ACE2: from vasopeptidase to SARS virus receptor.
Identifieur interne : 005482 ( Main/Exploration ); précédent : 005481; suivant : 005483ACE2: from vasopeptidase to SARS virus receptor.
Auteurs : Anthony J. Turner [Royaume-Uni] ; Julian A. Hiscox ; Nigel M. HooperSource :
- Trends in pharmacological sciences [ 0165-6147 ] ; 2004.
Descripteurs français
- KwdFr :
- Animaux, Hormones peptidiques (métabolisme), Hormones peptidiques (physiologie), Humains, Isoenzymes (génétique), Isoenzymes (physiologie), Peptide hydrolases (physiologie), Peptidyl-Dipeptidase A (génétique), Peptidyl-Dipeptidase A (physiologie), Récepteurs viraux (génétique), Vaisseaux sanguins (métabolisme), Vaisseaux sanguins (physiologie), Virus du SRAS (génétique).
- MESH :
- génétique : Isoenzymes, Peptidyl-Dipeptidase A, Récepteurs viraux, Virus du SRAS.
- métabolisme : Hormones peptidiques, Vaisseaux sanguins.
- physiologie : Hormones peptidiques, Isoenzymes, Peptide hydrolases, Peptidyl-Dipeptidase A, Vaisseaux sanguins.
- Animaux, Humains.
English descriptors
- KwdEn :
- Animals, Blood Vessels (metabolism), Blood Vessels (physiology), Humans, Isoenzymes (genetics), Isoenzymes (physiology), Peptide Hormones (metabolism), Peptide Hormones (physiology), Peptide Hydrolases (physiology), Peptidyl-Dipeptidase A (genetics), Peptidyl-Dipeptidase A (physiology), Receptors, Virus (genetics), SARS Virus (genetics).
- MESH :
- chemical , genetics : Isoenzymes, Peptidyl-Dipeptidase A, Receptors, Virus.
- genetics : SARS Virus.
- metabolism : Blood Vessels, Peptide Hormones.
- physiology : Blood Vessels, Isoenzymes, Peptide Hormones, Peptide Hydrolases, Peptidyl-Dipeptidase A.
- Animals, Humans.
Abstract
The zinc metallopeptidase angiotensin-converting enzyme 2 (ACE2) is the only known human homologue of the key regulator of blood pressure angiotensin-converting enzyme (ACE). Since its discovery in 2000, ACE2 has been implicated in heart function, hypertension and diabetes, with its effects being mediated, in part, through its ability to convert angiotensin II to angiotensin-(1-7). Unexpectedly, ACE2 also serves as the cellular entry point for the severe acute respiratory syndrome (SARS) virus and the enzyme is therefore a prime target for pharmacological intervention on several disease fronts.
DOI: 10.1016/j.tips.2004.04.001
PubMed: 15165741
Affiliations:
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Le document en format XML
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Hiscox</name></author><author><name sortKey="Hooper, Nigel M" sort="Hooper, Nigel M" uniqKey="Hooper N" first="Nigel M" last="Hooper">Nigel M. 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Turner</name><affiliation wicri:level="4"><nlm:affiliation>School of Biochemistry and Microbiology, University of Leeds, Leeds LS2 9JT, UK. a.j.turner@leeds.ac.uk</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biochemistry and Microbiology, University of Leeds, Leeds LS2 9JT</wicri:regionArea><orgName type="university">Université de Leeds</orgName><placeName><settlement type="city">Leeds</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Yorkshire-et-Humber</region></placeName></affiliation></author><author><name sortKey="Hiscox, Julian A" sort="Hiscox, Julian A" uniqKey="Hiscox J" first="Julian A" last="Hiscox">Julian A. Hiscox</name></author><author><name sortKey="Hooper, Nigel M" sort="Hooper, Nigel M" uniqKey="Hooper N" first="Nigel M" last="Hooper">Nigel M. Hooper</name></author></analytic><series><title level="j">Trends in pharmacological sciences</title><idno type="ISSN">0165-6147</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Blood Vessels (metabolism)</term><term>Blood Vessels (physiology)</term><term>Humans</term><term>Isoenzymes (genetics)</term><term>Isoenzymes (physiology)</term><term>Peptide Hormones (metabolism)</term><term>Peptide Hormones (physiology)</term><term>Peptide Hydrolases (physiology)</term><term>Peptidyl-Dipeptidase A (genetics)</term><term>Peptidyl-Dipeptidase A (physiology)</term><term>Receptors, Virus (genetics)</term><term>SARS Virus (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Hormones peptidiques (métabolisme)</term><term>Hormones peptidiques (physiologie)</term><term>Humains</term><term>Isoenzymes (génétique)</term><term>Isoenzymes (physiologie)</term><term>Peptide hydrolases (physiologie)</term><term>Peptidyl-Dipeptidase A (génétique)</term><term>Peptidyl-Dipeptidase A (physiologie)</term><term>Récepteurs viraux (génétique)</term><term>Vaisseaux sanguins (métabolisme)</term><term>Vaisseaux sanguins (physiologie)</term><term>Virus du SRAS (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Isoenzymes</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Isoenzymes</term><term>Peptidyl-Dipeptidase A</term><term>Récepteurs viraux</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Blood Vessels</term><term>Peptide Hormones</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Hormones peptidiques</term><term>Vaisseaux sanguins</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Hormones peptidiques</term><term>Isoenzymes</term><term>Peptide hydrolases</term><term>Peptidyl-Dipeptidase A</term><term>Vaisseaux sanguins</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Blood Vessels</term><term>Isoenzymes</term><term>Peptide Hormones</term><term>Peptide Hydrolases</term><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The zinc metallopeptidase angiotensin-converting enzyme 2 (ACE2) is the only known human homologue of the key regulator of blood pressure angiotensin-converting enzyme (ACE). Since its discovery in 2000, ACE2 has been implicated in heart function, hypertension and diabetes, with its effects being mediated, in part, through its ability to convert angiotensin II to angiotensin-(1-7). Unexpectedly, ACE2 also serves as the cellular entry point for the severe acute respiratory syndrome (SARS) virus and the enzyme is therefore a prime target for pharmacological intervention on several disease fronts.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Yorkshire-et-Humber</li></region><settlement><li>Leeds</li></settlement><orgName><li>Université de Leeds</li></orgName></list><tree><noCountry><name sortKey="Hiscox, Julian A" sort="Hiscox, Julian A" uniqKey="Hiscox J" first="Julian A" last="Hiscox">Julian A. Hiscox</name><name sortKey="Hooper, Nigel M" sort="Hooper, Nigel M" uniqKey="Hooper N" first="Nigel M" last="Hooper">Nigel M. Hooper</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Turner, Anthony J" sort="Turner, Anthony J" uniqKey="Turner A" first="Anthony J" last="Turner">Anthony J. Turner</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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