Distribution of freed-serine in vertebrate brains

Nagata, Yoko; Horiike, Kihachiro; Maeda, Toshihiro

doi:10.1016/0006-8993(94)91932-1

Cited by 148 publications

(81 citation statements)

References 22 publications

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“…The data are in basic agreement and extend those of the literature. It was reported that only traces of d-Ser were detectable in brains of chicken, frog and carp, but large amounts in the brains (cerebra) of mouse, rat and bovine (Nagata et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

“…Further, derivatization of dl-amino acids with Marfey's reagent (1-fluoro-2,4-dinitrophenyl-l-alanine Quantification of free d-amino acids 467 ORIGINAL RESEARCH amide) followed by thin-layer chromatographic separation of the resulting diastereomers was intensively used for the determination of d-Ala in physiological samples (Konno et al, 1993;Nagata et al, 1994). An overview of the general use of Marfey's reagent and some variants has recently been published (Bhushan and Brückner, 2004).…”

Section: Introductionmentioning

confidence: 99%

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Gas chromatographic quantification of free D‐amino acids in higher vertebrates

Pätzold¹,

Schieber²,

Brückner³

2005

Biomedical Chromatography

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D-amino acids were determined in brain, body fluids (urine, blood coagulate, serum, plasma) and faeces of animals belonging to nine out of 11 taxonomic orders of vertebrates (Artiodactyla, Aves, Carnivora, Lagomorpha, Marsupalia, Osteichthyes, Primates, Rodentia, Tubilidentata). Free amino acids were isolated by means of cation exchangers and converted into volatile N(O)-perfluoroacylamino acid propyl esters. Derivatives of amino acids were separated into d-and l-enantiomers using Chirasil-l-Val capillary columns and detected by selected ion monitoring mass spectrometry. Quantification of amino acids was achieved by comparison of analytes with amino acid standards using l-norleucine as internal standard. Large relative amounts of d-serine were determined in brains of mammals but not of birds. In body fluids the d-enantiomers of most proteinogenic l-amino acids were detected, largest absolute and relative amounts were found in urine. Therein quantities of d-Ala and d-Ser exceeded 50% relative to the l-enantiomers in many instances.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Gas chromatographic quantification of free D‐amino acids in higher vertebrates

Pätzold¹,

Schieber²,

Brückner³

2005

Biomedical Chromatography

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“…In rat brains, the localization of D-amino acid oxidase activity is reciprocal to that of D-serine (8,9), suggesting that D-amino acid oxidase determines the basal levels of D-serine in mammalian brains. However, we have found recently that, in the chicken brain, D-serine is degraded mainly by a D-serine dehydratase (DSD) 4 (10), which catalyzes the ␣,␤-elimination of water from D-serine to form pyruvate and ammonia.…”

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confidence: 99%

Crystal Structure of a Zinc-dependent d-Serine Dehydratase from Chicken Kidney

Tanaka

Senda

Venugopalan

et al. 2011

Journal of Biological Chemistry

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D-Serine is a co-agonist of the NMDA receptor, an excitatory neurotransmitter receptor important for higher brain functions, including learning and memory (1, 2). The NMDA receptor is a glutamate-gated ion channel (3), and glutamate does not activate the receptor unless a co-agonist binding site is simultaneously occupied by D-serine or glycine (4). Because significant concentrations of D-serine exist in vertebrate brains (5), D-serine is believed to physiologically control the sensitivity of the NMDA receptor to glutamate (6).In mammals, D-serine is produced by a bifunctional serine racemase/dehydratase (7) and is mainly degraded by D-amino acid oxidase (2, 7). In rat brains, the localization of D-amino acid oxidase activity is reciprocal to that of D-serine (8, 9), suggesting that D-amino acid oxidase determines the basal levels of D-serine in mammalian brains. However, we have found recently that, in the chicken brain, D-serine is degraded mainly by a D-serine dehydratase (DSD) 4 (10), which catalyzes the ␣,␤-elimination of water from D-serine to form pyruvate and ammonia. In addition, we have found that the chicken DSD (chDSD) has a primary structure similar to those of metal-activated D-threonine aldolases (11-13), which are fold-type III PLP-dependent enzymes (14), and is distinct from a well known metal-independent bacterial DSD (dsdA) belonging to the foldtype II PLP-dependent enzyme family (14,15). Interestingly, a fold-type III family protein coded by gene YGL196W of Saccharomyces cerevisiae was recently identified as a zinc-dependent DSD (scDSD) (16). To understand why avian species use DSD to metabolize D-serine in the brain and its physiological functions, it is important to reveal the structural and enzymatic properties of this novel DSD family.In the present study, we showed that chDSD requires Zn 2ϩ just as scDSD does. Then, to reveal the catalytic roles of Zn 2ϩ in the dehydration of D-serine, we determined the crystal structures of chDSD, EDTA-treated chDSD, and the EDTA-treated chDSD⅐D-serine complex. Although there is only one DSD entry in the Protein Data Bank (PDB), DSD from Burkholderia xenovorans LB400 (PDB code 3GWQ), the structure contains neither PLP nor zinc, and the enzymatic properties of this DSD *

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“…Neurophysiological studies of expressed NMDA receptors indicate that with certain combinations of NR1 and NR2 subunits, D-serine is up to three times more potent than glycine at the glycine site (Matsui et al, 1995;Priestley et al, 1995). Although D-amino acids have long been known to exist in bacteria, worms, and insects (Corrigan, 1969), only very recently have high levels of D-serine been demonstrated in mammalian tissues, especially in the brain (Hashimoto et al, 1992a(Hashimoto et al, , 1993aNagata, 1992;Chouinard et al, 1993;Nagata et al, 1994).We have mapped D-serine immunohistochemically in rat brain and observed a pattern that parallels the localization of D-serine binding sites associated with NMDA receptors in the forebrain (Schell et al, 1995). D-Serine is concentrated in gray matter regions enriched in NMDA receptors and is selectively localized to protoplasmic astrocytes.…”

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confidence: 99%

d-Serine as a Neuromodulator: Regional and Developmental Localizations in Rat Brain Glia Resemble NMDA Receptors

Schell¹,

Brady²,

Molliver³

et al. 1997

J. Neurosci.

391

349

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D-Serine is localized in mammalian brain to a discrete population of glial cells near NMDA receptors, suggesting that D-serine is an endogenous agonist of the receptor-associated glycine site. To explore this possibility, we have compared the immunohistochemical localizations of D-serine, glycine, and NMDA receptors in rat brain. In the telencephalon, D-serine is concentrated in protoplasmic astrocytes, which are abundant in neuropil in close vicinity to NMDA receptor 2A/B subunits. Ultrastructural examination of the CA1 region of hippocampus reveals D-serine in the cytosolic matrix of astrocytes that ensheath neurons and blood vessels, whereas NR2A/B is concentrated in dendritic spines. By contrast, glycine immunoreactivity in telencephalon is the lowest in brain. During postnatal week 2, D-serine levels in cerebellum are comparable to those in adult cerebral cortex but fall to undetectable levels by day 26.During week 2, we observe parallel ontogeny of D-serine in Bergmann glia and NR2A/B in Purkinje cells, suggesting a role for astrocytic D-serine in NMDA receptor-mediated synaptogenesis. D-Serine in the radial processes of Bergmann glia is also well positioned to regulate NMDA receptor-dependent granule cell migration. In the inner granule layer, D-serine is found transiently in protoplasmic astrocytes surrounding glomeruli, where it could regulate development of the mossy fiber/granule cell synapse. D-Serine seems to be the endogenous ligand of glycine sites in the telencephalon and developing cerebellum, whereas glycine predominates in the adult cerebellum, olfactory bulb, and hindbrain. Key words: D-serine; glycine; NMDA receptor; glia; D-amino acid; cerebellumActivation of NMDA receptor channels requires both glutamate and stimulation of a "glycine site" (Johnson and Ascher, 1987;Reynolds et al., 1987;Kemp and Leeson, 1993). Neurophysiological studies of expressed NMDA receptors indicate that with certain combinations of NR1 and NR2 subunits, D-serine is up to three times more potent than glycine at the glycine site (Matsui et al., 1995;Priestley et al., 1995). Although D-amino acids have long been known to exist in bacteria, worms, and insects (Corrigan, 1969), only very recently have high levels of D-serine been demonstrated in mammalian tissues, especially in the brain (Hashimoto et al., 1992a(Hashimoto et al., , 1993aNagata, 1992;Chouinard et al., 1993;Nagata et al., 1994).We have mapped D-serine immunohistochemically in rat brain and observed a pattern that parallels the localization of D-serine binding sites associated with NMDA receptors in the forebrain (Schell et al., 1995). D-Serine is concentrated in gray matter regions enriched in NMDA receptors and is selectively localized to protoplasmic astrocytes. We have also demonstrated that agonists of non-NMDA receptors enhance the efflux of preloaded D-serine from cultures of cortical type 2 astrocytes. These data suggest that D-serine is an endogenous ligand at the glycine site of many NMDA receptors and that glutamate releases D-serine from glial ...

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Distribution of freed-serine in vertebrate brains

Cited by 148 publications

References 22 publications

Gas chromatographic quantification of free D‐amino acids in higher vertebrates

Gas chromatographic quantification of free D‐amino acids in higher vertebrates

Crystal Structure of a Zinc-dependent d-Serine Dehydratase from Chicken Kidney

d-Serine as a Neuromodulator: Regional and Developmental Localizations in Rat Brain Glia Resemble NMDA Receptors

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