Proteinase dysbalance in pathology: the neprilysin (NEP) and angiotensin-converting enzyme (ACE) families.
Identifieur interne : 003D66 ( Main/Exploration ); précédent : 003D65; suivant : 003D67Proteinase dysbalance in pathology: the neprilysin (NEP) and angiotensin-converting enzyme (ACE) families.
Auteurs : A J Turner [Royaume-Uni] ; N N NalivaevaSource :
- Cellular and molecular biology (Noisy-le-Grand, France) [ 1165-158X ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Néprilysine, Peptide hydrolases, Rénine.
- métabolisme : Néprilysine, Peptide hydrolases, Peptides bêta-amyloïdes, Rénine.
- Animaux, Humains, Spécificité du substrat.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Neprilysin, Peptide Hydrolases, Renin.
- chemical , metabolism : Amyloid beta-Peptides, Neprilysin, Peptide Hydrolases, Renin.
- Animals, Humans, Substrate Specificity.
Abstract
Proteolytic enzymes constitute some 2% of the human genome and provide important therapeutic targets in many diseases. The identification of many novel proteases from genome sequencing programmes provides both qualitative and quantitative challenges to target identification and validation. Some approaches to dealing with these questions and addressing functional correlates of proteolytic activity at the level of molecular cell biology are provided in this review focusing on two spheres of interest: neurodegeneration and cardiovascular regulation. The role and regulation of the neprilysin (NEP) family of metalloproteinases is highlighted in particular in the context of proteolytic events underlying the pathology of Alzheimer's disease. The second exemplar involves the newly appreciated complexity of the renin-angiotensin system as a regulator of the cardiovascular system. The application of functional genomics approaches to the discovery of angiotensin-converting enzyme-2 (ACE2) as a counterbalance to the well known hypertensive target ACE will be highlighted and their differential cellular targeting and enzymology addressed. Finally, the serendipitous discovery of ACE2 as the SARS virus receptor illustrates the surprises always in store from nature.
PubMed: 17543197
Affiliations:
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Le document en format XML
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The identification of many novel proteases from genome sequencing programmes provides both qualitative and quantitative challenges to target identification and validation. Some approaches to dealing with these questions and addressing functional correlates of proteolytic activity at the level of molecular cell biology are provided in this review focusing on two spheres of interest: neurodegeneration and cardiovascular regulation. The role and regulation of the neprilysin (NEP) family of metalloproteinases is highlighted in particular in the context of proteolytic events underlying the pathology of Alzheimer's disease. The second exemplar involves the newly appreciated complexity of the renin-angiotensin system as a regulator of the cardiovascular system. The application of functional genomics approaches to the discovery of angiotensin-converting enzyme-2 (ACE2) as a counterbalance to the well known hypertensive target ACE will be highlighted and their differential cellular targeting and enzymology addressed. Finally, the serendipitous discovery of ACE2 as the SARS virus receptor illustrates the surprises always in store from nature.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Yorkshire-et-Humber</li></region><settlement><li>Leeds</li></settlement><orgName><li>Université de Leeds</li></orgName></list><tree><noCountry><name sortKey="Nalivaeva, N N" sort="Nalivaeva, N N" uniqKey="Nalivaeva N" first="N N" last="Nalivaeva">N N Nalivaeva</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Turner, A J" sort="Turner, A J" uniqKey="Turner A" first="A J" last="Turner">A J Turner</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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