COVID-19, ACE2, and the cardiovascular consequences.
Identifieur interne : 000913 ( 2020/Analysis ); précédent : 000912; suivant : 000914COVID-19, ACE2, and the cardiovascular consequences.
Auteurs : Andrew M. South [États-Unis] ; Debra I. Diz [États-Unis] ; Mark C. Chappell [États-Unis]Source :
- American journal of physiology. Heart and circulatory physiology [ 1522-1539 ] ; 2020.
Descripteurs français
- KwdFr :
- Animaux, Humains, Infections à coronavirus (enzymologie), Infections à coronavirus (virologie), Infections à coronavirus (épidémiologie), Maladies cardiovasculaires (enzymologie), Maladies cardiovasculaires (virologie), Mâle, Pandémies, Peptidyl-Dipeptidase A (métabolisme), Pneumopathie virale (enzymologie), Pneumopathie virale (virologie), Pneumopathie virale (épidémiologie), Pénétration virale, Rats, Rats de lignée LEW.
- MESH :
- enzymologie : Infections à coronavirus, Maladies cardiovasculaires, Pneumopathie virale.
- métabolisme : Peptidyl-Dipeptidase A.
- virologie : Infections à coronavirus, Maladies cardiovasculaires, Pneumopathie virale.
- épidémiologie : Infections à coronavirus, Pneumopathie virale.
- Animaux, Humains, Mâle, Pandémies, Pénétration virale, Rats, Rats de lignée LEW.
English descriptors
- KwdEn :
- Animals, Betacoronavirus (metabolism), Betacoronavirus (physiology), Cardiovascular Diseases (enzymology), Cardiovascular Diseases (virology), Coronavirus Infections (enzymology), Coronavirus Infections (epidemiology), Coronavirus Infections (virology), Humans, Male, Pandemics, Peptidyl-Dipeptidase A (metabolism), Pneumonia, Viral (enzymology), Pneumonia, Viral (epidemiology), Pneumonia, Viral (virology), Rats, Rats, Inbred Lew, Virus Internalization.
- MESH :
- chemical , metabolism : Peptidyl-Dipeptidase A.
- enzymology : Cardiovascular Diseases, Coronavirus Infections, Pneumonia, Viral.
- epidemiology : Coronavirus Infections, Pneumonia, Viral.
- metabolism : Betacoronavirus.
- physiology : Betacoronavirus.
- virology : Cardiovascular Diseases, Coronavirus Infections, Pneumonia, Viral.
- Animals, Humans, Male, Pandemics, Rats, Rats, Inbred Lew, Virus Internalization.
Abstract
The novel SARS coronavirus SARS-CoV-2 pandemic may be particularly deleterious to patients with underlying cardiovascular disease (CVD). The mechanism for SARS-CoV-2 infection is the requisite binding of the virus to the membrane-bound form of angiotensin-converting enzyme 2 (ACE2) and internalization of the complex by the host cell. Recognition that ACE2 is the coreceptor for the coronavirus has prompted new therapeutic approaches to block the enzyme or reduce its expression to prevent the cellular entry and SARS-CoV-2 infection in tissues that express ACE2 including lung, heart, kidney, brain, and gut. ACE2, however, is a key enzymatic component of the renin-angiotensin-aldosterone system (RAAS); ACE2 degrades ANG II, a peptide with multiple actions that promote CVD, and generates Ang-(1-7), which antagonizes the effects of ANG II. Moreover, experimental evidence suggests that RAAS blockade by ACE inhibitors, ANG II type 1 receptor antagonists, and mineralocorticoid antagonists, as well as statins, enhance ACE2 which, in part, contributes to the benefit of these regimens. In lieu of the fact that many older patients with hypertension or other CVDs are routinely treated with RAAS blockers and statins, new clinical concerns have developed regarding whether these patients are at greater risk for SARS-CoV-2 infection, whether RAAS and statin therapy should be discontinued, and the potential consequences of RAAS blockade to COVID-19-related pathologies such as acute and chronic respiratory disease. The current perspective critically examines the evidence for ACE2 regulation by RAAS blockade and statins, the cardiovascular benefits of ACE2, and whether ACE2 blockade is a viable approach to attenuate COVID-19.
DOI: 10.1152/ajpheart.00217.2020
PubMed: 32228252
Affiliations:
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pubmed:32228252Le document en format XML
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Diz</name><affiliation wicri:level="2"><nlm:affiliation>Cardiovascular Sciences Center, Wake Forest School of Medicine, Winston-Salem, North Carolina.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Caroline du Nord</region></placeName><wicri:cityArea>Cardiovascular Sciences Center, Wake Forest School of Medicine, Winston-Salem</wicri:cityArea></affiliation></author><author><name sortKey="Chappell, Mark C" sort="Chappell, Mark C" uniqKey="Chappell M" first="Mark C" last="Chappell">Mark C. 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The mechanism for SARS-CoV-2 infection is the requisite binding of the virus to the membrane-bound form of angiotensin-converting enzyme 2 (ACE2) and internalization of the complex by the host cell. Recognition that ACE2 is the coreceptor for the coronavirus has prompted new therapeutic approaches to block the enzyme or reduce its expression to prevent the cellular entry and SARS-CoV-2 infection in tissues that express ACE2 including lung, heart, kidney, brain, and gut. ACE2, however, is a key enzymatic component of the renin-angiotensin-aldosterone system (RAAS); ACE2 degrades ANG II, a peptide with multiple actions that promote CVD, and generates Ang-(1-7), which antagonizes the effects of ANG II. Moreover, experimental evidence suggests that RAAS blockade by ACE inhibitors, ANG II type 1 receptor antagonists, and mineralocorticoid antagonists, as well as statins, enhance ACE2 which, in part, contributes to the benefit of these regimens. In lieu of the fact that many older patients with hypertension or other CVDs are routinely treated with RAAS blockers and statins, new clinical concerns have developed regarding whether these patients are at greater risk for SARS-CoV-2 infection, whether RAAS and statin therapy should be discontinued, and the potential consequences of RAAS blockade to COVID-19-related pathologies such as acute and chronic respiratory disease. The current perspective critically examines the evidence for ACE2 regulation by RAAS blockade and statins, the cardiovascular benefits of ACE2, and whether ACE2 blockade is a viable approach to attenuate COVID-19.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Nord</li></region></list><tree><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="South, Andrew M" sort="South, Andrew M" uniqKey="South A" first="Andrew M" last="South">Andrew M. South</name></region><name sortKey="Chappell, Mark C" sort="Chappell, Mark C" uniqKey="Chappell M" first="Mark C" last="Chappell">Mark C. Chappell</name><name sortKey="Diz, Debra I" sort="Diz, Debra I" uniqKey="Diz D" first="Debra I" last="Diz">Debra I. Diz</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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