Angiotensin-converting enzyme 2 in acute respiratory distress syndrome
Identifieur interne : 003A64 ( Main/Exploration ); précédent : 003A63; suivant : 003A65Angiotensin-converting enzyme 2 in acute respiratory distress syndrome
Auteurs : Y. Imai [Autriche] ; K. Kuba [Autriche] ; J. M. Penninger [Autriche]Source :
- Cellular and Molecular Life Sciences [ 1420-682X ] ; 2007-08-01.
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Abstract
Abstract.: Angiotensin-converting enzyme (ACE) and ACE2 are highly homologous metalloproteases that provide essential catalytic functions in the renin-angiotensin system (RAS). Angiotensin II is one key effector peptide of the RAS, inducing vasoconstriction and exerting multiple biological functions. ACE cleaves angiotensin I to generate angiotensin II, whereas ACE2 reduces angiotensin II levels. Accumulating evidence has demonstrated a physiological and pathological role of ACE2 in the cardiovascular systems. Intriguingly, the SARS coronavirus, the cause of severe acute respiratory syndrome (SARS), utilizes ACE2 as an essential receptor for cell fusion and in vivo infections. Moreover, recent studies have demonstrated that ACE2 protects murine lungs from acute lung injury as well as SARS-Spike protein-mediated lung injury, suggesting a dual role of ACE2 in SARS infections and protection from ARDS.
Url:
DOI: 10.1007/s00018-007-6228-6
Affiliations:
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Imai</name><affiliation wicri:level="3"><country xml:lang="fr">Autriche</country><wicri:regionArea>IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Dr. Bohrgasse 3, 1030, Vienna</wicri:regionArea><placeName><settlement type="city">Vienne (Autriche)</settlement><region nuts="2" type="province">Vienne (Autriche)</region></placeName></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Autriche</country></affiliation></author><author><name sortKey="Kuba, K" sort="Kuba, K" uniqKey="Kuba K" first="K." last="Kuba">K. 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Life Sci.</title><idno type="ISSN">1420-682X</idno><idno type="eISSN">1420-9071</idno><imprint><publisher>Birkhäuser-Verlag; www.birkhäuser.ch</publisher><pubPlace>Basel</pubPlace><date type="published" when="2007-08-01">2007-08-01</date><biblScope unit="volume">64</biblScope><biblScope unit="issue">15</biblScope><biblScope unit="page" from="2006">2006</biblScope><biblScope unit="page" to="2012">2012</biblScope></imprint><idno type="ISSN">1420-682X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1420-682X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ACE</term><term>Renin-angiotensin system (RAS)</term><term>acute respiratory distress syndrome (ARDS)</term><term>angiotensin</term><term>angiotensin-converting enzyme 2 (ACE2)</term><term>severe acute respiratory syndrome (SARS)</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract.: Angiotensin-converting enzyme (ACE) and ACE2 are highly homologous metalloproteases that provide essential catalytic functions in the renin-angiotensin system (RAS). Angiotensin II is one key effector peptide of the RAS, inducing vasoconstriction and exerting multiple biological functions. ACE cleaves angiotensin I to generate angiotensin II, whereas ACE2 reduces angiotensin II levels. Accumulating evidence has demonstrated a physiological and pathological role of ACE2 in the cardiovascular systems. Intriguingly, the SARS coronavirus, the cause of severe acute respiratory syndrome (SARS), utilizes ACE2 as an essential receptor for cell fusion and in vivo infections. Moreover, recent studies have demonstrated that ACE2 protects murine lungs from acute lung injury as well as SARS-Spike protein-mediated lung injury, suggesting a dual role of ACE2 in SARS infections and protection from ARDS.</div></front></TEI><affiliations><list><country><li>Autriche</li></country><region><li>Vienne (Autriche)</li></region><settlement><li>Vienne (Autriche)</li></settlement></list><tree><country name="Autriche"><region name="Vienne (Autriche)"><name sortKey="Imai, Y" sort="Imai, Y" uniqKey="Imai Y" first="Y." last="Imai">Y. Imai</name></region><name sortKey="Imai, Y" sort="Imai, Y" uniqKey="Imai Y" first="Y." last="Imai">Y. Imai</name><name sortKey="Kuba, K" sort="Kuba, K" uniqKey="Kuba K" first="K." last="Kuba">K. Kuba</name><name sortKey="Penninger, J M" sort="Penninger, J M" uniqKey="Penninger J" first="J. M." last="Penninger">J. M. Penninger</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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