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      Organ-specific distribution of ACE2 mRNA and correlating peptidase activity in rodents

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          Abstract

          Biochemical analysis revealed that angiotensin-converting enzyme related carboxy-peptidase (ACE2) cleaves angiotensin (Ang) II to Ang-(1–7), a heptapeptide identified as an endogenous ligand for the G protein-coupled receptor Mas. No data are currently available that systematically describe ACE2 distribution and activity in rodents. Therefore, we analyzed the ACE2 expression in different tissues of mice and rats on mRNA (RNase protection assay) and protein levels (immunohistochemistry, ACE2 activity, western blot). Although ACE2 mRNA in both investigated species showed the highest expression in the ileum, the mouse organ exceeded rat ACE2, as also demonstrated in the kidney and colon. Corresponding to mRNA, ACE2 activity was highest in the ileum and mouse kidney but weak in the rat kidney, which was also confirmed by immunohistochemistry. Contrary to mRNA, we found weak activity in the lung of both species. Our data demonstrate a tissue- and species-specific pattern for ACE2 under physiological conditions.

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          Susceptibility to SARS coronavirus S protein-driven infection correlates with expression of angiotensin converting enzyme 2 and infection can be blocked by soluble receptor

          Heike Hofmann, Martina Geier, Andrea Marzi … (2004)
          The angiotensin converting enzyme 2 (ACE2) has been identified as a receptor for the severe acute respiratory syndrome associated coronavirus (SARS-CoV). Here we show that ACE2 expression on cell lines correlates with susceptibility to SARS-CoV S-driven infection, suggesting that ACE2 is a major receptor for SARS-CoV. The soluble ectodomain of ACE2 specifically abrogated S-mediated infection and might therefore be exploited for the generation of inhibitors. Deletion of a major portion of the cytoplasmic domain of ACE2 had no effect on S-driven infection, indicating that this domain is not important for receptor function. Our results point to a central role of ACE2 in SARS-CoV infection and suggest a minor contribution of the cytoplasmic domain to receptor function.
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            The angiotensin-converting enzyme gene family: genomics and pharmacology.

            Anthony Turner, Nigel Hooper (2002)
            Modulation of the renin-angiotensin system (RAS), and particularly inhibition of angiotensin-converting enzyme (ACE), a zinc metallopeptidase, has long been a prime strategy in the treatment of hypertension. However, other angiotensin metabolites are gaining in importance as our understanding of the RAS increases. Recently, genomic approaches have identified the first human homologue of ACE, termed ACEH (or ACE2). ACEH differs in specificity and physiological roles from ACE, which opens a potential new area for discovery biology. The gene that encodes collectrin, a homologue of ACEH, is upregulated in response to renal injury. Collectrin lacks a catalytic domain, which indicates that there is more to ACE-like function than simple peptide hydrolysis.
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              The role of ACE2 in cardiovascular physiology.

              Gavin Y. Oudit, Michael A. Crackower, Peter Backx … (2003)
              The renin-angiotensin system (RAS) is critically involved in cardiovascular and renal function and in disease conditions, and has been shown to be a far more complex system than initially thought. A recently discovered homologue of angiotensin-converting enzyme (ACE)--ACE2--appears to negatively regulate the RAS. ACE2 cleaves Ang I and Ang II into the inactive Ang 1-9 and Ang 1-7, respectively. ACE2 is highly expressed in kidney and heart and is especially confined to the endothelium. With quantitative trait locus (QTL) mapping, ACE2 was defined as a QTL on the X chromosome in rat models of hypertension. In these animal models, kidney ACE2 messenger RNA and protein expression were markedly reduced, making ACE2 a candidate gene for this QTL. Targeted disruption of ACE2 in mice failed to elicit hypertension, but resulted in severe impairment in myocardial contractility with increased angiotensin II levels. Genetic ablation of ACE in the ACE2 null mice rescued the cardiac phenotype. These genetic data show that ACE2 is an essential regulator of heart function in vivo. Basal renal morphology and function were not altered by the inactivation of ACE2. The novel role of ACE2 in hydrolyzing several other peptides-such as the apelin peptides, opioids, and kinin metabolites-raises the possibility that peptide systems other than angiotensin and its derivatives also may have an important role in regulating cardiovascular and renal function.
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                Author and article information

                Contributors
                Thomas Walther
                Journal
                Journal ID (nlm-ta): Peptides
                Journal ID (iso-abbrev): Peptides
                Title: Peptides
                Publisher: Elsevier Inc.
                ISSN (Print): 0196-9781
                ISSN (Electronic): 1873-5169
                Publication date PMC-release: 16 February 2005
                Publication date (Print): July 2005
                Publication date (Electronic): 16 February 2005
                Volume: 26
                Issue: 7
                Pages: 1270-1277
                Affiliations
                [a ]Department of Cardiology, Charité, Campus Benjamin Franklin (CBF), Germany
                [b ]Department of Pharmacology, Erasmus Medical Center, Dr. Molewaterplein 50, Room: Ee14-00b, 3015 GE Rotterdam, The Netherlands
                [c ]Institute for Veterinary Pathology, Freie Universitat, Berlin, Germany
                [d ]Institute of Cell Biology, University of Bern, Bern, Switzerland
                [e ]Research Institute of Molecular Pharmacology, Berlin-Buch, Germany
                Author notes
                [* ]Corresponding author. Tel.: +31 10 4087530; fax: +31 10 4089458. t.walther@ 123456erasmusmc.nl
                Article
                Publisher ID: S0196-9781(05)00021-5
                DOI: 10.1016/j.peptides.2005.01.009
                PMC ID: 7115528
                PubMed ID: 15949646
                SO-VID: 6d22811c-132d-43cd-8ee7-557c5ba229b1
                Copyright © Copyright © 2005 Elsevier Inc. All rights reserved.
                License:

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

                History
                Date received : 22 November 2004
                Date revision received : 8 January 2005
                Date accepted : 11 January 2005
                Categories
                Subject: Article

                ScienceOpen disciplines: Biochemistry
                Keywords: angiotensin-converting enzyme 2,enzyme activity,peptidase,tissue distribution,renin–angiotensin system
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: angiotensin-converting enzyme 2, enzyme activity, peptidase, tissue distribution, renin–angiotensin system

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