[Lessons from SARS: a new potential therapy for acute respiratory distress syndrome (ARDS) with angiotensin converting enzyme 2 (ACE2)].
Identifieur interne : 002F64 ( Main/Exploration ); précédent : 002F63; suivant : 002F65[Lessons from SARS: a new potential therapy for acute respiratory distress syndrome (ARDS) with angiotensin converting enzyme 2 (ACE2)].
Auteurs : Yumiko Imai [Autriche] ; Keiji Kuba ; Josef M. PenningerSource :
- Masui. The Japanese journal of anesthesiology [ 0021-4892 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux, Clonage moléculaire, Humains, Peptidyl-Dipeptidase A (déficit), Peptidyl-Dipeptidase A (génétique), Peptidyl-Dipeptidase A (physiologie), Peptidyl-Dipeptidase A (usage thérapeutique), Récepteurs viraux, Souris, Souris transgéniques, Syndrome de détresse respiratoire de l'adulte (traitement médicamenteux), Syndrome de détresse respiratoire de l'adulte (étiologie), Syndrome respiratoire aigu sévère (virologie), Système rénine-angiotensine (physiologie), Virus du SRAS.
- MESH :
- déficit : Peptidyl-Dipeptidase A.
- génétique : Peptidyl-Dipeptidase A.
- physiologie : Peptidyl-Dipeptidase A, Système rénine-angiotensine.
- traitement médicamenteux : Syndrome de détresse respiratoire de l'adulte.
- usage thérapeutique : Peptidyl-Dipeptidase A.
- virologie : Syndrome respiratoire aigu sévère.
- étiologie : Syndrome de détresse respiratoire de l'adulte.
- Animaux, Clonage moléculaire, Humains, Récepteurs viraux, Souris, Souris transgéniques, Virus du SRAS.
English descriptors
- KwdEn :
- Animals, Cloning, Molecular, Humans, Mice, Mice, Transgenic, Peptidyl-Dipeptidase A (deficiency), Peptidyl-Dipeptidase A (genetics), Peptidyl-Dipeptidase A (physiology), Peptidyl-Dipeptidase A (therapeutic use), Receptors, Virus, Renin-Angiotensin System (physiology), Respiratory Distress Syndrome, Adult (drug therapy), Respiratory Distress Syndrome, Adult (etiology), SARS Virus, Severe Acute Respiratory Syndrome (virology).
- MESH :
- chemical , deficiency : Peptidyl-Dipeptidase A.
- chemical , genetics : Peptidyl-Dipeptidase A.
- chemical , physiology : Peptidyl-Dipeptidase A.
- chemical , therapeutic use : Peptidyl-Dipeptidase A.
- drug therapy : Respiratory Distress Syndrome, Adult.
- etiology : Respiratory Distress Syndrome, Adult.
- physiology : Renin-Angiotensin System.
- virology : Severe Acute Respiratory Syndrome.
- Animals, Cloning, Molecular, Humans, Mice, Mice, Transgenic, Receptors, Virus, SARS Virus.
Abstract
During several months of 2002, severe acute respiratory syndrome (SARS) caused by SARS-coronavirus (SARS-CoV) spread rapidly from China throughout the world causing more than 800 deaths due to the development of acute respiratory distress syndrome (ARDS). Interestingly, a novel homologue of angiotensin converting-enzyme (ACE), termed angiotensin converting enzyme 2 (ACE2) has been identified as a receptor for SARS-CoV. ACE and ACE2 share homology in their catalytic domain and provide different key functions in the renin-angiotensin system. ACE cleaves angiotensin I to generate angiotensin II that is a key effector peptide of the system and exerts multiple biological functions, whereas ACE2 reduces angiotensin II levels and thus is a negative regulator of the system. Importantly, our recent studies using ACE2 knockout mice have demonstrated that ACE2 protects murine lungs from ARDS. Furthermore, SARS-CoV infections and the Spike protein of the SARS-CoV reduce ACE2 expression. Notably, injection of SARS-CoV Spike into mice worsens acute lung failure in vivo that can be attenuated by blocking the renin-angiotensin pathway, suggesting the activation of pulmonary RAS influences the pathogenesis of ARDS and SARS.
PubMed: 18340998
Affiliations:
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The Japanese journal of anesthesiology</title><idno type="ISSN">0021-4892</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cloning, Molecular</term><term>Humans</term><term>Mice</term><term>Mice, Transgenic</term><term>Peptidyl-Dipeptidase A (deficiency)</term><term>Peptidyl-Dipeptidase A (genetics)</term><term>Peptidyl-Dipeptidase A (physiology)</term><term>Peptidyl-Dipeptidase A (therapeutic use)</term><term>Receptors, Virus</term><term>Renin-Angiotensin System (physiology)</term><term>Respiratory Distress Syndrome, Adult (drug therapy)</term><term>Respiratory Distress Syndrome, Adult (etiology)</term><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome (virology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Clonage moléculaire</term><term>Humains</term><term>Peptidyl-Dipeptidase A (déficit)</term><term>Peptidyl-Dipeptidase A (génétique)</term><term>Peptidyl-Dipeptidase A (physiologie)</term><term>Peptidyl-Dipeptidase A (usage thérapeutique)</term><term>Récepteurs viraux</term><term>Souris</term><term>Souris transgéniques</term><term>Syndrome de détresse respiratoire de l'adulte (traitement médicamenteux)</term><term>Syndrome de détresse respiratoire de l'adulte (étiologie)</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Système rénine-angiotensine (physiologie)</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Respiratory Distress Syndrome, Adult</term></keywords><keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" qualifier="etiology" xml:lang="en"><term>Respiratory Distress Syndrome, Adult</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Peptidyl-Dipeptidase A</term><term>Système rénine-angiotensine</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Renin-Angiotensin System</term></keywords><keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Syndrome de détresse respiratoire de l'adulte</term></keywords><keywords scheme="MESH" qualifier="usage thérapeutique" xml:lang="fr"><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="étiologie" xml:lang="fr"><term>Syndrome de détresse respiratoire de l'adulte</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cloning, Molecular</term><term>Humans</term><term>Mice</term><term>Mice, Transgenic</term><term>Receptors, Virus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Clonage moléculaire</term><term>Humains</term><term>Récepteurs viraux</term><term>Souris</term><term>Souris transgéniques</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">During several months of 2002, severe acute respiratory syndrome (SARS) caused by SARS-coronavirus (SARS-CoV) spread rapidly from China throughout the world causing more than 800 deaths due to the development of acute respiratory distress syndrome (ARDS). Interestingly, a novel homologue of angiotensin converting-enzyme (ACE), termed angiotensin converting enzyme 2 (ACE2) has been identified as a receptor for SARS-CoV. ACE and ACE2 share homology in their catalytic domain and provide different key functions in the renin-angiotensin system. ACE cleaves angiotensin I to generate angiotensin II that is a key effector peptide of the system and exerts multiple biological functions, whereas ACE2 reduces angiotensin II levels and thus is a negative regulator of the system. Importantly, our recent studies using ACE2 knockout mice have demonstrated that ACE2 protects murine lungs from ARDS. Furthermore, SARS-CoV infections and the Spike protein of the SARS-CoV reduce ACE2 expression. Notably, injection of SARS-CoV Spike into mice worsens acute lung failure in vivo that can be attenuated by blocking the renin-angiotensin pathway, suggesting the activation of pulmonary RAS influences the pathogenesis of ARDS and SARS.</div></front></TEI><affiliations><list><country><li>Autriche</li></country></list><tree><noCountry><name sortKey="Kuba, Keiji" sort="Kuba, Keiji" uniqKey="Kuba K" first="Keiji" last="Kuba">Keiji Kuba</name><name sortKey="Penninger, Josef M" sort="Penninger, Josef M" uniqKey="Penninger J" first="Josef M" last="Penninger">Josef M. Penninger</name></noCountry><country name="Autriche"><noRegion><name sortKey="Imai, Yumiko" sort="Imai, Yumiko" uniqKey="Imai Y" first="Yumiko" last="Imai">Yumiko Imai</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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