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 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.
Turner
Anthony J
AJ
School of Biochemistry and Microbiology, University of Leeds, Leeds LS2 9JT, UK. a.j.turner@leeds.ac.uk
Hiscox
Julian A
JA
Hooper
Nigel M
NM
D000818:Animals; D001808:Blood Vessels / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D007527:Isoenzymes / Q000235:genetics* / Q000502:physiology*; D036361:Peptide Hormones / Q000378:metabolism / Q000502:physiology*; D010447:Peptide Hydrolases / Q000502:physiology*; D007703:Peptidyl-Dipeptidase A / Q000235:genetics / Q000502:physiology*; D011991:Receptors, Virus / Q000235:genetics*; D045473:Severe acute respiratory syndrome-related coronavirus / Q000235:genetics*
D007527:Isoenzymes; D036361:Peptide Hormones; D011991:Receptors, Virus; D010447:Peptide Hydrolases; D007703:Peptidyl-Dipeptidase A