Membrane-associated zinc peptidase families: comparing ACE and ACE2.
Identifieur interne : 002611 ( PubMed/Curation ); précédent : 002610; suivant : 002612Membrane-associated zinc peptidase families: comparing ACE and ACE2.
Auteurs : J L Guy [Royaume-Uni] ; D W Lambert ; F J Warner ; N M Hooper ; A J TurnerSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2005.
Descripteurs français
- KwdFr :
- Animaux, Carboxypeptidases (métabolisme), Glycoprotéines membranaires (métabolisme), Humains, Inhibiteurs de l'enzyme de conversion de l'angiotensine (pharmacologie), Metalloendopeptidases (métabolisme), Peptidyl-Dipeptidase A (métabolisme), Protéines de Drosophila (métabolisme), Récepteurs viraux (métabolisme), Sites de fixation, Spécificité du substrat, Système rénine-angiotensine (physiologie), Séquence d'acides aminés, Virus du SRAS (métabolisme).
- MESH :
- métabolisme : Carboxypeptidases, Glycoprotéines membranaires, Metalloendopeptidases, Peptidyl-Dipeptidase A, Protéines de Drosophila, Récepteurs viraux, Virus du SRAS.
- pharmacologie : Inhibiteurs de l'enzyme de conversion de l'angiotensine.
- physiologie : Système rénine-angiotensine.
- Animaux, Humains, Sites de fixation, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Angiotensin-Converting Enzyme Inhibitors (pharmacology), Animals, Binding Sites, Carboxypeptidases (metabolism), Drosophila Proteins (metabolism), Humans, Membrane Glycoproteins (metabolism), Metalloendopeptidases (metabolism), Peptidyl-Dipeptidase A (metabolism), Receptors, Virus (metabolism), Renin-Angiotensin System (physiology), SARS Virus (metabolism), Substrate Specificity.
- MESH :
- chemical , metabolism : Carboxypeptidases, Drosophila Proteins, Membrane Glycoproteins, Metalloendopeptidases, Peptidyl-Dipeptidase A, Receptors, Virus.
- chemical , pharmacology : Angiotensin-Converting Enzyme Inhibitors.
- metabolism : SARS Virus.
- physiology : Renin-Angiotensin System.
- Amino Acid Sequence, Animals, Binding Sites, Humans, Substrate Specificity.
Abstract
In contrast to the relatively ubiquitous angiotensin-converting enzyme (ACE), expression of the mammalian ACE homologue, ACE2, was initially described in the heart, kidney and testis. ACE2 is a type I integral membrane protein with its active site domain exposed to the extracellular surface of endothelial cells and the renal tubular epithelium. Here ACE2 is poised to metabolise circulating peptides which may include angiotensin II, a potent vasoconstrictor and the product of angiotensin I cleavage by ACE. To this end, ACE2 may counterbalance the effects of ACE within the renin-angiotensin system (RAS). Indeed, ACE2 has been implicated in the regulation of heart and renal function where it is proposed to control the levels of angiotensin II relative to its hypotensive metabolite, angiotensin-(1-7). The recent solution of the structure of ACE2, and ACE, has provided new insight into the substrate and inhibitor profiles of these two key regulators of the RAS. As the complexity of this crucial pathway is unravelled, there is a growing interest in the therapeutic potential of agents that modulate the activity of ACE2.
DOI: 10.1016/j.bbapap.2004.10.010
PubMed: 16054014
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xml:lang="fr"><term>Carboxypeptidases</term><term>Glycoprotéines membranaires</term><term>Metalloendopeptidases</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de Drosophila</term><term>Récepteurs viraux</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Inhibiteurs de l'enzyme de conversion de l'angiotensine</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Système rénine-angiotensine</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Renin-Angiotensin System</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Humans</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Sites de fixation</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In contrast to the relatively ubiquitous angiotensin-converting enzyme (ACE), expression of the mammalian ACE homologue, ACE2, was initially described in the heart, kidney and testis. ACE2 is a type I integral membrane protein with its active site domain exposed to the extracellular surface of endothelial cells and the renal tubular epithelium. Here ACE2 is poised to metabolise circulating peptides which may include angiotensin II, a potent vasoconstrictor and the product of angiotensin I cleavage by ACE. To this end, ACE2 may counterbalance the effects of ACE within the renin-angiotensin system (RAS). Indeed, ACE2 has been implicated in the regulation of heart and renal function where it is proposed to control the levels of angiotensin II relative to its hypotensive metabolite, angiotensin-(1-7). The recent solution of the structure of ACE2, and ACE, has provided new insight into the substrate and inhibitor profiles of these two key regulators of the RAS. As the complexity of this crucial pathway is unravelled, there is a growing interest in the therapeutic potential of agents that modulate the activity of ACE2.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16054014</PMID><DateCompleted><Year>2005</Year><Month>09</Month><Day>27</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1751</Volume><Issue>1</Issue><PubDate><Year>2005</Year><Month>Aug</Month><Day>01</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim. Biophys. 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Indeed, ACE2 has been implicated in the regulation of heart and renal function where it is proposed to control the levels of angiotensin II relative to its hypotensive metabolite, angiotensin-(1-7). The recent solution of the structure of ACE2, and ACE, has provided new insight into the substrate and inhibitor profiles of these two key regulators of the RAS. As the complexity of this crucial pathway is unravelled, there is a growing interest in the therapeutic potential of agents that modulate the activity of ACE2.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Guy</LastName><ForeName>J L</ForeName><Initials>JL</Initials><AffiliationInfo><Affiliation>Proteolysis Research Group, School of Biochemistry and Microbiology, University of Leeds, Leeds, LS2 9JT, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lambert</LastName><ForeName>D W</ForeName><Initials>DW</Initials></Author><Author ValidYN="Y"><LastName>Warner</LastName><ForeName>F J</ForeName><Initials>FJ</Initials></Author><Author ValidYN="Y"><LastName>Hooper</LastName><ForeName>N M</ForeName><Initials>NM</Initials></Author><Author ValidYN="Y"><LastName>Turner</LastName><ForeName>A J</ForeName><Initials>AJ</Initials></Author></AuthorList><Language>eng</Language><GrantList 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