Primary structure, recombinant expression and homology modelling of human brain prolyl oligopeptidase, an important therapeutic target in the treatment of neuropsychiatric diseases
2005; Wiley; Volume: 11; Issue: 5 Linguagem: Inglês
10.1002/psc.676
ISSN1099-1387
AutoresTeresa Tarragó, Eduard Sabidó, Marcelo J. Kogan, Eliandre de Oliveira, Ernest Giralt,
Tópico(s)Chemical Synthesis and Analysis
ResumoJournal of Peptide ScienceVolume 11, Issue 5 p. 283-287 Research Article Primary structure, recombinant expression and homology modelling of human brain prolyl oligopeptidase, an important therapeutic target in the treatment of neuropsychiatric diseases† Teresa Tarragó, Teresa Tarragó Institut de Recerca Biomèdica de Barcelona, Parc Científic de Barcelona, E-08028 Barcelona, SpainSearch for more papers by this authorEduard Sabidó, Eduard Sabidó Institut de Recerca Biomèdica de Barcelona, Parc Científic de Barcelona, E-08028 Barcelona, SpainSearch for more papers by this authorMarcelo Javier Kogan, Marcelo Javier Kogan Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, ChileSearch for more papers by this authorEliandre de Oliveira, Eliandre de Oliveira Plataforma de Proteòmica, Parc Científic de Barcelona, Serveis Científico-Tècnics, Universitat de Barcelona, E-08028 Barcelona, SpainSearch for more papers by this authorProfessor Ernest Giralt, Corresponding Author Professor Ernest Giralt [email protected] Institut de Recerca Biomèdica de Barcelona, Parc Científic de Barcelona, E-08028 Barcelona, Spain Departament de Química Orgànica Universitat de Barcelona, E-08028 Barcelona, SpainInstitut de Recerca Biomèdica de Barcelona, Parc Científic de Barcelona, Josep Samitier 1-5, E-08028 Barcelona, SpainSearch for more papers by this author Teresa Tarragó, Teresa Tarragó Institut de Recerca Biomèdica de Barcelona, Parc Científic de Barcelona, E-08028 Barcelona, SpainSearch for more papers by this authorEduard Sabidó, Eduard Sabidó Institut de Recerca Biomèdica de Barcelona, Parc Científic de Barcelona, E-08028 Barcelona, SpainSearch for more papers by this authorMarcelo Javier Kogan, Marcelo Javier Kogan Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, ChileSearch for more papers by this authorEliandre de Oliveira, Eliandre de Oliveira Plataforma de Proteòmica, Parc Científic de Barcelona, Serveis Científico-Tècnics, Universitat de Barcelona, E-08028 Barcelona, SpainSearch for more papers by this authorProfessor Ernest Giralt, Corresponding Author Professor Ernest Giralt [email protected] Institut de Recerca Biomèdica de Barcelona, Parc Científic de Barcelona, E-08028 Barcelona, Spain Departament de Química Orgànica Universitat de Barcelona, E-08028 Barcelona, SpainInstitut de Recerca Biomèdica de Barcelona, Parc Científic de Barcelona, Josep Samitier 1-5, E-08028 Barcelona, SpainSearch for more papers by this author First published: 19 April 2005 https://doi.org/10.1002/psc.676Citations: 14 † Selected paper part of a special issue dedicated to the memory of Murray Goodman. AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat REFERENCES 1Palumbo M, Rodin RL, Goodman M. Synthesis and conformational studies in solution of sequential copolypeptides. Poly(L-prolyl-L-α-phenylglycyl-L-proline). Biochemistry 1975; 14: 485–491. 2Goodman M, Niu GCC, Su K. Conformational aspects of polypeptide structure. XXXI. Helical poly[(S)-thiazolidine-4-carboxylic acid] and poly[(S)-oxazolidine-4-carboxylic acid]. Theoretical results. J. Am. Chem. Soc. 1970; 92: 5219–5220. 3Goodman M, Bhumralkar M, Jefferson EA, Kwak J, Locardi E. Collagen mimetics. Biopolymers (Pept. Sci.) 1998; 47: 127–142. 4Kinberger GA, Cai W, Goodman M. Collagen mimetic dendrimers. J. Am. Chem. Soc. 2002; 124: 15 162–15 163. 5Crespo L, Sanclimens G, Montaner B, Perez-Tomas R, Royo M, Pons M, Albericio F, Giralt E. Peptide dendrimers based on polyproline helices. J. Am. Chem. Soc. 2002; 124: 8876–8883. 6Farrera-Sinfreu J, Zaccaro L, Vidal D, Salvatella X, Giralt E, Pons M, Albericio F, Royo M. A new class of foldamers based on cis–amino-L-proline. J. Am. Chem. Soc. 2004; 126: 6048–6057. 7Polgar L. The prolyl oligopeptidase family. Cell. Mol. Life Sci. 2002; 59: 349–362. 8Polgar L. Structure-function of prolyl oligopeptidase and its role in neurological disorders. Curr. Med. Chem.-Central Nervous System Agents 2002; 2: 251–257. 9Maes M, Goossens F, Scharpe S, Calabrese J, Desnyder R, Meltzer HY. Alterations in plasma prolyl endopeptidase activity in depression, mania, and schizophrenia: effects of antidepressants, mood stabilizers, and antipsychotic drugs. Psychiatry Res. 1995; 58: 217–225. 10Maes M, Goossens F, Lin A, De Meester I, Van Gastel A, Scharpe S. Effects of psychological stress on serum prolyl endopeptidase and dipeptidyl peptidase IV activity in humans: higher serum prolyl endopeptidase activity is related to stress-induced anxiety. Psychoneuroendocrinology 1998; 23: 485–495. 11Maes M, Lin AH, Bonaccorso S, Goossens F, Van Gastel A, Pioli R, Delmeire L, Scharpe S. Higher serum prolyl endopeptidase activity in patients with post-traumatic stress disorder. J Affect Disord. 1999; 53: 27–34. 12Fulop V, Bocskei Z, Polgar L. Prolyl oligopeptidase: an unusual β-propeller domain regulates proteolysis. Cell 1998; 94: 161–170. 13Vanhoof G, Goossens F, Hendriks L, De Meester I, Hendriks D, Vriend G, Van Broeckhoven C, Scharpe S. Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase. Gene 1994; 149: 363–366. 14Shirasawa Y, Osawa T, Hirashima A. Molecular cloning and characterization of prolyl endopeptidase from human T cells. J. Biochem. (Tokyo) 1994; 115: 724–729. 15Wong AH, Van Tol HH. Schizophrenia: from phenomenology to neurobiology. Neurosci. Biobehav. Rev. 2003; 27: 269–306. 16Bellemere G, Morain P, Vaudry H, Jegou S. Effect of S 17 092, a novel prolyl endopeptidase inhibitor, on substance P and α-melanocyte-stimulating hormone breakdown in the rat brain. J. Neurochem. 2003; 84: 919–929. 17Song KS, Raskin I. A prolyl endopeptidase-inhibiting benzofuran dimer from Polyozellus multiflex. J. Nat. Prod. 2002; 65: 76–78. 18Kobayashi W, Miyase T, Sano M, Umehara K, Warashina T, Noguchi H. Prolyl endopeptidase inhibitors from the roots of Lindera strychnifolia F. Vill. Biol. Pharm. Bull. 2002; 25: 1049–1052. 19Szeltner Z, Renner V, Polgar L. Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family. Protein Sci. 2000; 9: 353–360. 20Venalainen JI, Juvonen RO, Forsberg MM, Garcia-Horsman A, Poso A, Wallen EA, Gynther J, Mannisto PT. Substrate-dependent, non-hyperbolic kinetics of pig brain prolyl oligopeptidase and its tight binding inhibition by JTP-4819. Biochem. Pharmacol. 2002; 64: 463–471. 21Szeltner Z, Rea D, Renner V, Juliano L, Fulop V, Polgar L. Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding. J. Biol. Chem. 2003; 278: 48 786–48 793. 22Wallen EA, Christiaans JA, Jarho EM, Forsberg MM, Venalainen JI, Mannisto PT, Gynther J. New prolyl oligopeptidase inhibitors developed from dicarboxylic acid bis(l-prolyl-pyrrolidine) amides. J. Med. Chem. 2003; 46: 4543–4551. 23Vendeville S, Goossens F, Debreu-Fontaine MA, Landry V, Davioud-Charvet E, Grellier P, Scharpe S, Sergheraert C. Comparison of the inhibition of human and Trypanosoma cruzi prolyl endopeptidases. Bioorg. Med. Chem. 2002; 10: 1719–1729. 24Miura N, Shibata S, Watanabe S. Increase in the septal vasopressin content by prolyl endopeptidase inhibitors in rats. Neurosci. Lett. 1995; 196: 128–130. 25Barelli H, Petit A, Hirsch E, Wilk S, De Nanteuil G, Morain P, Checler F. S 17092-1, a highly potent, specific and cell permeant inhibitor of human proline endopeptidase. Biochem. Biophys. Res. Commun. 1999; 257: 657–661. 26Saito M, Hashimoto M, Kawaguchi N, Fukami H, Tanaka T, Higuchi N. Synthesis and inhibitory activity of acyl-peptidyl-prolinal derivatives toward post-proline cleaving enzyme as nootropic agents. J. Enzyme Inhib. 1990; 3: 163–178. 27Augustynsa K, Borlooa M, Belyaeva A, Rajana P, Goossens F, Hendriks D, Scharpé S, Haemers A. Synthesis of peptidyl acetals as inhibitors of prolyl endopeptidase. Bioorg. Med. Chem. Lett. 1995; 5: 1265–1270. 28DeWeese-Scott C, Moult J. Molecular modeling of protein function regions. Proteins 2004; 55: 942–961. Citing Literature Volume11, Issue5Special Issue: Special Issue dedicated to the memory of Murray GoodmanMay 2005Pages 283-287 ReferencesRelatedInformation
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