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

Katagiri, Masatoshi; Tojo, Hiromasa; Horiike, Kihachiro; Yamano, Toshìo

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

Cited by 23 publications

(20 citation statements)

References 27 publications

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“…As the regulation mechanisms of the D-amino acid amounts in mammals, the biosynthesis of the D-amino acids from the L-enantiomers, 10,55,56) the transporters that take up specific D-amino acids into cells, 57,58) and the oxidative degradation of D-amino acids [25][26][27] are well known. DAO, ubiquitously present in mammals, catalyzes the oxidation of neutral D-amino acids to form a-keto acids, and the amounts of neutral D-amino acids naturally occurring in these animals should be diminished by the DAO reaction.…”

Section: Distribution Of D-amino Acids In the Brains Of Mutant Mice Lmentioning

confidence: 99%

“…25) This enzyme is widely observed in creatures, and most of the vertebrates have DAO in the kidney, liver and brain. 26,27) Since the oxidation by DAO is one of the major regulatory pathways of Damino acids, it is important to investigate the effects of DAO activity on the amounts of naturally occurring D-amino acids in mammals. In this review, we present the tissue distributions of D-Asp, D-Ser, D-Ala, D-Leu and D-Pro in the brains of the mutant ddY/DAO Ϫ mice lacking DAO activity, and control ddY/DAO ϩ mice having normal DAO activity.…”

Section: Introductionmentioning

confidence: 99%

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Sensitive Determination of D-Amino Acids in Mammals and the Effect of D-Amino-Acid Oxidase Activity on Their Amounts

Hamase

Konno

Morikawa

et al. 2005

Biological & Pharmaceutical Bulletin

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Section: Distribution Of D-amino Acids In the Brains Of Mutant Mice Lmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Sensitive Determination of D-Amino Acids in Mammals and the Effect of D-Amino-Acid Oxidase Activity on Their Amounts

Hamase

Konno

Morikawa

et al. 2005

Biological & Pharmaceutical Bulletin

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“…Expressed as mol/min/mg of protein with d-alanine as a substrate in hog tissues (Katagiri et al, 1991). In lung tissue the enzyme was detected with an enzyme immunoassay; however, enzyme activity could not be determined.…”

mentioning

confidence: 99%

“…The ability of L-amino acid oxidase to also oxidize ␣-hydroxy acids is peculiar to the rat kidney, where the enzyme is frequently designated ␣-hydroxy acid oxidase. Amino acid oxidase activity in hog has been observed in kidney, liver, and brain (Table 2) (Katagiri et al, 1991). Based on an enzyme immunoassay, the enzyme was detected in low amounts in lung, although no enzyme activity could be detected.…”

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confidence: 99%

Enzyme-Catalyzed Activation of Anticancer Prodrugs

2004

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“…C. elegans DAO. In mammals, DAO and DDO activities are highest in the kidney, followed by the liver and brain, and are low in other peripheral tissues (3,33,67,72). Exogenous D-amino acids derived from enterobacteria and/or the diet can be absorbed by the intestine and transferred via the circulatory system to the kidney and liver, where they are metabolized by DAO or DDO (13).…”

Section: Discussionmentioning

confidence: 99%

Spatiotemporal Localization of d-Amino Acid Oxidase and d-Aspartate Oxidases during Development in Caenorhabditis elegans

Saitoh

Katane

Kawata

et al. 2012

Molecular and Cellular Biology

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(58,61). Its concentration in the blood of silkworms was reported to increase during particular stages of metamorphosis, although the physiological role of D-Ser in metamorphosis remains unclear (11). It is also present in the mammalian forebrain, where it persists at high concentrations throughout the life of the animal. DSer is now considered a neuromodulator that binds to the glycinebinding site of the N-methyl-D-Asp (NMDA) receptor, a subtype of the L-glutamate (L-Glu) receptor, and potentiates glutamatergic neurotransmission in the central nervous system (51,60,68). In fact, astroglia-derived D-Ser has been shown to regulate NMDA receptor-dependent long-term potentiation and/or long-term depression, which are basic processes of learning and memory, in the hypothalamic and hippocampal excitatory synapses (25,54). In addition, D-Ser is also found in the cerebellum during the early postnatal period, and it was recently reported that D-Ser derived from the Bergmann glia serves as an endogenous ligand for the ␦2 L-Glu receptor to regulate long-term depression at synapses between parallel fibers and Purkinje cells in the immature cerebellum but not the mature one (31). These lines of evidence suggest the physiological significance of D-Ser in the regulation of higher brain functions through the L-Glu receptors, and indeed, perturbation of D-Ser levels in the central nervous system has now been implicated in the pathophysiology of various neuropsychiatric disorders, including schizophrenia (4, 23, 24, 71), Alzheimer's disease (28, 70), and amyotrophic lateral sclerosis (59).Unlike the tissue-specific expression of D-Ser, substantial amounts of free D-Asp are present in a wide variety of tissues and cells in invertebrates and vertebrates, particularly in the central nervous, neuroendocrine, and endocrine systems. D-Asp is proposed to play an important role in regulating developmental processes, hormone secretion, and steroidogenesis (12,26,35). For instance, it has been reported that in male lizards, intraperitoneally administered D-Asp is taken up rapidly by the testis, which induces a significant increase in testosterone levels and a significant decrease in 17␤-estradiol levels in the testis and plasma (57). Interestingly, a reverse relationship is found between males and females; specifically, in female lizards, exogenous D-Asp induces a significant decrease in testosterone levels in the ovary and plasma, while it enhances follicular production of 17␤-estradiol by upregulating the local aromatase activity (2). Similar findings have also been reported in studies of the green frog (16, 56). These observations suggest that D-Asp is an important regulatory molecule of gonads. In addition, it was recently shown that the amount of D-Asp in human seminal plasma and spermatozoa is significantly reduced in oligoasthenoteratospermic and/or azoospermic donors compared with normospermic donors (14). Moreover, in human female patients undergoing in vitro fertilization, the D-Asp content of the preovulatory follicular fluid ...

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

Cited by 23 publications

References 27 publications

Sensitive Determination of D-Amino Acids in Mammals and the Effect of D-Amino-Acid Oxidase Activity on Their Amounts

Sensitive Determination of D-Amino Acids in Mammals and the Effect of D-Amino-Acid Oxidase Activity on Their Amounts

Enzyme-Catalyzed Activation of Anticancer Prodrugs

Spatiotemporal Localization of d-Amino Acid Oxidase and d-Aspartate Oxidases during Development in Caenorhabditis elegans

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