Membrane-associated zinc peptidase families: comparing ACE and ACE2
| Autor: | Jodie L. Guy, Daniel W. Lambert, F. J. Warner, A J Turner, Nigel M. Hooper |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
CP-A
carboxypeptidase-A CoV coronavirus QTL quantitative trait locus Angiotensin-Converting Enzyme Inhibitors Carboxypeptidases 030204 cardiovascular system & hematology Biochemistry Substrate Specificity Analytical Chemistry Renin-Angiotensin System Angiotensin 0302 clinical medicine Drosophila Proteins Receptor Integral membrane protein 0303 health sciences Kidney Membrane Glycoproteins biology Metallopeptidase Metalloendopeptidases SNP single nucleotide polymorphism Cell biology medicine.anatomical_structure Severe acute respiratory syndrome-related coronavirus Receptors Virus NEP neutral endopeptidase/neprilysin Angiotensin-Converting Enzyme 2 hormones hormone substitutes and hormone antagonists ACE angiotensin-converting enzyme Biophysics Peptidyl-Dipeptidase A Article 03 medical and health sciences RAS renin–angiotensin system Renin–angiotensin system Extracellular medicine Animals Humans SARS severe acute respiratory syndrome Amino Acid Sequence Binding site Molecular Biology 030304 developmental biology SARS Binding Sites Structure Angiotensin-converting enzyme Angiotensin II Coronavirus SHR spontaneous hypertensive rat biology.protein |
| Zdroj: | Biochimica et Biophysica Acta. Proteins and Proteomics |
| ISSN: | 1570-9639 |
| DOI: | 10.1016/j.bbapap.2004.10.010 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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