SARS‐coronavirus modulation of myocardial ACE2 expression and inflammation in patients with SARS
Identifieur interne : 001F23 ( Ncbi/Merge ); précédent : 001F22; suivant : 001F24SARS‐coronavirus modulation of myocardial ACE2 expression and inflammation in patients with SARS
Auteurs : G. Y. Oudit ; Z. Kassiri ; C. Jiang ; P. P. Liu ; S. M. Poutanen ; J. M. Penninger ; J. ButanySource :
- European Journal of Clinical Investigation [ 0014-2972 ] ; 2009.
Descripteurs français
- KwdFr :
- Activation virale, Animaux, Autopsie, Humains, Immunohistochimie, Maladies cardiovasculaires (), Maladies cardiovasculaires (virologie), Myocarde (anatomopathologie), Mâle, Peptidyl-Dipeptidase A (génétique), Peptidyl-Dipeptidase A (métabolisme), Régulation négative, Souris, Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- anatomopathologie : Myocarde.
- génétique : Peptidyl-Dipeptidase A, Virus du SRAS.
- métabolisme : Peptidyl-Dipeptidase A, Virus du SRAS.
- virologie : Maladies cardiovasculaires.
- Activation virale, Animaux, Autopsie, Humains, Immunohistochimie, Maladies cardiovasculaires, Mâle, Régulation négative, Souris.
English descriptors
- KwdEn :
- Animals, Autopsy, Cardiovascular Diseases (prevention & control), Cardiovascular Diseases (virology), Down-Regulation, Humans, Immunohistochemistry, Male, Mice, Myocardium (pathology), Peptidyl-Dipeptidase A (genetics), Peptidyl-Dipeptidase A (metabolism), SARS Virus (genetics), SARS Virus (metabolism), Virus Activation.
- MESH :
- chemical , genetics : Peptidyl-Dipeptidase A.
- chemical , metabolism : Peptidyl-Dipeptidase A.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- pathology : Myocardium.
- prevention & control : Cardiovascular Diseases.
- virology : Cardiovascular Diseases.
- Animals, Autopsy, Down-Regulation, Humans, Immunohistochemistry, Male, Mice, Virus Activation.
Abstract
Url:
DOI: 10.1111/j.1365-2362.2009.02153.x
PubMed: 19453650
PubMed Central: 7163766
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Links to Exploration step
PMC:7163766Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Autopsy</term>
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<term>Down-Regulation</term>
<term>Humans</term>
<term>Immunohistochemistry</term>
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<term>Mice</term>
<term>Myocardium (pathology)</term>
<term>Peptidyl-Dipeptidase A (genetics)</term>
<term>Peptidyl-Dipeptidase A (metabolism)</term>
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<term>Maladies cardiovasculaires (virologie)</term>
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<term>Virus du SRAS (métabolisme)</term>
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<front><div type="abstract" xml:lang="en"><title>Abstract</title>
<p><bold>Background </bold>
Angiotensin converting enzyme 2 (ACE2), a monocarboxylase that degrades angiotensin II to angiotensin 1–7, is also the functional receptor for severe acute respiratory syndrome (SARS) coronavirus (SARS‐CoV) and is highly expressed in the lungs and heart. Patients with SARS also suffered from cardiac disease including arrhythmias, sudden cardiac death, and systolic and diastolic dysfunction.</p>
<p><bold>Materials and methods </bold>
We studied mice infected with the human strain of the SARS‐CoV and encephalomyocarditis virus and examined ACE2 mRNA and protein expression. Autopsy heart samples from patients who succumbed to the SARS crisis in Toronto (Canada) were used to investigate the impact of SARS on myocardial structure, inflammation and ACE2 protein expression.</p>
<p><bold>Results </bold>
Pulmonary infection with the human SARS‐CoV in mice led to an ACE2‐dependent myocardial infection with a marked decrease in ACE2 expression confirming a critical role of ACE2 in mediating SARS‐CoV infection in the heart. The SARS‐CoV viral RNA was detected in 35% (7/20) of autopsied human heart samples obtained from patients who succumbed to the SARS crisis during the Toronto SARS outbreak. Macrophage‐specific staining showed a marked increase in macrophage infiltration with evidence of myocardial damage in patients who had SARS‐CoV in their hearts. The presence of SARS‐CoV in the heart was also associated with marked reductions in ACE2 protein expression.</p>
<p><bold>Conclusions </bold>
Our data show that SARS‐CoV can mediate myocardial inflammation and damage associated with down‐regulation of myocardial ACE2 system, which may be responsible for the myocardial dysfunction and adverse cardiac outcomes in patients with SARS.</p>
</div>
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<front><div type="abstract" xml:lang="en"><title>Abstract</title>
<p><bold>Background </bold>
Angiotensin converting enzyme 2 (ACE2), a monocarboxylase that degrades angiotensin II to angiotensin 1–7, is also the functional receptor for severe acute respiratory syndrome (SARS) coronavirus (SARS‐CoV) and is highly expressed in the lungs and heart. Patients with SARS also suffered from cardiac disease including arrhythmias, sudden cardiac death, and systolic and diastolic dysfunction.</p>
<p><bold>Materials and methods </bold>
We studied mice infected with the human strain of the SARS‐CoV and encephalomyocarditis virus and examined ACE2 mRNA and protein expression. Autopsy heart samples from patients who succumbed to the SARS crisis in Toronto (Canada) were used to investigate the impact of SARS on myocardial structure, inflammation and ACE2 protein expression.</p>
<p><bold>Results </bold>
Pulmonary infection with the human SARS‐CoV in mice led to an ACE2‐dependent myocardial infection with a marked decrease in ACE2 expression confirming a critical role of ACE2 in mediating SARS‐CoV infection in the heart. The SARS‐CoV viral RNA was detected in 35% (7/20) of autopsied human heart samples obtained from patients who succumbed to the SARS crisis during the Toronto SARS outbreak. Macrophage‐specific staining showed a marked increase in macrophage infiltration with evidence of myocardial damage in patients who had SARS‐CoV in their hearts. The presence of SARS‐CoV in the heart was also associated with marked reductions in ACE2 protein expression.</p>
<p><bold>Conclusions </bold>
Our data show that SARS‐CoV can mediate myocardial inflammation and damage associated with down‐regulation of myocardial ACE2 system, which may be responsible for the myocardial dysfunction and adverse cardiac outcomes in patients with SARS.</p>
</div>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">SARS-coronavirus modulation of myocardial ACE2 expression and inflammation in patients with SARS.</title>
<author><name sortKey="Oudit, G Y" sort="Oudit, G Y" uniqKey="Oudit G" first="G Y" last="Oudit">G Y Oudit</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Medicine, University of Alberta, Edmonton, Alberta, Canada. gavin.oudit@ualberta.ca</nlm:affiliation>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>Department of Medicine, University of Alberta, Edmonton, Alberta</wicri:regionArea>
<wicri:noRegion>Alberta</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kassiri, Z" sort="Kassiri, Z" uniqKey="Kassiri Z" first="Z" last="Kassiri">Z. Kassiri</name>
</author>
<author><name sortKey="Jiang, C" sort="Jiang, C" uniqKey="Jiang C" first="C" last="Jiang">C. Jiang</name>
</author>
<author><name sortKey="Liu, P P" sort="Liu, P P" uniqKey="Liu P" first="P P" last="Liu">P P Liu</name>
</author>
<author><name sortKey="Poutanen, S M" sort="Poutanen, S M" uniqKey="Poutanen S" first="S M" last="Poutanen">S M Poutanen</name>
</author>
<author><name sortKey="Penninger, J M" sort="Penninger, J M" uniqKey="Penninger J" first="J M" last="Penninger">J M Penninger</name>
</author>
<author><name sortKey="Butany, J" sort="Butany, J" uniqKey="Butany J" first="J" last="Butany">J. Butany</name>
</author>
</analytic>
<series><title level="j">European journal of clinical investigation</title>
<idno type="eISSN">1365-2362</idno>
<imprint><date when="2009" type="published">2009</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Autopsy</term>
<term>Cardiovascular Diseases (prevention & control)</term>
<term>Cardiovascular Diseases (virology)</term>
<term>Down-Regulation</term>
<term>Humans</term>
<term>Immunohistochemistry</term>
<term>Male</term>
<term>Mice</term>
<term>Myocardium (pathology)</term>
<term>Peptidyl-Dipeptidase A (genetics)</term>
<term>Peptidyl-Dipeptidase A (metabolism)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
<term>Virus Activation</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation virale</term>
<term>Animaux</term>
<term>Autopsie</term>
<term>Humains</term>
<term>Immunohistochimie</term>
<term>Maladies cardiovasculaires ()</term>
<term>Maladies cardiovasculaires (virologie)</term>
<term>Myocarde (anatomopathologie)</term>
<term>Mâle</term>
<term>Peptidyl-Dipeptidase A (génétique)</term>
<term>Peptidyl-Dipeptidase A (métabolisme)</term>
<term>Régulation négative</term>
<term>Souris</term>
<term>Virus du SRAS (génétique)</term>
<term>Virus du SRAS (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peptidyl-Dipeptidase A</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptidyl-Dipeptidase A</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Myocarde</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peptidyl-Dipeptidase A</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peptidyl-Dipeptidase A</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Myocardium</term>
</keywords>
<keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Cardiovascular Diseases</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Maladies cardiovasculaires</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Cardiovascular Diseases</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Autopsy</term>
<term>Down-Regulation</term>
<term>Humans</term>
<term>Immunohistochemistry</term>
<term>Male</term>
<term>Mice</term>
<term>Virus Activation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Activation virale</term>
<term>Animaux</term>
<term>Autopsie</term>
<term>Humains</term>
<term>Immunohistochimie</term>
<term>Maladies cardiovasculaires</term>
<term>Mâle</term>
<term>Régulation négative</term>
<term>Souris</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Angiotensin converting enzyme 2 (ACE2), a monocarboxylase that degrades angiotensin II to angiotensin 1-7, is also the functional receptor for severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) and is highly expressed in the lungs and heart. Patients with SARS also suffered from cardiac disease including arrhythmias, sudden cardiac death, and systolic and diastolic dysfunction.</div>
</front>
</TEI>
</pubmed>
</double>
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