Angiotensin converting enzyme 2 as the molecular bridge between epidemiologic and clinical features of COVID-19
Identifieur interne : 000450 ( Pmc/Corpus ); précédent : 000449; suivant : 000451Angiotensin converting enzyme 2 as the molecular bridge between epidemiologic and clinical features of COVID-19
Auteurs : Tonino Bombardini ; Eugenio PicanoSource :
- The Canadian Journal of Cardiology [ 0828-282X ] ; 2020.
Url:
DOI: 10.1016/j.cjca.2020.03.026
PubMed: 32299780
PubMed Central: 7118531
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PMC:7118531Le document en format XML
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<author><name sortKey="Bombardini, Tonino" sort="Bombardini, Tonino" uniqKey="Bombardini T" first="Tonino" last="Bombardini">Tonino Bombardini</name>
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<author><name sortKey="Picano, Eugenio" sort="Picano, Eugenio" uniqKey="Picano E" first="Eugenio" last="Picano">Eugenio Picano</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Angiotensin converting enzyme 2 as the molecular bridge between epidemiologic and clinical features of COVID-19</title>
<author><name sortKey="Bombardini, Tonino" sort="Bombardini, Tonino" uniqKey="Bombardini T" first="Tonino" last="Bombardini">Tonino Bombardini</name>
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<author><name sortKey="Picano, Eugenio" sort="Picano, Eugenio" uniqKey="Picano E" first="Eugenio" last="Picano">Eugenio Picano</name>
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<series><title level="j">The Canadian Journal of Cardiology</title>
<idno type="ISSN">0828-282X</idno>
<idno type="eISSN">1916-7075</idno>
<imprint><date when="2020">2020</date>
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<biblStruct><analytic><author><name sortKey="Zisman, L S" uniqKey="Zisman L">L.S. Zisman</name>
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<biblStruct><analytic><author><name sortKey="Imai, Y" uniqKey="Imai Y">Y. Imai</name>
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<author><name sortKey="Kuba, K" uniqKey="Kuba K">K. Kuba</name>
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<author><name sortKey="Rao, S" uniqKey="Rao S">S. Rao</name>
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<pmc article-type="letter"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Can J Cardiol</journal-id>
<journal-id journal-id-type="iso-abbrev">Can J Cardiol</journal-id>
<journal-title-group><journal-title>The Canadian Journal of Cardiology</journal-title>
</journal-title-group>
<issn pub-type="ppub">0828-282X</issn>
<issn pub-type="epub">1916-7075</issn>
<publisher><publisher-name>Canadian Cardiovascular Society. Published by Elsevier Inc.</publisher-name>
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<article-meta><article-id pub-id-type="pmid">32299780</article-id>
<article-id pub-id-type="pmc">7118531</article-id>
<article-id pub-id-type="publisher-id">S0828-282X(20)30299-3</article-id>
<article-id pub-id-type="doi">10.1016/j.cjca.2020.03.026</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
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<title-group><article-title>Angiotensin converting enzyme 2 as the molecular bridge between epidemiologic and clinical features of COVID-19</article-title>
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<contrib-group><contrib contrib-type="author" id="au1"><name><surname>Bombardini</surname>
<given-names>Tonino</given-names>
</name>
<degrees>MD, PhD</degrees>
<role>Cardiologist</role>
<email>tbombardini@yahoo.it</email>
<xref rid="cor1" ref-type="corresp">∗</xref>
</contrib>
<contrib contrib-type="author" id="au2"><name><surname>Picano</surname>
<given-names>Eugenio</given-names>
</name>
<degrees>MD, PhD</degrees>
<role>Cardiologist</role>
</contrib>
</contrib-group>
<aff id="aff1"><label>1</label>
CNR, Consiglio Nazionale Ricerche - National Research Council, Institute of Clinical Physiology, Biomedicine Department, Pisa, Italy</aff>
<author-notes><corresp id="cor1"><label>∗</label>
Address for correspondence:Tonino Bombardini, MD, PhD. Tel: +39050 3152398 Fax: +390503152374 <email>tbombardini@yahoo.it</email>
</corresp>
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<pub-date pub-type="pmc-release"><day>29</day>
<month>3</month>
<year>2020</year>
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<pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="epub"><day>29</day>
<month>3</month>
<year>2020</year>
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<history><date date-type="received"><day>18</day>
<month>3</month>
<year>2020</year>
</date>
<date date-type="accepted"><day>18</day>
<month>3</month>
<year>2020</year>
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<permissions><copyright-statement>© 2020 Canadian Cardiovascular Society. Published by Elsevier Inc. All rights reserved.</copyright-statement>
<copyright-year>2020</copyright-year>
<copyright-holder></copyright-holder>
<license><license-p>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.</license-p>
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<body><p id="p0010">Pre-existent cardiovascular disease is a recognized risk factor for COVID-19 infection (<xref rid="bib1" ref-type="bibr">1</xref>
). COVID-19 spike protein uses the angiotensin-converting-enzyme 2 (ACE2) as the binding site to enter the host cell in tongue, bronchi and lungs. Any condition enhancing the expression of ACE2 would increase the vulnerability to infection. Heart failure, coronary artery disease, hypertension, diabetes, ACE inhibitors (ACEi) or angiotensin receptor blockers (ARBs) increase the expression of ACE2, which can be considered nature's endogenous ACE inhibitor at the cellular level. The renin-angiotensin system has 2 arms (<xref rid="fig1" ref-type="fig">Figure 1</xref>
, upper panel): the pressor (conventional) arm, composed of Angiotensin II, angiotensin-converting-enzyme (ACE), Angiotensin II-type 1 receptor (AT1R), and the depressor (non conventional) arm consisting of Angiotensin 1-7, ACE2, MAS receptor (MAS R) and Angiotensin II, type 2 receptor (AT2R) (<xref rid="bib2" ref-type="bibr">2</xref>
). The ACE2 (the "good" guy, possibly "the best of enzymes") arm opposes the conventional arm and has beneficial effects in heart failure and acute respiratory distress syndrome (ARDS) (<xref rid="bib3" ref-type="bibr">3</xref>
). COVID-19 spike protein is the "ugly" character in the play. It uses the "good" ACE2 as the binding site. While ACE is detectable in the entire capillary network of the alveoli in the human lung, ACE2 is primarily produced in club cells of distal bronchioles and type 2 pneumocytes in alveolar epithelium. Both cell types are involved in preventing ARDS. Club cells secrete a solution similar to surfactant and proteins protective against airway inflammation and oxidative stress. Type-2 pneumocytes are "the defender of the alveolus" and synthesize, secrete and recycle all components of the surfactant that regulates alveolar surface tension in the lungs. The binding of COVID-19 spike protein to ACE2 down-regulates the enzyme, which in turn may contribute to ARDS for the unopposed, detrimental action of ACE (the "bad" guy or "the worst of enzymes") on lung tissue, triggering vasoconstriction, inflammation, apoptosis and fibrosis. (<xref rid="fig1" ref-type="fig">Figure 1</xref>
, lower panel). The CHT)" title="https://www.escardio.org/Councils/Council-on-Hypertension-(CHT)">Council on Hypertension of the European Society of Cardiology (<xref rid="bib4" ref-type="bibr">4</xref>
) highlighted the lack of any evidence supporting harmful effect of ACEi and ARBs in the context of the pandemic COVID-19 outbreak. This is important since an hypothesis suggests that ACEi might be helpful in treating COVID-19 ARDS. Chongqing Medical University is currently conducting a retrospective observational study that aims to evaluate the clinical differences between adult hypertensive patients with COVID-19 treated and those not treated with ACEi. This study will be completed by April 30, 2020.<fig id="fig1"><label>Figure 1</label>
<caption><p><bold>Upper panel:</bold>
The normal physiology of ACE (the worst of all enzymes) and ACE2 (the best of all enzymes). COVID-19 uses ACE2 (in club cells in distal bronchioli and pneumocytes type 2 cells in alveoli) as a binding site. <bold>Lower panel</bold>
: The expression of ACE2 is increased in highly prevalent cardiovascular diseases, theoretically augmenting the possibility of infection. After binding with spike receptors of COVID-19, ACE2 looses efficacy and ACE2 counter effect against ACE is attenuated or lost in spite of greater ACE2 expression.</p>
</caption>
<graphic xlink:href="gr1_lrg"></graphic>
</fig>
</p>
</body>
<back><ref-list id="cebib0010"><title>References</title>
<ref id="bib1"><label>1</label>
<element-citation publication-type="journal" id="sref1"><person-group person-group-type="author"><collab>The Novel Coronavirus Pneumonia Emergency Response Epidemiology Team</collab>
</person-group>
<article-title>The Epidemiological Characteristics of an Outbreak of 2019 Novel Coronavirus Diseases (COVID-19) — China, 2020[J]</article-title>
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</ref>
<ref id="bib2"><label>2</label>
<element-citation publication-type="journal" id="sref2"><person-group person-group-type="author"><name><surname>Zisman</surname>
<given-names>L.S.</given-names>
</name>
</person-group>
<article-title>ACE and ACE2: a tale of two enzymes</article-title>
<source>Eur Heart J</source>
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<ref id="bib3"><label>3</label>
<element-citation publication-type="journal" id="sref3"><person-group person-group-type="author"><name><surname>Imai</surname>
<given-names>Y.</given-names>
</name>
<name><surname>Kuba</surname>
<given-names>K.</given-names>
</name>
<name><surname>Rao</surname>
<given-names>S.</given-names>
</name>
</person-group>
<article-title>Angiotensin-converting enzyme 2 protects from severe acute lung failure</article-title>
<source>Nature</source>
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<ref id="bib4"><label>4</label>
<mixed-citation publication-type="other" id="sref4">De Simone G. ESC Council on Hypertension On behalf of the Nucleus Members. Position Statement of the ESC Council on Hypertension on ACE-Inhibitors and Angiotensin Receptor Blockers. March, 13, 2020</mixed-citation>
</ref>
</ref-list>
<fn-group><fn id="d32e204"><p id="ntpara0010">(TB is a former associate researcher of CNR; EP is research director of CNR).</p>
</fn>
</fn-group>
</back>
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