana Yagil, Ivona Kozieradzki, Sam Scanga, Antonio J. Oliveira-dos-santos, Joan Da Costa, Liyong Zhang
    Abstract:

    Cardiovascular diseases are predicted to be the most common cause of death worldwide by 2020. Here we show that Angiotensin-Converting Enzyme 2 (ace2) maps to a defined quantitative trait locus (QTL) on the X chromosome in three different rat models of hypertension. In all hypertensive rat strains, ACE2 messenger RNA and protein expression were markedly reduced, suggesting that ace2 is a candidate gene for this QTL. Targeted disruption of ACE2 in mice results in a severe cardiac contractility defect, increased angiotensin II levels, and upregulation of hypoxia-induced genes in the heart. Genetic ablation of ACE on an ACE2 mutant background completely rescues the cardiac phenotype. But disruption of ACER, a Drosophila ACE2 homologue, results in a severe defect of heart morphogenesis. These genetic data for ACE2 show that it is an essential regulator of heart function in vivo.

Xing-yi Ge - One of the best experts on this subject based on the ideXlab platform.

  • predicting the angiotensin converting Enzyme 2 ace2 utilizing capability as the receptor of sars cov 2
    Microbes and Infection, 2020
    Co-Authors: Yuan-bo Zhao, Qiong Wang, Jin-yan Li, Zhi-jian Zhou, Ce-heng Liao, Xing-yi Ge
    Abstract:

    SARS-CoV-2, the newly identified human coronavirus causing severe pneumonia pandemic, was probably originated from Chinese horseshoe bats. However, direct transmission of the virus from bats to humans is unlikely due to lack of direct contact, implying the existence of unknown intermediate hosts. Angiotensin converting Enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2s of certain species can be utilized by SARS-CoV-2. Here, we evaluated and ranked the receptor-utilizing capability of ACE2s from various species by phylogenetic clustering and sequence alignment with the currently known ACE2s utilized by SARS-CoV-2. As a result, we predicted that SARS-CoV-2 tends to utilize ACE2s of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2.

  • Predicting the Angiotensin Converting Enzyme 2 (ACE2) Utilizing Capability as the Receptor of SARS-CoV-2
    2020
    Co-Authors: Yuan-bo Zhao, Qiong Wang, Jin-yan Li, Zhi-jian Zhou, Ce-heng Liao, Xing-yi Ge
    Abstract:

    SARS-CoV-2, the newly identified human coronavirus causing severe pneumonia epidemic, was probably originated from Chinese horseshoe bats. However, direct transmission of the virus from bats to humans is unlikely due to lack of direct contact, implying the existence of unknown intermediate hosts. Angiotensin converting Enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2s of certain species can be utilized by SARS-CoV-2. Here, we evaluated and ranked the receptor-utilizing capability of ACE2s from various species by phylogenetic clustering and sequence alignment with the currently known ACE2s utilized by SARS-CoV-2, predicting potential intermediate hosts of SARS-CoV-2.

Wenhui Li - One of the best experts on this subject based on the ideXlab platform.

  • Angiotensin-Converting Enzyme 2, the Cellular Receptor for Severe Acute Respiratory Syndrome Coronavirus and Human Coronavirus NL63
    Nidoviruses, 2008
    Co-Authors: Wenhui Li, Hyeryun Choe, Michael Farzan
    Abstract:

    The identification of a viral receptor can make a significant contribution to our understanding of viral pathogenesis and viral evolution, and to the development of vaccines and antiviral therapeutics. This chapter describes the shared cellular receptor for severe acute respiratory syndrome coronavirus (SARS-CoV) and human coronavirus NL63 (HCoVNL63). Identification of this receptor contributed to our understanding of the zoonotic transmission of SARS-CoV and of the distinctive entry mechanisms of both SARS-CoV and HCoV-NL63. These are discussed in the context of the structure of the SARS-CoV S protein receptor-binding domain (RBD) bound to this common receptor, Angiotensin-Converting Enzyme 2 (ACE2). Functional studies of the viral receptor, described in the chapter, support a critical role for palm civets in transmitting virus to humans.

  • a 193 amino acid fragment of the sars coronavirus s protein efficiently binds angiotensin converting Enzyme 2
    Journal of Biological Chemistry, 2004
    Co-Authors: Swee Kee Wong, Hyeryun Choe, Wenhui Li, Michael J. Moore, Michael Farzan
    Abstract:

    Abstract The coronavirus spike (S) protein mediates infection of receptor-expressing host cells and is a critical target for antiviral neutralizing antibodies. Angiotensin-Converting Enzyme 2 (ACE2) is a functional receptor for the coronavirus (severe acute respiratory syndrome (SARS)-CoV) that causes SARS. Here we demonstrate that a 193-amino acid fragment of the S protein (residues 318–510) bound ACE2 more efficiently than did the full S1 domain (residues 12–672). Smaller S protein fragments, expressing residues 327–510 or 318–490, did not detectably bind ACE2. A point mutation at aspartic acid 454 abolished association of the full S1 domain and of the 193-residue fragment with ACE2. The 193-residue fragment blocked S protein-mediated infection with an IC50 of less than 10 nm, whereas the IC50 of the S1 domain was ∼50 nm. These data identify an independently folded receptor-binding domain of the SARS-CoV S protein.

  • angiotensin converting Enzyme 2 is a functional receptor for the sars coronavirus
    Nature, 2003
    Co-Authors: Wenhui Li, Natalya Vasilieva, Jianhua Sui, Swee Kee Wong, Michael A Berne, Mohan Somasundaran, Katherine Luzuriaga, John L. Sullivan, Michael J. Moore, Thomas C Greenough
    Abstract:

    Spike (S) proteins of coronaviruses, including the coronavirus that causes severe acute respiratory syndrome (SARS), associate with cellular receptors to mediate infection of their target cells1,2. Here we identify a metallopeptidase, Angiotensin-Converting Enzyme 2 (ACE2)3,4, isolated from SARS coronavirus (SARS-CoV)-permissive Vero E6 cells, that efficiently binds the S1 domain of the SARS-CoV S protein. We found that a soluble form of ACE2, but not of the related Enzyme ACE1, blocked association of the S1 domain with Vero E6 cells. 293T cells transfected with ACE2, but not those transfected with human immunodeficiency virus-1 receptors, formed multinucleated syncytia with cells expressing S protein. Furthermore, SARS-CoV replicated efficiently on ACE2-transfected but not mock-transfected 293T cells. Finally, anti-ACE2 but not anti-ACE1 antibody blocked viral replication on Vero E6 cells. Together our data indicate that ACE2 is a functional receptor for SARS-CoV.

Anthony J. Turner - One of the best experts on this subject based on the ideXlab platform.

  • Angiotensin-Converting Enzyme-2 (ACE2)
    xPharm: The Comprehensive Pharmacology Reference, 2020
    Co-Authors: Anthony J. Turner, Nigel M. Hooper
    Abstract:

    Angiotensin-Converting Enzyme-2 (ACE2) may be involved in the physiological metabolism of angiotensin II to angiotensin(1–7) …

  • angiotensin converting Enzyme 2 sars cov 2 receptor and regulator of the renin angiotensin system celebrating the 20th anniversary of the discovery of ace2
    Circulation Research, 2020
    Co-Authors: Mahmoud Gheblawi, Anthony J. Turner, Jiu-chang Zhong, Kaiming Wang, Anissa Viveiros, Quynh Nguyen, Mohan K Raizada, Maria B Grant, Gavin Y. Oudit
    Abstract:

    ACE2 (Angiotensin-Converting Enzyme 2) has a multiplicity of physiological roles that revolve around its trivalent function: a negative regulator of the renin-angiotensin system, facilitator of ami...

  • Angiotensin-Converting Enzyme 2
    Handbook of Proteolytic Enzymes, 2012
    Co-Authors: Anthony J. Turner, Nigel M. Hooper
    Abstract:

    Publisher Summary This chapter describes the activity, specificity and structural chemistry of Angiotensin-Converting Enzyme 2 (ACE2). The complete cDNA for human ACE2 encodes a protein of 805 amino acids that exhibits 40% identity and 61% similarity to human ACE. Human ACE2 is a type I integral membrane protein which contains a 17 amino acid N-terminal signal sequence and a 22 amino acid hydrophobic transmembrane sequence near the C-terminus followed by a 43 amino acid cytoplasmic domain, which contains potential phosphorylation sites. The juxtamembrane, transmembrane and cytoplasmic domains of ACE2 do not resemble ACE but share similarity with a 220 amino acid transmembrane glycoprotein termed collectrin, which is localized to the renal collecting ducts. Collectrin has no protease domain and its function is unknown. The homology of ACE2 and ACE is particularly striking around the HEXXH zinc-binding motif which is identical in the two proteins. ACE2 also contains eight cysteine residues, six of which are conserved in the N- and C-terminal domains of endothelial ACE, and has seven potential Af-linked glycosylation sites. The ACE2 gene, located on chromosome Xp22, contains 18 exons and many of those resemble the corresponding exons in the ACE gene.

  • Calmodulin interacts with Angiotensin-Converting Enzyme-2 (ACE2) and inhibits shedding of its ectodomain
    FEBS Letters, 2007
    Co-Authors: Daniel W. Lambert, Nigel M. Hooper, Nicola E. Clarke, Anthony J. Turner
    Abstract:

    Angiotensin-Converting Enzyme-2 (ACE2) is a regulatory protein of the renin–angiotensin system (RAS) and a receptor for the causative agent of severe-acute respiratory syndrome (SARS), the SARS-coronavirus. We have previously shown that ACE2 can be shed from the cell surface in response to phorbol esters by a process involving TNF-α converting Enzyme (TACE; ADAM17). In this study, we demonstrate that inhibitors of calmodulin also stimulate shedding of the ACE2 ectodomain, a process at least partially mediated by a metalloproteinase. We also show that calmodulin associates with ACE2 and that this interaction is decreased by calmodulin inhibitors.

  • angiotensin converting Enzyme 2 ace2 comparative modeling of the active site specificity requirements and chloride dependence
    Biochemistry, 2003
    Co-Authors: Richard M Jackson, Nigel M. Hooper, Ravi K Acharya, Edward D Sturrock, Anthony J. Turner
    Abstract:

    Angiotensin-Converting Enzyme 2 (ACE2), a homologue of ACE, represents a new and potentially important target in cardio-renal disease. A model of the active site of ACE2, based on the crystal structure of testicular ACE, has been developed and indicates that the catalytic mechanism of ACE2 resembles that of ACE. Structural differences exist between the active site of ACE (dipeptidyl carboxypeptidase) and ACE2 (carboxypeptidase) that are responsible for the differences in specificity. The main differences occur in the ligand-binding pockets, particularly at the S2‘ subsite and in the binding of the peptide carboxy-terminus. The model explains why the classical ACE inhibitor lisinopril is unable to bind to ACE2. On the basis of the ability of ACE2 to cleave a variety of biologically active peptides, a consensus sequence of Pro-X-Pro-hydrophobic/basic for the protease specificity of ACE2 has been defined that is supported by the ACE2 model. The dipeptide, Pro-Phe, completely inhibits ACE2 activity at 180 μM ...

Jiu-chang Zhong - One of the best experts on this subject based on the ideXlab platform.

Related terms

  • renin angiotensin system
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