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PMID: 15165741 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

ACE2: from vasopeptidase to SARS virus receptor.

Trends in pharmacological sciences ·Vol. 25 ·No. 6 ·2004-06-00 ·Pages 291-4

Turner AJ, Hiscox JA, Hooper NM

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.

MeSH Terms
Animals Blood Vessels/metabolism,physiology Humans Isoenzymes/genetics,physiology Peptide Hormones/metabolism,physiology Peptide Hydrolases/physiology Peptidyl-Dipeptidase A/genetics,physiology Receptors, Virus/genetics SARS Virus/genetics
Chemicals
Isoenzymes Peptide Hormones Receptors, Virus Peptide Hydrolases Peptidyl-Dipeptidase A
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Turner Anthony J
School of Biochemistry and Microbiology, University of Leeds, Leeds LS2 9JT, UK. a.j.turner@leeds.ac.uk
Hiscox Julian A
Hooper Nigel M
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Article Info
Journal
Trends in pharmacological sciences
Abbr.
Trends Pharmacol Sci
ISSN
0165-6147
DOI
10.1016/j.tips.2004.04.001
Email
a.j.turner@leeds.ac.uk
Published
2004-06-00
Pages
291-4
Language
English
Region
England
NLM ID
7906158
PMCID
PMC7119032
Subset
IM
External Links
PubMed source DOI: 10.1016/j.tips.2004.04.001 PMC Full Text View journal details
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