Aminopeptidase‐N/CD13 (EC 3.4.11.2) inhibitors: Chemistry, biological evaluations, and therapeutic prospects
Identifieur interne : 000899 ( Istex/Corpus ); précédent : 000898; suivant : 000900Aminopeptidase‐N/CD13 (EC 3.4.11.2) inhibitors: Chemistry, biological evaluations, and therapeutic prospects
Auteurs : Brigitte Bauvois ; Daniel DauzonneSource :
- Medicinal Research Reviews [ 0198-6325 ] ; 2006-01.
English descriptors
- Teeft :
- Acid, Acid derivatives, Acta, Actinonin, Active site, Alanine aminopeptidase, Alanyl aminopeptidase, Amastatin, Amino acids, Aminopeptidase, Aminopeptidase inhibitor bestatin, Aminopeptidase inhibitors, Aminopeptidases, Analog, Analogue, Angew chem, Angiogenesis, Angiotensin, Ansorge, Antibiot, Antibiotic, Antibiotic actinonin, Anticancer, Aoyagi, Apoptosis, Arch biochem biophys, Arndt, Asymmetric synthesis, Bacillus laterosporus, Bauvois, Benzyl ester, Bestatin, Betulinic, Betulinic acid, Biochem, Biochem biophys, Biochem pharmacol, Biol, Biol chem, Biol pharm bull, Biomed pharmacother, Bioorg, Biophys, Brain angiotensin, Cancer lett, Carcinoma, Cell lines, Cell motility, Chem, Chem lett, Chem pharm bull, Chemical synthesis, Chemotactic, Chiral, Chronic pain, Clin, Clin cancer, Clinical trials, Commun, Competitive inhibitor, Contract grant sponsor, Coric, Curcumin, Cyclic imide skeleton, Dauzonne, Dauzonne figure, Derivative, Dual inhibitors, Enantioselective synthesis, Endopeptidase, Endothelial, Endothelial cells, Enhancement, Enkephalin, Enzymatic activity, Enzyme, Enzyme inhib, Enzyme inhibition values, Febs lett, Hashimoto, Human aminopeptidase, Immunol, Inhibition, Inhibitor, Inhibitors figure, Inhibitory effect, Institut curie, Ishizuka, Jung, Kato, Langner, Lendeckel, Lett, Leucine, Leucine aminopeptidase, Leuhistin, Leukemia, Lymphocyte, Lymphoma, Matrix, Melanoma, Mizutani, Molecular mechanisms, Multiple sclerosis, Myeloid, Neutrophil, Ollis, Pathway, Peptidase, Peptidase inhibitors, Peptide, Perkin, Pharm, Pharmacol, Potent inhibitor, Probestin, Proc natl acad, Protease, Psammaplin, Receptor, Recherche, Recherche medicale, Reinhold, Riemann, Roques, Selective inhibitors, Shapiro, Stereoselective, Stereoselective synthesis, Streptomyces, Streptomyces azureus, Streptomyces neyagawaensis, Structural analogues, Structure determination, Suda, Synthetic inhibitors, Takahashi, Takeuchi, Takita, Tetrahedron, Tetrahedron asymmetry, Tetrahedron lett, Ubenimex, Umezawa, Vasopressin, Vasopressin release, Wang.
Abstract
Aminopeptidase N (APN)/CD13 (EC 3.4.11.2) is a transmembrane protease present in a wide variety of human tissues and cell types (endothelial, epithelial, fibroblast, leukocyte). APN/CD13 expression is dysregulated in inflammatory diseases and in cancers (solid and hematologic tumors). APN/CD13 serves as a receptor for coronaviruses. Natural and synthetic inhibitors of APN activity have been characterized. These inhibitors have revealed that APN is able to modulate bioactive peptide responses (pain management, vasopressin release) and to influence immune functions and major biological events (cell proliferation, secretion, invasion, angiogenesis). Therefore, inhibition of APN/CD13 may lead to the development of anti‐cancer and anti‐inflammatory drugs. This review provides an update on the biological and pharmacological profiles of known natural and synthetic APN inhibitors. Current status on their potential use as therapeutic agents is discussed with regard to toxicity and specificity. © 2005 Wiley Periodicals, Inc. Med Res Rev
Url:
DOI: 10.1002/med.20044
Links to Exploration step
ISTEX:FD4C65CFDBEB66581B3B02FCFA3C0E7C1CB3B4A8Le document en format XML
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B" first="Brigitte" last="Bauvois">Brigitte Bauvois</name><affiliation><mods:affiliation>Unité INSERM 507, Hôpital Necker, Université René Descartes Paris V, Bâtiment Lavoisier, 161 rue de Sèvres, 75015 Paris, France</mods:affiliation></affiliation></author><author><name sortKey="Dauzonne, Daniel" sort="Dauzonne, Daniel" uniqKey="Dauzonne D" first="Daniel" last="Dauzonne">Daniel Dauzonne</name><affiliation><mods:affiliation>UMR 176 Institut Curie‐CNRS, Institut Curie, Section Recherche, 26 rue d'Ulm, 75248 Paris CEDEX 05, France</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: daniel.dauzonne@curie.fr</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: UMR 176 Institut Curie‐CNRS, Institut Curie, Section Recherche, 26 rue d'Ulm, 75248 Paris CEDEX 05, France.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Medicinal Research Reviews</title><title level="j" type="alt">MEDICINAL RESEARCH REVIEWS</title><idno type="ISSN">0198-6325</idno><idno type="eISSN">1098-1128</idno><imprint><biblScope unit="vol">26</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="88">88</biblScope><biblScope unit="page" to="130">130</biblScope><biblScope unit="page-count">43</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2006-01">2006-01</date></imprint><idno type="ISSN">0198-6325</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0198-6325</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acid</term><term>Acid derivatives</term><term>Acta</term><term>Actinonin</term><term>Active site</term><term>Alanine aminopeptidase</term><term>Alanyl aminopeptidase</term><term>Amastatin</term><term>Amino acids</term><term>Aminopeptidase</term><term>Aminopeptidase inhibitor bestatin</term><term>Aminopeptidase inhibitors</term><term>Aminopeptidases</term><term>Analog</term><term>Analogue</term><term>Angew chem</term><term>Angiogenesis</term><term>Angiotensin</term><term>Ansorge</term><term>Antibiot</term><term>Antibiotic</term><term>Antibiotic actinonin</term><term>Anticancer</term><term>Aoyagi</term><term>Apoptosis</term><term>Arch biochem biophys</term><term>Arndt</term><term>Asymmetric synthesis</term><term>Bacillus laterosporus</term><term>Bauvois</term><term>Benzyl ester</term><term>Bestatin</term><term>Betulinic</term><term>Betulinic acid</term><term>Biochem</term><term>Biochem biophys</term><term>Biochem pharmacol</term><term>Biol</term><term>Biol chem</term><term>Biol pharm bull</term><term>Biomed pharmacother</term><term>Bioorg</term><term>Biophys</term><term>Brain angiotensin</term><term>Cancer lett</term><term>Carcinoma</term><term>Cell lines</term><term>Cell motility</term><term>Chem</term><term>Chem lett</term><term>Chem pharm bull</term><term>Chemical synthesis</term><term>Chemotactic</term><term>Chiral</term><term>Chronic pain</term><term>Clin</term><term>Clin cancer</term><term>Clinical trials</term><term>Commun</term><term>Competitive inhibitor</term><term>Contract grant sponsor</term><term>Coric</term><term>Curcumin</term><term>Cyclic imide skeleton</term><term>Dauzonne</term><term>Dauzonne figure</term><term>Derivative</term><term>Dual inhibitors</term><term>Enantioselective synthesis</term><term>Endopeptidase</term><term>Endothelial</term><term>Endothelial cells</term><term>Enhancement</term><term>Enkephalin</term><term>Enzymatic activity</term><term>Enzyme</term><term>Enzyme inhib</term><term>Enzyme inhibition values</term><term>Febs lett</term><term>Hashimoto</term><term>Human aminopeptidase</term><term>Immunol</term><term>Inhibition</term><term>Inhibitor</term><term>Inhibitors figure</term><term>Inhibitory effect</term><term>Institut curie</term><term>Ishizuka</term><term>Jung</term><term>Kato</term><term>Langner</term><term>Lendeckel</term><term>Lett</term><term>Leucine</term><term>Leucine aminopeptidase</term><term>Leuhistin</term><term>Leukemia</term><term>Lymphocyte</term><term>Lymphoma</term><term>Matrix</term><term>Melanoma</term><term>Mizutani</term><term>Molecular mechanisms</term><term>Multiple sclerosis</term><term>Myeloid</term><term>Neutrophil</term><term>Ollis</term><term>Pathway</term><term>Peptidase</term><term>Peptidase inhibitors</term><term>Peptide</term><term>Perkin</term><term>Pharm</term><term>Pharmacol</term><term>Potent inhibitor</term><term>Probestin</term><term>Proc natl acad</term><term>Protease</term><term>Psammaplin</term><term>Receptor</term><term>Recherche</term><term>Recherche medicale</term><term>Reinhold</term><term>Riemann</term><term>Roques</term><term>Selective inhibitors</term><term>Shapiro</term><term>Stereoselective</term><term>Stereoselective synthesis</term><term>Streptomyces</term><term>Streptomyces azureus</term><term>Streptomyces neyagawaensis</term><term>Structural analogues</term><term>Structure determination</term><term>Suda</term><term>Synthetic inhibitors</term><term>Takahashi</term><term>Takeuchi</term><term>Takita</term><term>Tetrahedron</term><term>Tetrahedron asymmetry</term><term>Tetrahedron lett</term><term>Ubenimex</term><term>Umezawa</term><term>Vasopressin</term><term>Vasopressin release</term><term>Wang</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Aminopeptidase N (APN)/CD13 (EC 3.4.11.2) is a transmembrane protease present in a wide variety of human tissues and cell types (endothelial, epithelial, fibroblast, leukocyte). APN/CD13 expression is dysregulated in inflammatory diseases and in cancers (solid and hematologic tumors). APN/CD13 serves as a receptor for coronaviruses. Natural and synthetic inhibitors of APN activity have been characterized. These inhibitors have revealed that APN is able to modulate bioactive peptide responses (pain management, vasopressin release) and to influence immune functions and major biological events (cell proliferation, secretion, invasion, angiogenesis). Therefore, inhibition of APN/CD13 may lead to the development of anti‐cancer and anti‐inflammatory drugs. This review provides an update on the biological and pharmacological profiles of known natural and synthetic APN inhibitors. Current status on their potential use as therapeutic agents is discussed with regard to toxicity and specificity. © 2005 Wiley Periodicals, Inc. 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Bauvois</name><affiliations><json:string>Unité INSERM 507, Hôpital Necker, Université René Descartes Paris V, Bâtiment Lavoisier, 161 rue de Sèvres, 75015 Paris, France</json:string></affiliations></json:item><json:item><name>Daniel Dauzonne</name><affiliations><json:string>UMR 176 Institut Curie‐CNRS, Institut Curie, Section Recherche, 26 rue d'Ulm, 75248 Paris CEDEX 05, France</json:string><json:string>E-mail: daniel.dauzonne@curie.fr</json:string><json:string>Correspondence address: UMR 176 Institut Curie‐CNRS, Institut Curie, Section Recherche, 26 rue d'Ulm, 75248 Paris CEDEX 05, France.</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>aminopeptidase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>ectoenzyme</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>natural inhibitor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>synthetic inhibitor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>bestatin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>cancer</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>inflammation</value></json:item></subject><articleId><json:string>MED20044</json:string></articleId><arkIstex>ark:/67375/WNG-JMJBPVQS-K</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>reviewArticle</json:string></originalGenre><abstract>Aminopeptidase N (APN)/CD13 (EC 3.4.11.2) is a transmembrane protease present in a wide variety of human tissues and cell types (endothelial, epithelial, fibroblast, leukocyte). APN/CD13 expression is dysregulated in inflammatory diseases and in cancers (solid and hematologic tumors). APN/CD13 serves as a receptor for coronaviruses. Natural and synthetic inhibitors of APN activity have been characterized. These inhibitors have revealed that APN is able to modulate bioactive peptide responses (pain management, vasopressin release) and to influence immune functions and major biological events (cell proliferation, secretion, invasion, angiogenesis). Therefore, inhibition of APN/CD13 may lead to the development of anti‐cancer and anti‐inflammatory drugs. This review provides an update on the biological and pharmacological profiles of known natural and synthetic APN inhibitors. Current status on their potential use as therapeutic agents is discussed with regard to toxicity and specificity. © 2005 Wiley Periodicals, Inc. 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APN/CD13 expression is dysregulated in inflammatory diseases and in cancers (solid and hematologic tumors). APN/CD13 serves as a receptor for coronaviruses. Natural and synthetic inhibitors of APN activity have been characterized. These inhibitors have revealed that APN is able to modulate bioactive peptide responses (pain management, vasopressin release) and to influence immune functions and major biological events (cell proliferation, secretion, invasion, angiogenesis). Therefore, inhibition of APN/CD13 may lead to the development of anti‐cancer and anti‐inflammatory drugs. This review provides an update on the biological and pharmacological profiles of known natural and synthetic APN inhibitors. Current status on their potential use as therapeutic agents is discussed with regard to toxicity and specificity. © 2005 Wiley Periodicals, Inc. Med Res Rev</abstract><note type="funding">The Institut National de la Santé et de la Recherche Médicale (INSERM)</note><note type="funding">the Centre National de La Recherche Scientifique (CNRS)</note><note type="funding">the Institut Curie, the Association pour la Recherche sur le Cancer (ARC number 3473)</note><note type="funding">la Fondation pour la Recherche Médicale</note><note type="funding">La Ligue Nationale Contre le Cancer</note><subject lang="en"><genre>keywords</genre><topic>aminopeptidase</topic><topic>ectoenzyme</topic><topic>natural inhibitor</topic><topic>synthetic inhibitor</topic><topic>bestatin</topic><topic>cancer</topic><topic>inflammation</topic></subject><relatedItem type="host"><titleInfo><title>Medicinal Research Reviews</title></titleInfo><titleInfo type="abbreviated"><title>Med. Res. 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J Pept Sci 2001; 7(2): 63–73.</note><part><date>2001</date><detail type="volume"><caption>vol.</caption><number>7</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>63</start><end>73</end></extent></part><relatedItem type="host"><titleInfo><title>J Pept Sci</title></titleInfo><part><date>2001</date><detail type="volume"><caption>vol.</caption><number>7</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>63</start><end>73</end></extent></part></relatedItem></relatedItem><identifier type="istex">FD4C65CFDBEB66581B3B02FCFA3C0E7C1CB3B4A8</identifier><identifier type="ark">ark:/67375/WNG-JMJBPVQS-K</identifier><identifier type="DOI">10.1002/med.20044</identifier><identifier type="ArticleID">MED20044</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2005 Wiley Periodicals, Inc.</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-L0C46X92-X">wiley</recordContentSource><recordOrigin>Converted from (version ) to MODS version 3.6.</recordOrigin><recordCreationDate encoding="w3cdtf">2019-11-15</recordCreationDate></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-JMJBPVQS-K/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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