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Mitochondrial oxidative damage is a basic mechanism of aging, and multiple studies demonstrate that this process is attenuated by calorie restriction (CR). However, the molecular mechanism that underlies the beneficial effect of CR on mitochondrial dysfunction is unclear. Here, we investigated in mice the mechanisms underlying CR-mediated protection against(More)
Based on enzymatic activity, the localization and the identification of D-amino-acid oxidase-containing cells in rat whole brain was systematically studied in serial fixed sections. The oxidase activity was absent or scarce in the forebrain, was confined to the brain stem (midbrain, pons and medulla oblongata) and cerebellum, and its localization was(More)
Free D-serine distribution in vertebrate brains was investigated. In various brain regions of the lower vertebrate species, carp, frog and chick, free D-serine levels were low. On the contrary, in the mammals, mouse, rat and bull, the contents of free D-serine were high in the forebrain (around 400 nmol/g wet weight, and the ratio of D-serine to L-serine,(More)
Three isozymes of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas arvilla C-1 were separated using DEAE-Toyopearl chromatography. The specific activities of each isozyme were similar to one another. The molecular weights of isozymes 1, 2, and 3 were estimated to be approximately 67,000, 64,000, and 59,000, respectively, from gel filtration. On(More)
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. The oxidases in kidney, liver and cerebellum of hog were indistinguishable as regards immunoreactivity toward anti-hog kidney DAO antibody, specific(More)
An enzymatic method for measuring the O(2) concentrations of aqueous solutions was developed by involving 4-chlorocatechol and catechol 2,3-dioxygenase from Pseudomonas putida. With this system, the amount of O(2) in a sample solution can be measured as the amount of 5-chloro-2-hydroxymuconate semialdehyde formed through the enzyme reaction. The product was(More)
D-serine dehydratase (DSD) catalyses the conversion of d-serine to pyruvate and ammonia. d-Serine is a physiological modulator of glutamate neurotransmission in vertebrate brains. In mammals d-serine is degraded by d-amino-acid oxidase, whereas in chicken brain it is degraded by DSD, as we have recently demonstrated [Tanaka et al. (2007) Anal. Biochem. 362,(More)
N-methyl-D-aspartate receptors (NMDARs) play critical roles in excitatory synaptic transmission in the vertebrate central nervous system. NMDARs need D-serine for their channel activities in various brain regions. In mammalian brains, D-serine is produced from L-serine by serine racemase and degraded by D-amino acid oxidase (DAO) to 3-hydroxypyruvate. In(More)
Recent evidence has shown that D-aspartate modulates hormone secretion in the vertebral neuroendocrine system. Because only D-aspartate oxidase (DDO) can degrade D-aspartate, we determined DDO localisation in the pituitary and pineal glands to elucidate the control mechanisms of local D-aspartate concentration. Brain tissues and pituitary and pineal glands(More)