TAILIEUCHUNG - Báo cáo khoa hoc: Is rat an appropriate animal model to study the involvement of D-serine catabolism in schizophrenia? insights from characterization of D-amino acid oxidase

D-Amino acid oxidase (DAAO; EC ) has been proposed to play a main role in the degradation ofD-serine, an allosteric activator of the N-methyl-D-aspartate-type glutamate receptor in the human brain, and to be associated with the onset of schizophrenia. | IFEBS Journal Is rat an appropriate animal model to study the involvement of D-serine catabolism in schizophrenia insights from characterization of D-amino acid oxidase Luca F. Frattini1 2 Luciano Piubelli1 2 Silvia Sacchi1 2 Gianluca Molla1 2 and Loredano Pollegioni1 2 1 Dipartimento di Biotecnologie e Scienze della Vita Universita degli studi dell Insubria Varese Italy 2 Centro Interuniversitario di Ricerca in Biotecnologie Proteiche The Protein Factory Universita degli studi dell Insubria Politecnico di Milano and ICRM-CNR Milan Italy Keywords drug design D-serine flavoproteins ligand binding schizophrenia Correspondence L. Pollegioni Dipartimento di Biotecnologie e Scienze della Vita University degli studi dell Insubria via . Dunant 3 21100 Varese Italy Fax 39 332 421500 Tel 39 332 421506 E-mail Received 7 June 2011 revised 12 September 2011 accepted 14 September 2011 doi D-Amino acid oxidase DAAO EC has been proposed to play a main role in the degradation of D-serine an allosteric activator of the N-methyl-D-aspartate-type glutamate receptor in the human brain and to be associated with the onset of schizophrenia. To prevent excessive D-serine degradation novel drugs for schizophrenia treatment based on DAAO inhibition were designed and tested on rats. However the properties of rat DAAO are unknown and various in vivo trials have demonstrated the effects of DAAO inhibitors on D-serine concentration in rats. In the present study rat DAAO was efficiently expressed in Escherichia coli. The recombinant enzyme was purified as an active 40 kDa monomeric flavoenzyme showing the basic properties of the dehydrogenase-oxidase class of flavoproteins. Rat DAAO differs significantly from the human counterpart because a it possesses a different substrate specificity b it shows a lower kinetic efficiency mainly as a result of a low substrate affinity c it differs in affinity for the binding of .

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