Immunochemical relationship of d-amino acid oxidases in various tissues and animals

doi:10.1016/0305-0491(91)90053-G

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry

Volume 99, Issue 2, 1991, Pages 345-350

https://doi.org/10.1016/0305-0491(91)90053-G Get rights and content

Abstract

1.
1. By means of an enzyme immunoassay, the contents of d-amino acid oxidase (DAO) were determined in kidney, liver, cerebellum and lung of hog, but the oxidase was not detectable in heart or cerebrum.
2.
2. The oxidases in kidney, liver and cerebellum of hog were indistinguishable as regards immunoreactivity toward anti-hog kidney DAO antibody, specific activity and molecular weight.
3.
3. The oxidases in rat and dog kidneys immunochemically cross-reacted with anti-hog DAO antibody.
4.
4. The overall structure of the hog oxidase was more similar to that of the dog enzyme than that of the rat, while the structure around the catalytic site of the hog oxidase was more similar to that of the rat oxidase than that of the dog enzyme.
5.
5. On immunoblot analysis, two forms of the oxidase were detected in extracts of hog, rat and dog kidneys.

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Selective DAAO inhibitors have demonstrated promising therapeutic effects in clinical studies, including clinically alleviating symptoms of schizophrenic patients and ameliorating cognitive function in Alzheimer’s patients with early phase. Herein we report the synthesis and preliminary evaluation of a ¹¹C-labeled positron emission tomography ligand based on a DAAO inhibitor, DAO-1903 (8). ¹¹C-Isotopologue of 8 was prepared in high radiochemical yield with high radiochemical purity (>99%) and high molar activity (>37 GBq/µmol). In vitro autoradiography studies indicated that the ligand possessed high in vitro specific binding to DAAO, while in vivo dynamic PET studies demonstrated that [¹¹C]8 failed to cross the blood–brain barrier possibly due to moderate brain efflux mechanism. Further chemical scaffold optimization is necessary to overcome limited brain permeability and improve specific binding.
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Citation Excerpt :
During these pathophysiological processes, DAAO could mediate the metabolic reaction of some important metabolites [4–6] (such as D-serine, hydrogen peroxide). Importantly, DAAO inhibitors screening has been the considerable pharmacological approach in depression and other diseases therapy, and immunochemical investigation [5,7,8]. Moreover, the related study for exploring DAAO inhibitors as the potential medicines for disease treatment has attracted great interesting of researchers.
In this work, a unique D-amino acid oxidase reactor for enhanced enzymolysis efficiency is presented. A kind of magnetic polymer matrices, composed of iron oxide nanoparticles and porous polymer membrane (poly styrene-co-maleic anhydride), was prepared. With covalent bonding D-Amino acid oxidase on the surface of the matrices and characterization of scanning electron microscope and vibrating sample magnetometer, it demonstrated that the membrane enzyme reactor was successfully constructed. The enzymolysis efficiency of the enzyme reactor was evaluated and the apparent Michaelis-Menten constants of D-Amino acid oxidase were determined (K_m was 1.10 mM, V_max was 23.8 mM min⁻¹) by a chiral ligand exchange capillary electrophoresis protocol with methionine as the substrate. The results indicated that the enzyme reactor could exhibit good stability and excellent reusability. Importantly, because the enzyme and the substrate could be confined into the pores of the matrices, the enzyme reactor displayed the improved enzymolysis efficiency due to the confinement effect. Further, the prepared enzyme reactor was applied for D-Amino acid oxidase inhibitors screening. It has displayed that the proposed protocol could pave a new way for fabrication of novel porous polymer membrane based enzyme reactors to screen enzyme inhibitors.
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Hypofunction of the N-methyl-d-aspartate receptor (NMDAR) has been implicated in the pathophysiology of schizophrenia. The NMDAR contains a d-serine/glycine site on the NR1 subunit that may be a promising therapeutic target for psychiatric illness. This review outlines the complex regulation of endogenous NMDAR d-serine/glycine site agonists and explores their contribution to schizophrenia pathogenesis and their potential clinical utility. Genetic studies have associated genes influencing NMDAR d-serine/glycine site activation with an increased susceptibility to schizophrenia. Postmortem studies have identified abnormalities in several transcripts affecting d-serine/glycine site activity, consistent with in vivo reports of alterations in levels of endogenous d-serine/glycine site agonists and antagonists. Genetically modified mice with aberrant NMDAR d-serine/glycine site function model certain features of the negative and cognitive symptoms of schizophrenia, and similar behavioral abnormalities have been observed in other candidate genes models. Compounds that directly activate the NMDAR d-serine/glycine site or inhibit glycine transport have demonstrated beneficial effects in preclinical models and clinical trials. Future pharmacological approaches for schizophrenia treatment may involve targeting enzymes that affect d-serine synthesis and metabolism.
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Ionotropic AMPA and NMDA glutamate receptors are ligand-gated ion channels that mediate fast synaptic transmission in the brain and play a crucial role in learning and memory. Dysfunction of these receptors is believed to be associated with a number of neuropsychiatric disorders, including schizophrenia. As direct activation of these ionotropic receptors can lead to excitoxicity, allosteric modulation of these receptors could minimize side-effects to achieve better therapeutic efficacy. Our review here focuses on the allosteric modulation of the NMDA receptor. Endogenous glycine and d-serine both act as co-agonists on the strychnine-insensitive GlyB site on the NMDA receptor, and along with glutamate, co-activate the NMDA receptor. Forebrain synaptic glycine and d-serine levels are regulated by the Glycine Transporter-1 (GlyT1) and the arginine–serine–cysteine transporter-1 (Asc-1), respectively; in addition to d-serine metabolism by d-Amino Acid Oxidase (DAAO). Together, these processes prevent the GlyB site from being saturated by the high extracellular levels of brain glycine, and perhaps d-serine, in vivo. Blockade of NMDA receptors by phencyclidine induces schizophrenia-like symptoms with the associated cognitive deficits. It was proposed that: a) blockade of GlyT1 mediated reuptake of glycine, or b) inhibition of d-amino Acid Oxidase, or Asc-1 will elevate brain glycine, and d-serine to upregulate NMDA receptor functions via glycine and d-serine co-agonistic allosteric modulation of the GlyB sites on the NMDA receptor. These approaches may provide novel treatments to schizophrenia, provided that some of the known adverse effects associated with existing GlyT1 agents can be safely and adequately dealt with.
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We review the role of two susceptibility genes; G72 and DAAO in glutamate neurotransmission and the aetiology of schizophrenia. The gene product of G72 is an activator of DAAO (D-amino acid oxidase), which is the only enzyme oxidising D-serine. D-serine is an important co-agonist for the NMDA glutamate receptor and plays a role in neuronal migration and cell death. Studies of D-serine revealed lower serum levels in schizophrenia patients as compared to healthy controls. Furthermore, administration of D-serine as add-on medication reduced the symptoms of schizophrenia. The underlying mechanism of the involvement of G72 and DAAO in schizophrenia is probably based on decreased levels of D-serine and decreased NMDA receptor functioning in patients. The involvement of this gene is therefore indirect support for the glutamate dysfunction hypothesis in schizophrenia.
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Recently, the gene called DAAO was reported to be associated with schizophrenia in the French Canadian populations. Here, we report a result obtained in the study of our large collection of 547 schizophrenia cases and 536 controls in the Chinese population. Six single-nucleotide polymorphisms (SNPs) were genotyped at and around the DAAO locus, covering a 10-kb region entirely encompassing the complementary DNA sequences of DAAO. We found statistically significant differences in allele distributions on one marker: SNP rs3741775 (P = 0.0000001). In the haplotype analysis based on the information of linkage-disequilibrium block across this gene locus, we demonstrated a highly significant association between schizophrenia and a DAAO haplotype (P = 2.0173 × 10⁻²¹), which therefore provides an independent statistical support for association of the DAAO gene with schizophrenia and indicates that the DAAO gene may play a significant role in the etiology of schizophrenia in the Han Chinese.

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^‡: Present address: Department of Biochemistry, Hyogo College of Medicine, Nishinomiya 663, Japan.

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Immunochemical relationship of d-amino acid oxidases in various tissues and animals

Abstract

Biochim. biophys. Acta

Biochim. biophys. Acta

Expl Cell Res.

Brain Res. Bull.

Biochim. biophys. Acta

J. biol. Chem.

Bioorg. Chem.

FEBS Lett.

Comp. Biochem. Physiol.

Comp. Biochem. Physiol.

J. biol. Chem.

Biochim. biophys. Acta

Anal. Biochem.

The genetic and biochemical properties of the d-Amino acid oxidases in human tissues

Ann. hum. Genet.

d-Amino acid oxidase from pig kidney [d-amino acid: O2 oxidoreductase (deaminating), E.C. 1.4.3.3]

Biochem. Prep.

d-Amino acid oxidase in leukocytes: a possible d-amino-acid-linked antimicrobial system

Molecular cloning and sequence analysis of cDNAs encoding porcine kidney d-amino acid oxidase

Biochemistry

Studies on peroxisomes. III. Further studies on the intraparticulate localization of peroxisomal components in the liver of the rat

Biochim. biophys. Acta

Histochemical staining of cells containing flavoenzyme d-amino acid oxidase based on its enzymatic activity: application of a coupled peroxidation method

Acta Histochem. Cytochem.

d-Amino acid oxidase from pig kidney [d-amino acid: O₂ oxidoreductase (deaminating), E.C. 1.4.3.3]