Aminopeptidase‐N/CD13 (EC 3.4.11.2) inhibitors: Chemistry, biological evaluations, and therapeutic prospects
Identifieur interne : 000F79 ( Main/Curation ); précédent : 000F78; suivant : 000F80Aminopeptidase‐N/CD13 (EC 3.4.11.2) inhibitors: Chemistry, biological evaluations, and therapeutic prospects
Auteurs : Brigitte Bauvois [France] ; Daniel Dauzonne [France]Source :
- 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
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<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>
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<term>Aminopeptidase</term>
<term>Aminopeptidase inhibitor bestatin</term>
<term>Aminopeptidase inhibitors</term>
<term>Aminopeptidases</term>
<term>Analog</term>
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<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>
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<term>Betulinic acid</term>
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<term>Biochem biophys</term>
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<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>
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<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>
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<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>
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<term>Inhibition</term>
<term>Inhibitor</term>
<term>Inhibitors figure</term>
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<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>
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<term>Myeloid</term>
<term>Neutrophil</term>
<term>Ollis</term>
<term>Pathway</term>
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<term>Peptidase inhibitors</term>
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<term>Pharmacol</term>
<term>Potent inhibitor</term>
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<term>Protease</term>
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<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>
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<term>Streptomyces azureus</term>
<term>Streptomyces neyagawaensis</term>
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<term>Suda</term>
<term>Synthetic inhibitors</term>
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<term>Takeuchi</term>
<term>Takita</term>
<term>Tetrahedron</term>
<term>Tetrahedron asymmetry</term>
<term>Tetrahedron lett</term>
<term>Ubenimex</term>
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<term>Vasopressin</term>
<term>Vasopressin release</term>
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<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. Med Res Rev</div>
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