Using the multiplication of COVID-19 severe acute respiratory syndrome cases due to SARS-COV2, some concerns about angiotensin-converting enzyme 1 (ACE1) inhibitors (ACEi) and angiotensin II type 1 receptor blockers (ARB) have emerged. manifestation in either animal or human studies. Finally, some studies support Rabbit Polyclonal to BL-CAM (phospho-Tyr807) the hypothesis that elevated ACE2 membrane manifestation and cells activity by administration of ARB and/or infusion of soluble ACE2 could confer protecting properties against inflammatory tissue damage in COVID-19 illness. In summary, based on the currently available evidence and as advocated by many medical societies, ACEi or ARB should not be discontinued because of issues with COVID-19 illness, except when the hemodynamic scenario is definitely precarious and case-by-case adjustment is required. strong class=”kwd-title” Keywords: COVID-19, Renin-angiotensin-aldosterone system, Arterial hypertension Rsum Avec la multiplication des cas de syndrome respiratoire aigu svre COVID-19?dus au SRAS-COV2, certaines proccupations concernant les inhibiteurs de lenzyme de conversion de langiotensine 1 (IEC) et les antagonistes des rcepteurs de type 1? langiotensine II (ARB) ont t souleves. Lenzyme membranaire ACE2 (enzyme de conversion de langiotensine 2) sert de rcepteur au SRAS-COV2, permettant ainsi child entre dans les cellules. Ainsi, la crainte quun traitement pr-existant par IEC ou ARB pourrait augmenter le risque de Reparixin ic50 dvelopper un syndrome respiratoire aigu svre en cas dinfection au COVID-19?a merg. LACE2?est une enzyme (carboxypeptidase) qui contribue linactivation de langiotensine II et, par consquent, soppose physiologiquement aux effets de langiotensine II. Les IEC ninhibent pas lACE2. Bien quil ait t dmontr in vitro que les ARB rgulent positivement lexpression membranaire/lactivit tissulaire de lACE2, les tudes chez lHomme ne sont pas concordantes. De plus, ce jour, il ny a pas de donnes pour soutenir lhypothse quun traitement par IEC ou ARB pourrait faciliter lentre cellulaire du SRAS-COV2?en augmentant lexpression membranaire et lactivit tissulaire dACE2. Enfin, certaines Reparixin ic50 tudes soutiennent lhypothse selon laquelle laugmentation de lexpression membranaire dACE2, ladministration dARB ou ladministration dACE 2?soluble circulante pourrait confrer des effets protecteurs potentiels sur la survenue de lsions tissulaires inflammatoires svres en cas dinfection par le COVID-19. Des essais thrapeutiques sont en cours. En rsum, sur la foundation des preuves actuellement disponibles et comme le prconisent de nombreuses socits savantes, les IEC ou ARB ne doivent pas tre interrompus en raison dune illness par le COVID-19?en dehors des situations o la scenario hmodynamique est prcaire avec alors un ajustement au cas par cas prconis. strong class=”kwd-title” Mots cls: COVID-19, Systme rnine-angiotensine-aldostrone, Hypertension artrielle 1.?Intro Cardiovascular patients show increased risk of severe forms of coronavirus 2019 (COVID-19) infection [1], [2]. Clinical manifestations are principally respiratory, but some patients may also show cardiovascular complications [1]. The present article reviews the current state of knowledge regarding the relation between the renin-angiotensin-aldosterone system (RAAS), particularly ACE2, and COVID-19, and between Reparixin ic50 RAAS blockers and COVID-19. 2.?ACE2 and COVID-19 In human physiology, peptides are degraded by a limited number of non-specific extracellular enzymes known as peptidases or proteases. These are membrane proteins, the active sites of which face the extracellular space. Endopeptidases cut within the peptide chain, while exopeptidases release C- or N-terminal amino acids. Angiotensin-converting enzymes are exopeptidases (carboxypeptidases), relatively specific to the amino acids surrounding the cut site, although these may be common to several peptides. It is therefore important to be aware that a given peptidase is not as such specific to a given peptide. Angiotensin-converting enzyme 2 (ACE2) is an enzyme (carboxypeptidase) mainly located in the membrane, circulating forms being created by enzyme splicing of the membrane anchor; it is homologous to the angiotensin-converting enzyme (formerly simply known as ACE however now better denoted ACE1) 1st referred to in 2000 [3], [4]. ACE2 down-regulates the renin-angiotensin program and works as a deactivator of angiotensin II (also called angiotensin-(1-8), a dynamic peptide leading to vasoconstriction, pro-fibrosis, pro-inflammation actions, stimulating aldosterone secretion by binding towards the AT1 receptor), switching it into angiotensin-(1-7), a dynamic peptide with opposing properties to angiotensin II [5]. Many animal studies demonstrated that angiotensin-(1-7), by binding towards the Mas receptor, induced vasodilatation and demonstrated anti-fibrosis and anti-inflammatory properties [6] (Fig. 1 ). Angiotensin II can be deactivated by an aminopeptidase which changes angiotensin II into angiotensin III, which induces vasodilatation and raises natriuresis and bradykinin by preferential binding to AT2 receptors with 30-fold higher affinity than for AT1 receptors [7], [8]. ACE2 also changes angiotensin 1 [also referred to as angiotensin-(1-10)] into angiotensin-(1-9), of unfamiliar action, which can be further changed into angiotensin-(1-7) by ACE1. The RAAS can therefore become split into an activator program composed of the historic and traditional angiotensin II/ACE1/AT1R/aldosterone pathway, and an inhibitor program composed of the angiotensin-(1-7)/ACE2/MasR pathway, the second option capable both to deactivate angiotensin II and counter its results. The pharmacology from the angiotensin-(1-7)/ACE2/MasR pathway, as opposed to the angiotensin II/ACE1/AT1R/aldosterone pathway,.