ACE2: from vasopeptidase to SARS virus receptor
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 me...
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Veröffentlicht in: | Trends in pharmacological sciences (Regular ed.) 2004-06, Vol.25 (6), p.291-294 |
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description | 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_str_mv | 10.1016/j.tips.2004.04.001 |
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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.</description><subject>Animals</subject><subject>Blood Vessels - metabolism</subject><subject>Blood Vessels - physiology</subject><subject>Humans</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - physiology</subject><subject>Peptide Hormones - metabolism</subject><subject>Peptide Hormones - physiology</subject><subject>Peptide Hydrolases - physiology</subject><subject>Peptidyl-Dipeptidase A - genetics</subject><subject>Peptidyl-Dipeptidase A - physiology</subject><subject>Receptors, Virus - genetics</subject><subject>SARS Virus - genetics</subject><issn>0165-6147</issn><issn>1873-3735</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKAzEUhoMotl5ewIXMyt20OcnMpCMilFIvUBCsrkMmOaMpbTMm04Jvb4YWLxvhQBb_d_4cPkIugA6AQjFcDFrbhAGjNBt0Q-GA9GEkeMoFzw9JP0J5WkAmeuQkhAWllHMGx6QHeUxEBn0yHE-m7DqpvVslWxVcg01rjQqYtC6Zj5_nydb6TUg86pg4f0aOarUMeL5_T8nr3fRl8pDOnu4fJ-NZqvMsb1NTClFxNNTkrGBcFCLjStSszKpaFUabkiNozHWleT0Czs0or7JMVCBKzUaKn5LbXW-zqVZoNK5br5ay8Xal_Kd0ysq_ydq-yze3lQKgpJzFgqt9gXcfGwytXNmgcblUa3SbELmyKAoQEWQ7UHsXgsf6-xOgsvMsF7LzLDvPshsKceny93k_K3uxEbjZARglbS16GbTFtUZjo8pWGmf_6_8C4qCOrg</recordid><startdate>20040601</startdate><enddate>20040601</enddate><creator>Turner, Anthony J</creator><creator>Hiscox, Julian A</creator><creator>Hooper, Nigel M</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20040601</creationdate><title>ACE2: from vasopeptidase to SARS virus receptor</title><author>Turner, Anthony J ; Hiscox, Julian A ; Hooper, Nigel M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c545t-d977b3ed0d5262376743a7f294bfa6dcd93e1ce5cbc3f8133d85b447b179c28a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Blood Vessels - metabolism</topic><topic>Blood Vessels - physiology</topic><topic>Humans</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - physiology</topic><topic>Peptide Hormones - metabolism</topic><topic>Peptide Hormones - physiology</topic><topic>Peptide Hydrolases - physiology</topic><topic>Peptidyl-Dipeptidase A - genetics</topic><topic>Peptidyl-Dipeptidase A - physiology</topic><topic>Receptors, Virus - genetics</topic><topic>SARS Virus - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Turner, Anthony J</creatorcontrib><creatorcontrib>Hiscox, Julian A</creatorcontrib><creatorcontrib>Hooper, Nigel M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Trends in pharmacological sciences (Regular ed.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Turner, Anthony J</au><au>Hiscox, Julian A</au><au>Hooper, Nigel M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ACE2: from vasopeptidase to SARS virus receptor</atitle><jtitle>Trends in pharmacological sciences (Regular ed.)</jtitle><addtitle>Trends Pharmacol Sci</addtitle><date>2004-06-01</date><risdate>2004</risdate><volume>25</volume><issue>6</issue><spage>291</spage><epage>294</epage><pages>291-294</pages><issn>0165-6147</issn><eissn>1873-3735</eissn><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). 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subjects | 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 |
title | ACE2: from vasopeptidase to SARS virus receptor |
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