Angiotensin-converting enzyme 2 and new insights into the renin-angiotensin system
Autor: | Daniel W. Lambert, Nigel M. Hooper, Anthony J. Turner |
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Rok vydání: | 2007 |
Předmět: |
Lung Diseases
Metallopeptidase CoV coronavirus ACE2 Biochemistry TNF tumour necrosis factor Renin-Angiotensin System Angiotensin AT1 angiotensin receptor type 1 Receptor ADAM a disintegrin and metalloproteinase biology Liver Diseases MDCK Madin–Darby Canine Kidney Diabetes Cardiovascular Diseases Angiotensin-converting enzyme 2 Ang angiotensin Kidney Diseases Angiotensin-Converting Enzyme 2 HNF hepatocyte nuclear factor MODY maturity-onset diabetes mellitus hormones hormone substitutes and hormone antagonists medicine.medical_specialty ACE angiotensin-converting enzyme Peptidyl-Dipeptidase A Article HEK human embryonic kidney Internal medicine RAS renin–angiotensin system Renin–angiotensin system medicine Animals Humans SARS severe acute respiratory syndrome ARDS acute respiratory distress syndrome ACE Pharmacology mas receptor for Ang (1-7) SARS Angiotensin II receptor type 1 business.industry Angiotensin-converting enzyme Carboxypeptidase Angiotensin II TACE TNF-α converting enzyme Endocrinology biology.protein ARDS business |
Zdroj: | Biochemical Pharmacology |
ISSN: | 1873-2968 |
Popis: | Components of the renin-angiotensin system are well established targets for pharmacological intervention in a variety of disorders. Many such therapies abrogate the effects of the hypertensive and mitogenic peptide, angiotensin II, by antagonising its interaction with its receptor, or by inhibiting its formative enzyme, angiotensin-converting enzyme (ACE). At the turn of the millennium, a homologous enzyme, termed ACE2, was identified which increasingly shares the limelight with its better-known homologue. In common with ACE, ACE2 is a type I transmembrane metallopeptidase; however, unlike ACE, ACE2 functions as a carboxypeptidase, cleaving a single C-terminal residue from a distinct range of substrates. One such substrate is angiotensin II, which is hydrolysed by ACE2 to the vasodilatory peptide angiotensin 1-7. In this commentary we discuss the latest developments in the rapidly progressing study of the physiological and patho-physiological roles of ACE2 allied with an overview of the current understanding of its molecular and cell biology. We also discuss parallel developments in the study of collectrin, a catalytically inactive homologue of ACE2 with critical functions in the pancreas and kidney. |
Databáze: | OpenAIRE |
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