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Volumn 29, Issue 8, 2006, Pages 481-491

d-Serine signalling in the brain: friend and foe

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; ASPARAGINE; ASPARTIC ACID; CALCIUM ION; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; DEXTRO SERINE; GLUTAMIC ACID; MAGNESIUM ION; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NITRIC OXIDE; POTASSIUM ION; PROTEIN KINASE C;

EID: 33746362592     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tins.2006.06.008     Document Type: Review
Times cited : (139)

References (96)
  • 1
    • 0141533205 scopus 로고    scopus 로고
    • New roles for astrocytes: redefining the functional architecture of the brain
    • Nedergaard M., et al. New roles for astrocytes: redefining the functional architecture of the brain. Trends Neurosci. 26 (2003) 523-530
    • (2003) Trends Neurosci. , vol.26 , pp. 523-530
    • Nedergaard, M.1
  • 2
    • 0033566709 scopus 로고    scopus 로고
    • Three-dimensional relationships between hippocampal synapses and astrocytes
    • Ventura R., and Harris K.M. Three-dimensional relationships between hippocampal synapses and astrocytes. J. Neurosci. 19 (1999) 6897-6906
    • (1999) J. Neurosci. , vol.19 , pp. 6897-6906
    • Ventura, R.1    Harris, K.M.2
  • 3
    • 0035287432 scopus 로고    scopus 로고
    • Glia: listening and talking to the synapse
    • Haydon P.G. Glia: listening and talking to the synapse. Nat. Rev. Neurosci. 2 (2001) 185-193
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 185-193
    • Haydon, P.G.1
  • 4
    • 23044435896 scopus 로고    scopus 로고
    • Astrocytes, from brain glue to communication elements: the revolution continues
    • Volterra A., and Meldolesi J. Astrocytes, from brain glue to communication elements: the revolution continues. Nat. Rev. Neurosci. 6 (2005) 626-640
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 626-640
    • Volterra, A.1    Meldolesi, J.2
  • 5
    • 0036802874 scopus 로고    scopus 로고
    • Role of glia in synapse development
    • Pfrieger F.W. Role of glia in synapse development. Curr. Opin. Neurobiol. 12 (2002) 486-490
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 486-490
    • Pfrieger, F.W.1
  • 6
    • 4344597795 scopus 로고    scopus 로고
    • Glial modulation of synaptic transmission: Insights from the supraoptic nucleus of the hypothalamus
    • Oliet S.H., et al. Glial modulation of synaptic transmission: Insights from the supraoptic nucleus of the hypothalamus. Glia 47 (2004) 258-267
    • (2004) Glia , vol.47 , pp. 258-267
    • Oliet, S.H.1
  • 7
    • 0035993232 scopus 로고    scopus 로고
    • Neurobiology through the looking-glass: d-serine as a new glial-derived transmitter
    • Wolosker H., et al. Neurobiology through the looking-glass: d-serine as a new glial-derived transmitter. Neurochem. Int. 41 (2002) 327-332
    • (2002) Neurochem. Int. , vol.41 , pp. 327-332
    • Wolosker, H.1
  • 8
    • 2942718893 scopus 로고    scopus 로고
    • The N-methyl d-aspartate receptor glycine site and d-serine metabolism: an evolutionary perspective
    • Schell M.J. The N-methyl d-aspartate receptor glycine site and d-serine metabolism: an evolutionary perspective. Philos. Trans. R. Soc. Lond. B Biol. Sci. 359 (2004) 943-964
    • (2004) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.359 , pp. 943-964
    • Schell, M.J.1
  • 9
    • 0033539510 scopus 로고    scopus 로고
    • Serine racemase: a glial enzyme synthesizing d-serine to regulate glutamate-N-methyl-d-aspartate neurotransmission
    • Wolosker H., et al. Serine racemase: a glial enzyme synthesizing d-serine to regulate glutamate-N-methyl-d-aspartate neurotransmission. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 13409-13414
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13409-13414
    • Wolosker, H.1
  • 10
    • 0034601688 scopus 로고    scopus 로고
    • Human serine racemase: molecular cloning, genomic organization and functional analysis
    • De Miranda J., et al. Human serine racemase: molecular cloning, genomic organization and functional analysis. Gene 256 (2000) 183-188
    • (2000) Gene , vol.256 , pp. 183-188
    • De Miranda, J.1
  • 11
    • 0142058195 scopus 로고    scopus 로고
    • Rat cerebral serine racemase: amino acid deletion and truncation at carboxy terminus
    • Konno R. Rat cerebral serine racemase: amino acid deletion and truncation at carboxy terminus. Neurosci. Lett. 349 (2003) 111-114
    • (2003) Neurosci. Lett. , vol.349 , pp. 111-114
    • Konno, R.1
  • 12
    • 2942595866 scopus 로고    scopus 로고
    • Characterization and localization of a human serine racemase
    • Xia M., et al. Characterization and localization of a human serine racemase. Mol. Brain Res. 125 (2004) 96-104
    • (2004) Mol. Brain Res. , vol.125 , pp. 96-104
    • Xia, M.1
  • 13
    • 33644560634 scopus 로고    scopus 로고
    • Immunocytochemical analysis of d-serine distribution in the mammalian brain reveals novel anatomical compartmentalizations in glia and neurons
    • Williams S.M., et al. Immunocytochemical analysis of d-serine distribution in the mammalian brain reveals novel anatomical compartmentalizations in glia and neurons. Glia 53 (2006) 401-411
    • (2006) Glia , vol.53 , pp. 401-411
    • Williams, S.M.1
  • 14
    • 4143073125 scopus 로고    scopus 로고
    • Induction of serine racemase expression and d-serine release from microglia by amyloid β-peptide
    • Wu S.Z., et al. Induction of serine racemase expression and d-serine release from microglia by amyloid β-peptide. J. Neuroinflammation 1 (2004) 2
    • (2004) J. Neuroinflammation , vol.1 , pp. 2
    • Wu, S.Z.1
  • 15
    • 14944354601 scopus 로고    scopus 로고
    • Induction of serine racemase by inflammatory stimuli is dependent on AP-1
    • Wu S., and Barger S.W. Induction of serine racemase by inflammatory stimuli is dependent on AP-1. Ann. N. Y. Acad. Sci. 1035 (2004) 133-146
    • (2004) Ann. N. Y. Acad. Sci. , vol.1035 , pp. 133-146
    • Wu, S.1    Barger, S.W.2
  • 16
    • 33744900653 scopus 로고    scopus 로고
    • Neuron-derived d-serine: novel means to activate N-methyl-d-aspartate receptors
    • Kartvelishvily E., et al. Neuron-derived d-serine: novel means to activate N-methyl-d-aspartate receptors. J. Biol. Chem. 281 (2006) 14151-14162
    • (2006) J. Biol. Chem. , vol.281 , pp. 14151-14162
    • Kartvelishvily, E.1
  • 17
    • 0037195093 scopus 로고    scopus 로고
    • Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-d-aspartate (NMDA) receptor coagonist d-serine
    • De Miranda J., et al. Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-d-aspartate (NMDA) receptor coagonist d-serine. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 14542-14547
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14542-14547
    • De Miranda, J.1
  • 18
    • 0036912112 scopus 로고    scopus 로고
    • Allosteric regulation of mouse brain serine racemase
    • Neidle A., and Dunlop D.S. Allosteric regulation of mouse brain serine racemase. Neurochem. Res. 27 (2002) 1719-1724
    • (2002) Neurochem. Res. , vol.27 , pp. 1719-1724
    • Neidle, A.1    Dunlop, D.S.2
  • 19
    • 19944432442 scopus 로고    scopus 로고
    • Serine racemase modulates intracellular d-serine levels through an α,β-elimination activity
    • Foltyn V.N., et al. Serine racemase modulates intracellular d-serine levels through an α,β-elimination activity. J. Biol. Chem. 280 (2005) 1754-1763
    • (2005) J. Biol. Chem. , vol.280 , pp. 1754-1763
    • Foltyn, V.N.1
  • 20
    • 0037008687 scopus 로고    scopus 로고
    • Direct calcium binding results in activation of brain serine racemase
    • Cook S.P., et al. Direct calcium binding results in activation of brain serine racemase. J. Biol. Chem. 277 (2002) 27782-27792
    • (2002) J. Biol. Chem. , vol.277 , pp. 27782-27792
    • Cook, S.P.1
  • 21
    • 13844294076 scopus 로고    scopus 로고
    • Regulation of serine racemase activity by amino acids
    • Dunlop D.S., and Neidle A. Regulation of serine racemase activity by amino acids. Mol. Brain Res. 133 (2005) 208-214
    • (2005) Mol. Brain Res. , vol.133 , pp. 208-214
    • Dunlop, D.S.1    Neidle, A.2
  • 22
    • 25444532514 scopus 로고    scopus 로고
    • Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the β-eliminase activity
    • Strisovsky K., et al. Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the β-eliminase activity. Biochemistry 44 (2005) 13091-13100
    • (2005) Biochemistry , vol.44 , pp. 13091-13100
    • Strisovsky, K.1
  • 23
    • 13844306349 scopus 로고    scopus 로고
    • Serine racemase: activation by glutamate neurotransmission via glutamate receptor interacting protein and mediation of neuronal migration
    • Kim P.M., et al. Serine racemase: activation by glutamate neurotransmission via glutamate receptor interacting protein and mediation of neuronal migration. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 2105-2110
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 2105-2110
    • Kim, P.M.1
  • 24
    • 0035887859 scopus 로고    scopus 로고
    • Freshly isolated hippocampal CA1 astrocytes comprise two populations differing in glutamate transporter and AMPA receptor expression
    • Zhou M., and Kimelberg H.K. Freshly isolated hippocampal CA1 astrocytes comprise two populations differing in glutamate transporter and AMPA receptor expression. J. Neurosci. 21 (2001) 7901-7908
    • (2001) J. Neurosci. , vol.21 , pp. 7901-7908
    • Zhou, M.1    Kimelberg, H.K.2
  • 25
    • 31544465933 scopus 로고    scopus 로고
    • Serine racemase binds to PICK1: potential relevance to schizophrenia
    • Fujii K., et al. Serine racemase binds to PICK1: potential relevance to schizophrenia. Mol. Psychiatry 11 (2006) 150-157
    • (2006) Mol. Psychiatry , vol.11 , pp. 150-157
    • Fujii, K.1
  • 26
    • 0037472638 scopus 로고    scopus 로고
    • Mouse brain serine racemase catalyzes specific elimination of l-serine to pyruvate
    • Strisovsky K., et al. Mouse brain serine racemase catalyzes specific elimination of l-serine to pyruvate. FEBS Lett. 535 (2003) 44-48
    • (2003) FEBS Lett. , vol.535 , pp. 44-48
    • Strisovsky, K.1
  • 27
    • 0028988978 scopus 로고
    • d-serine, an endogenous synaptic modulator: localization to astrocytes and glutamate-stimulated release
    • Schell M.J., et al. d-serine, an endogenous synaptic modulator: localization to astrocytes and glutamate-stimulated release. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 3948-3952
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3948-3952
    • Schell, M.J.1
  • 28
    • 0033499883 scopus 로고    scopus 로고
    • Immunocytochemical localization of d-amino acid oxidase in rat brain
    • Moreno S., et al. Immunocytochemical localization of d-amino acid oxidase in rat brain. J. Neurocytol. 28 (1999) 169-185
    • (1999) J. Neurocytol. , vol.28 , pp. 169-185
    • Moreno, S.1
  • 29
    • 0037123710 scopus 로고    scopus 로고
    • Gene expression of d-amino acid oxidase in cultured rat astrocytes: regional and cell type specific expression
    • Urai Y., et al. Gene expression of d-amino acid oxidase in cultured rat astrocytes: regional and cell type specific expression. Neurosci. Lett. 324 (2002) 101-104
    • (2002) Neurosci. Lett. , vol.324 , pp. 101-104
    • Urai, Y.1
  • 30
    • 24944504370 scopus 로고    scopus 로고
    • Sensitive determination of d-amino acids in mammals and the effect of d-amino-acid oxidase activity on their amounts
    • Hamase K., et al. Sensitive determination of d-amino acids in mammals and the effect of d-amino-acid oxidase activity on their amounts. Biol. Pharm. Bull. 28 (2005) 1578-1584
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 1578-1584
    • Hamase, K.1
  • 31
    • 28744435349 scopus 로고    scopus 로고
    • Regulation of serine racemase activity by d-serine and nitric oxide in human glioblastoma cells
    • Shoji K., et al. Regulation of serine racemase activity by d-serine and nitric oxide in human glioblastoma cells. Neurosci. Lett. 392 (2006) 75-78
    • (2006) Neurosci. Lett. , vol.392 , pp. 75-78
    • Shoji, K.1
  • 32
    • 31344473768 scopus 로고    scopus 로고
    • Mutual regulation between serine and nitric oxide metabolism in human glioblastoma cells
    • Shoji K., et al. Mutual regulation between serine and nitric oxide metabolism in human glioblastoma cells. Neurosci. Lett. 394 (2006) 163-167
    • (2006) Neurosci. Lett. , vol.394 , pp. 163-167
    • Shoji, K.1
  • 34
    • 29244457820 scopus 로고    scopus 로고
    • Measuring the effect of glutamate receptor agonists on extracellular d-serine concentrations in the rat striatum using online microdialysis-capillary electrophoresis
    • Ciriacks C.M., and Bowser M.T. Measuring the effect of glutamate receptor agonists on extracellular d-serine concentrations in the rat striatum using online microdialysis-capillary electrophoresis. Neurosci. Lett. 393 (2006) 200-205
    • (2006) Neurosci. Lett. , vol.393 , pp. 200-205
    • Ciriacks, C.M.1    Bowser, M.T.2
  • 35
    • 17244382523 scopus 로고    scopus 로고
    • Glutamate receptor activation triggers a calcium-dependent and SNARE protein-dependent release of the gliotransmitter d-serine
    • Mothet J.P., et al. Glutamate receptor activation triggers a calcium-dependent and SNARE protein-dependent release of the gliotransmitter d-serine. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 5606-5611
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 5606-5611
    • Mothet, J.P.1
  • 36
    • 0037428452 scopus 로고    scopus 로고
    • Storage and release of ATP from astrocytes in culture
    • Coco S., et al. Storage and release of ATP from astrocytes in culture. J. Biol. Chem. 278 (2003) 1354-1362
    • (2003) J. Biol. Chem. , vol.278 , pp. 1354-1362
    • Coco, S.1
  • 37
    • 2542501505 scopus 로고    scopus 로고
    • Astrocytes contain a vesicular compartment that is competent for regulated exocytosis of glutamate
    • Bezzi P., et al. Astrocytes contain a vesicular compartment that is competent for regulated exocytosis of glutamate. Nat. Neurosci. 7 (2004) 613-620
    • (2004) Nat. Neurosci. , vol.7 , pp. 613-620
    • Bezzi, P.1
  • 38
    • 0037040505 scopus 로고    scopus 로고
    • Glial transport of the neuromodulator d-serine
    • Ribeiro C.S., et al. Glial transport of the neuromodulator d-serine. Brain Res. 929 (2002) 202-209
    • (2002) Brain Res. , vol.929 , pp. 202-209
    • Ribeiro, C.S.1
  • 39
    • 0031893563 scopus 로고    scopus 로고
    • Glial calcium: homeostasis and signaling function
    • Verkhratsky A., et al. Glial calcium: homeostasis and signaling function. Physiol. Rev. 78 (1998) 99-141
    • (1998) Physiol. Rev. , vol.78 , pp. 99-141
    • Verkhratsky, A.1
  • 40
    • 0031578954 scopus 로고    scopus 로고
    • Uptake of d- and l-serine in C6 glioma cells
    • Hayashi F., et al. Uptake of d- and l-serine in C6 glioma cells. Neurosci. Lett. 239 (1997) 85-88
    • (1997) Neurosci. Lett. , vol.239 , pp. 85-88
    • Hayashi, F.1
  • 41
    • 0034811460 scopus 로고    scopus 로고
    • Uptake of d-serine by synaptosomal P2 fraction isolated from rat brain
    • Yamamoto N., et al. Uptake of d-serine by synaptosomal P2 fraction isolated from rat brain. Synapse 42 (2001) 84-86
    • (2001) Synapse , vol.42 , pp. 84-86
    • Yamamoto, N.1
  • 42
    • 0037150760 scopus 로고    scopus 로고
    • A novel alanine-insensitive d-serine transporter in rat brain synaptosomal
    • Javitt D.C., et al. A novel alanine-insensitive d-serine transporter in rat brain synaptosomal. Brain Res. 941 (2002) 146-149
    • (2002) Brain Res. , vol.941 , pp. 146-149
    • Javitt, D.C.1
  • 43
    • 21344445016 scopus 로고    scopus 로고
    • d-Serine uptake by isolated retinas is consistent with ASCT-mediated transport
    • O'Brien K.B., et al. d-Serine uptake by isolated retinas is consistent with ASCT-mediated transport. Neurosci. Lett. 385 (2005) 58-63
    • (2005) Neurosci. Lett. , vol.385 , pp. 58-63
    • O'Brien, K.B.1
  • 44
    • 23644450359 scopus 로고    scopus 로고
    • Lack of the alanine-serine-cysteine transporter 1 causes tremors, seizures, and early postnatal death in mice
    • Xie X., et al. Lack of the alanine-serine-cysteine transporter 1 causes tremors, seizures, and early postnatal death in mice. Brain Res. 1052 (2005) 212-221
    • (2005) Brain Res. , vol.1052 , pp. 212-221
    • Xie, X.1
  • 45
    • 1542640509 scopus 로고    scopus 로고
    • Distribution and pharmacology of alanine-serine-cysteine transporter 1 (ASC-1) in rodent brain
    • Helboe L., et al. Distribution and pharmacology of alanine-serine-cysteine transporter 1 (ASC-1) in rodent brain. Eur. J. Neurosci. 18 (2003) 2227-2238
    • (2003) Eur. J. Neurosci. , vol.18 , pp. 2227-2238
    • Helboe, L.1
  • 46
    • 12144289325 scopus 로고    scopus 로고
    • High affinity d- and l-serine transporter ASC-1: cloning and dendritic localization in the rat cerebral and cerebellar cortices
    • Matsuo H., et al. High affinity d- and l-serine transporter ASC-1: cloning and dendritic localization in the rat cerebral and cerebellar cortices. Neurosci. Lett. 358 (2004) 123-126
    • (2004) Neurosci. Lett. , vol.358 , pp. 123-126
    • Matsuo, H.1
  • 47
    • 0031046980 scopus 로고    scopus 로고
    • d-Serine as a neuromodulator: regional and developmental localizations in rat brain glia resemble NMDA receptors
    • Schell M.J., et al. d-Serine as a neuromodulator: regional and developmental localizations in rat brain glia resemble NMDA receptors. J. Neurosci. 17 (1997) 1604-1615
    • (1997) J. Neurosci. , vol.17 , pp. 1604-1615
    • Schell, M.J.1
  • 48
    • 0038561177 scopus 로고    scopus 로고
    • Expression mechanisms underlying long-term potentiation: a postsynaptic view
    • Nicoll R.A. Expression mechanisms underlying long-term potentiation: a postsynaptic view. Philos. Trans. R. Soc. Lond. B Biol. Sci. 358 (2003) 721-726
    • (2003) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.358 , pp. 721-726
    • Nicoll, R.A.1
  • 49
    • 0344303605 scopus 로고    scopus 로고
    • Contribution of astrocytes to hippocampal long-term potentiation through release of d-serine
    • Yang Y., et al. Contribution of astrocytes to hippocampal long-term potentiation through release of d-serine. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 15194-15199
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 15194-15199
    • Yang, Y.1
  • 51
    • 16244413228 scopus 로고    scopus 로고
    • d-serine enhances impaired long-term potentiation in CA1 subfield of hippocampal slices from aged senescence-accelerated mouse prone/8
    • Yang S., et al. d-serine enhances impaired long-term potentiation in CA1 subfield of hippocampal slices from aged senescence-accelerated mouse prone/8. Neurosci. Lett. 379 (2005) 7-12
    • (2005) Neurosci. Lett. , vol.379 , pp. 7-12
    • Yang, S.1
  • 52
    • 33744493671 scopus 로고    scopus 로고
    • A critical role for the glial-derived neuromodulator d-serine in the age-related deficits of cellular mechanisms of learning and memory
    • Mothet J.P., et al. A critical role for the glial-derived neuromodulator d-serine in the age-related deficits of cellular mechanisms of learning and memory. Aging Cell 5 (2006) 267-274
    • (2006) Aging Cell , vol.5 , pp. 267-274
    • Mothet, J.P.1
  • 53
    • 0035808617 scopus 로고    scopus 로고
    • Exaggerated responses to chronic nociceptive stimuli and enhancement of N-methyl-d-aspartate receptor-mediated synaptic transmission in mutant mice lacking d-amino-acid oxidase
    • Wake K., et al. Exaggerated responses to chronic nociceptive stimuli and enhancement of N-methyl-d-aspartate receptor-mediated synaptic transmission in mutant mice lacking d-amino-acid oxidase. Neurosci. Lett. 297 (2001) 25-28
    • (2001) Neurosci. Lett. , vol.297 , pp. 25-28
    • Wake, K.1
  • 54
    • 0034712857 scopus 로고    scopus 로고
    • d-serine is an endogenous ligand for the glycine site of the N-methyl- d -aspartate receptor
    • Mothet J.P., et al. d-serine is an endogenous ligand for the glycine site of the N-methyl- d -aspartate receptor. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 4926-4931
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4926-4931
    • Mothet, J.P.1
  • 55
    • 0037636496 scopus 로고    scopus 로고
    • d-serine and serine racemase are present in the vertebrate retina and contribute to the physiological activation of NMDA receptors
    • Stevens E.R., et al. d-serine and serine racemase are present in the vertebrate retina and contribute to the physiological activation of NMDA receptors. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 6789-6794
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 6789-6794
    • Stevens, E.R.1
  • 56
    • 30144443355 scopus 로고    scopus 로고
    • Cellular distribution of d-serine, serine racemase and d-amino acid oxidase in the rat vestibular sensory epithelia
    • Dememes D., et al. Cellular distribution of d-serine, serine racemase and d-amino acid oxidase in the rat vestibular sensory epithelia. Neuroscience 137 (2006) 991-997
    • (2006) Neuroscience , vol.137 , pp. 991-997
    • Dememes, D.1
  • 57
    • 0035882489 scopus 로고    scopus 로고
    • Neurotrophin secretion from cultured microglia
    • Nakajima K., et al. Neurotrophin secretion from cultured microglia. J. Neurosci. Res. 65 (2001) 322-331
    • (2001) J. Neurosci. Res. , vol.65 , pp. 322-331
    • Nakajima, K.1
  • 58
    • 0032965534 scopus 로고    scopus 로고
    • Central nervous system neuronal migration
    • Hatten M.E. Central nervous system neuronal migration. Annu. Rev. Neurosci. 22 (1999) 511-539
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 511-539
    • Hatten, M.E.1
  • 59
    • 0141834805 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of cerebellar granule cell migration
    • Yacubova E., and Komuro H. Cellular and molecular mechanisms of cerebellar granule cell migration. Cell Biochem. Biophys. 37 (2003) 213-234
    • (2003) Cell Biochem. Biophys. , vol.37 , pp. 213-234
    • Yacubova, E.1    Komuro, H.2
  • 60
    • 18544374540 scopus 로고    scopus 로고
    • Mass spectrometrical analysis of human serine racemase in foetal brain
    • Hepner F., et al. Mass spectrometrical analysis of human serine racemase in foetal brain. J. Neural Transm. 112 (2005) 805-811
    • (2005) J. Neural Transm. , vol.112 , pp. 805-811
    • Hepner, F.1
  • 61
    • 3042547300 scopus 로고    scopus 로고
    • Serine racemase and d-serine transport in human placenta and evidence for a transplacental gradient for d-serine in humans
    • Chen Z., et al. Serine racemase and d-serine transport in human placenta and evidence for a transplacental gradient for d-serine in humans. J. Soc. Gynecol. Investig. 11 (2004) 294-303
    • (2004) J. Soc. Gynecol. Investig. , vol.11 , pp. 294-303
    • Chen, Z.1
  • 62
    • 0035971735 scopus 로고    scopus 로고
    • Ontogeny of ionotropic glutamate receptor expression in human fetal brain
    • Ritter L.M., et al. Ontogeny of ionotropic glutamate receptor expression in human fetal brain. Dev. Brain Res. 127 (2001) 123-133
    • (2001) Dev. Brain Res. , vol.127 , pp. 123-133
    • Ritter, L.M.1
  • 63
    • 13944275554 scopus 로고    scopus 로고
    • Neonatal NMDA receptor blockade disturbs neuronal migration in rat somatosensory cortex in vivo
    • Reiprich P., et al. Neonatal NMDA receptor blockade disturbs neuronal migration in rat somatosensory cortex in vivo. Cereb. Cortex 15 (2005) 349-358
    • (2005) Cereb. Cortex , vol.15 , pp. 349-358
    • Reiprich, P.1
  • 64
    • 0033667152 scopus 로고    scopus 로고
    • Mechanisms and disturbances of neuronal migration
    • Gressens P. Mechanisms and disturbances of neuronal migration. Pediatr. Res. 48 (2000) 725-730
    • (2000) Pediatr. Res. , vol.48 , pp. 725-730
    • Gressens, P.1
  • 65
    • 0345268791 scopus 로고    scopus 로고
    • Impaired development of the cerebellum in transgenic mice expressing the immediate-early protein IE180 of pseudorabies virus
    • Taharaguchi S., et al. Impaired development of the cerebellum in transgenic mice expressing the immediate-early protein IE180 of pseudorabies virus. Virology 307 (2003) 243-254
    • (2003) Virology , vol.307 , pp. 243-254
    • Taharaguchi, S.1
  • 66
    • 0037301661 scopus 로고    scopus 로고
    • The Yin and Yang of NMDA receptor signalling
    • Hardingham G.E., and Bading H. The Yin and Yang of NMDA receptor signalling. Trends Neurosci. 26 (2003) 81-89
    • (2003) Trends Neurosci. , vol.26 , pp. 81-89
    • Hardingham, G.E.1    Bading, H.2
  • 67
    • 0036830627 scopus 로고    scopus 로고
    • NMDA receptor pathways as drug targets
    • Kemp J.A., and McKernan R.M. NMDA receptor pathways as drug targets. Nat. Neurosci. 5 (2002) 1039-1042
    • (2002) Nat. Neurosci. , vol.5 , pp. 1039-1042
    • Kemp, J.A.1    McKernan, R.M.2
  • 68
    • 15044338779 scopus 로고    scopus 로고
    • Failures and successes of NMDA receptor antagonists: molecular basis for the use of open-channel blockers like memantine in the treatment of acute and chronic neurologic insults
    • Lipton S.A. Failures and successes of NMDA receptor antagonists: molecular basis for the use of open-channel blockers like memantine in the treatment of acute and chronic neurologic insults. NeuroRx 1 (2004) 101-110
    • (2004) NeuroRx , vol.1 , pp. 101-110
    • Lipton, S.A.1
  • 69
    • 0345269737 scopus 로고    scopus 로고
    • Disruption of glial glutamate transport by reactive oxygen species produced in motor neurons
    • Rao S.D., et al. Disruption of glial glutamate transport by reactive oxygen species produced in motor neurons. J. Neurosci. 23 (2003) 2627-2633
    • (2003) J. Neurosci. , vol.23 , pp. 2627-2633
    • Rao, S.D.1
  • 70
    • 0034800265 scopus 로고    scopus 로고
    • Glutamate release promotes growth of malignant gliomas
    • Takano T., et al. Glutamate release promotes growth of malignant gliomas. Nat. Med. 7 (2001) 1010-1015
    • (2001) Nat. Med. , vol.7 , pp. 1010-1015
    • Takano, T.1
  • 71
    • 0032903955 scopus 로고    scopus 로고
    • Glial cells in neurotoxicity development
    • Aschner M., et al. Glial cells in neurotoxicity development. Annu. Rev. Pharmacol. Toxicol. 39 (1999) 151-173
    • (1999) Annu. Rev. Pharmacol. Toxicol. , vol.39 , pp. 151-173
    • Aschner, M.1
  • 72
    • 1842587600 scopus 로고    scopus 로고
    • Astrocyte influences on ischemic neuronal death
    • Swanson R.A., et al. Astrocyte influences on ischemic neuronal death. Curr. Mol. Med. 4 (2004) 193-205
    • (2004) Curr. Mol. Med. , vol.4 , pp. 193-205
    • Swanson, R.A.1
  • 73
    • 8744276616 scopus 로고    scopus 로고
    • Amyloid β-peptide(1-42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain
    • Butterfield D.A., and Boyd-Kimball D. Amyloid β-peptide(1-42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain. Brain Pathol. 14 (2004) 426-432
    • (2004) Brain Pathol. , vol.14 , pp. 426-432
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 74
    • 0035146889 scopus 로고    scopus 로고
    • Activation of microglia by secreted amyloid precursor protein evokes release of glutamate by cystine exchange and attenuates synaptic function
    • Barger S.W., and Basile A.S. Activation of microglia by secreted amyloid precursor protein evokes release of glutamate by cystine exchange and attenuates synaptic function. J. Neurochem. 76 (2001) 846-854
    • (2001) J. Neurochem. , vol.76 , pp. 846-854
    • Barger, S.W.1    Basile, A.S.2
  • 75
    • 0033528286 scopus 로고    scopus 로고
    • Activation of microglial cells by PrP and β-amyloid fragments raises intracellular calcium through L-type voltage sensitive calcium channels
    • Silei V., et al. Activation of microglial cells by PrP and β-amyloid fragments raises intracellular calcium through L-type voltage sensitive calcium channels. Brain Res. 818 (1999) 168-170
    • (1999) Brain Res. , vol.818 , pp. 168-170
    • Silei, V.1
  • 76
    • 0031770236 scopus 로고    scopus 로고
    • Free d- and l-amino acids in ventricular cerebrospinal fluid from Alzheimer and normal subjects
    • Fisher G., et al. Free d- and l-amino acids in ventricular cerebrospinal fluid from Alzheimer and normal subjects. Amino Acids 15 (1998) 263-269
    • (1998) Amino Acids , vol.15 , pp. 263-269
    • Fisher, G.1
  • 77
    • 0028983838 scopus 로고
    • Free d-serine concentration in normal and Alzheimer human brain
    • Nagata Y., et al. Free d-serine concentration in normal and Alzheimer human brain. Brain Res. Bull. 38 (1995) 181-183
    • (1995) Brain Res. Bull. , vol.38 , pp. 181-183
    • Nagata, Y.1
  • 78
    • 9144232858 scopus 로고    scopus 로고
    • Possible role of d-serine in the pathophysiology of Alzheimer's disease
    • Hashimoto K., et al. Possible role of d-serine in the pathophysiology of Alzheimer's disease. Prog. Neuropsychopharmacol. Biol. Psychiatry 28 (2004) 385-388
    • (2004) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.28 , pp. 385-388
    • Hashimoto, K.1
  • 79
    • 15944378127 scopus 로고    scopus 로고
    • Targeting the JNK pathway as a therapeutic protective strategy for nervous system diseases
    • Bonny C., et al. Targeting the JNK pathway as a therapeutic protective strategy for nervous system diseases. Rev. Neurosci. 16 (2005) 57-67
    • (2005) Rev. Neurosci. , vol.16 , pp. 57-67
    • Bonny, C.1
  • 80
    • 18944381512 scopus 로고    scopus 로고
    • Neuroprotection against focal ischemic brain injury by inhibition of c-Jun N-terminal kinase and attenuation of the mitochondrial apoptosis-signaling pathway
    • Gao Y., et al. Neuroprotection against focal ischemic brain injury by inhibition of c-Jun N-terminal kinase and attenuation of the mitochondrial apoptosis-signaling pathway. J. Cereb. Blood Flow Metab. 25 (2005) 694-712
    • (2005) J. Cereb. Blood Flow Metab. , vol.25 , pp. 694-712
    • Gao, Y.1
  • 81
    • 28044436101 scopus 로고    scopus 로고
    • Acute treatment with morphine augments the expression of serine racemase and d-amino acid oxidase mRNAs in rat brain
    • Yoshikawa M., et al. Acute treatment with morphine augments the expression of serine racemase and d-amino acid oxidase mRNAs in rat brain. Eur. J. Pharmacol. 525 (2005) 94-97
    • (2005) Eur. J. Pharmacol. , vol.525 , pp. 94-97
    • Yoshikawa, M.1
  • 82
    • 25144513521 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase activation in dorsal root ganglion contributes to pain hypersensitivity
    • Doya H., et al. c-Jun N-terminal kinase activation in dorsal root ganglion contributes to pain hypersensitivity. Biochem. Biophys. Res. Commun. 335 (2005) 132-138
    • (2005) Biochem. Biophys. Res. Commun. , vol.335 , pp. 132-138
    • Doya, H.1
  • 83
    • 6344276678 scopus 로고    scopus 로고
    • Endogenous d-serine is involved in induction of neuronal death by N-methyl-d-aspartate and simulated ischemia in rat cerebrocortical slices
    • Katsuki H., et al. Endogenous d-serine is involved in induction of neuronal death by N-methyl-d-aspartate and simulated ischemia in rat cerebrocortical slices. J. Pharmacol. Exp. Ther. 311 (2004) 836-844
    • (2004) J. Pharmacol. Exp. Ther. , vol.311 , pp. 836-844
    • Katsuki, H.1
  • 84
    • 26844461474 scopus 로고    scopus 로고
    • d-serine is the dominant endogenous coagonist for NMDA receptor neurotoxicity in organotypic hippocampal slices
    • Shleper M., et al. d-serine is the dominant endogenous coagonist for NMDA receptor neurotoxicity in organotypic hippocampal slices. J. Neurosci. 25 (2005) 9413-9417
    • (2005) J. Neurosci. , vol.25 , pp. 9413-9417
    • Shleper, M.1
  • 85
    • 0037108758 scopus 로고    scopus 로고
    • Genetic and physiological data implicating the new human gene G72 and the gene for d-amino acid oxidase in schizophrenia
    • Chumakov I., et al. Genetic and physiological data implicating the new human gene G72 and the gene for d-amino acid oxidase in schizophrenia. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 13675-13680
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13675-13680
    • Chumakov, I.1
  • 86
    • 23644439204 scopus 로고    scopus 로고
    • Schizophrenia: genes at last?
    • Owen M.J., et al. Schizophrenia: genes at last?. Trends Genet. 21 (2005) 518-525
    • (2005) Trends Genet. , vol.21 , pp. 518-525
    • Owen, M.J.1
  • 87
    • 15844362335 scopus 로고    scopus 로고
    • Reduced glycine transporter type 1 expression leads to major changes in glutamatergic neurotransmission of CA1 hippocampal neurones in mice
    • Martina M., et al. Reduced glycine transporter type 1 expression leads to major changes in glutamatergic neurotransmission of CA1 hippocampal neurones in mice. J. Physiol. 563 (2005) 777-793
    • (2005) J. Physiol. , vol.563 , pp. 777-793
    • Martina, M.1
  • 88
    • 1642398017 scopus 로고    scopus 로고
    • N-Methyl-d-aspartate receptors: subunit assembly and trafficking to the synapse
    • Prybylowski K., and Wenthold R.J. N-Methyl-d-aspartate receptors: subunit assembly and trafficking to the synapse. J. Biol. Chem. 279 (2004) 9673-9676
    • (2004) J. Biol. Chem. , vol.279 , pp. 9673-9676
    • Prybylowski, K.1    Wenthold, R.J.2
  • 89
    • 0035369112 scopus 로고    scopus 로고
    • NMDA receptor subunits: diversity, development and disease
    • Cull-Candy S., et al. NMDA receptor subunits: diversity, development and disease. Curr. Opin. Neurobiol. 11 (2001) 327-335
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 327-335
    • Cull-Candy, S.1
  • 90
    • 0038606161 scopus 로고    scopus 로고
    • Structural model of the N-methyl-d-aspartate receptor glycine site probed by site-directed chemical coupling
    • Foucaud B., et al. Structural model of the N-methyl-d-aspartate receptor glycine site probed by site-directed chemical coupling. J. Biol. Chem. 278 (2003) 24011-24017
    • (2003) J. Biol. Chem. , vol.278 , pp. 24011-24017
    • Foucaud, B.1
  • 91
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core
    • Furukawa H., and Gouaux E. Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J. 22 (2003) 2873-2885
    • (2003) EMBO J. , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 92
    • 20444408992 scopus 로고    scopus 로고
    • Mechanism of partial agonist action at the NR1 subunit of NMDA receptors
    • Inanobe A., et al. Mechanism of partial agonist action at the NR1 subunit of NMDA receptors. Neuron 47 (2005) 71-84
    • (2005) Neuron , vol.47 , pp. 71-84
    • Inanobe, A.1
  • 93
    • 0032575065 scopus 로고    scopus 로고
    • Increased NMDA current and spine density in mice lacking the NMDA receptor subunit NR3A
    • Das S., et al. Increased NMDA current and spine density in mice lacking the NMDA receptor subunit NR3A. Nature 393 (1998) 377-381
    • (1998) Nature , vol.393 , pp. 377-381
    • Das, S.1
  • 94
    • 0023091647 scopus 로고
    • Glycine potentiates the NMDA response in cultured mouse brain neurons
    • Johnson J.W., and Ascher P. Glycine potentiates the NMDA response in cultured mouse brain neurons. Nature 325 (1987) 529-531
    • (1987) Nature , vol.325 , pp. 529-531
    • Johnson, J.W.1    Ascher, P.2
  • 95
    • 0023754192 scopus 로고
    • Requirement for glycine in activation of NMDA-receptors expressed in Xenopus oocytes
    • Kleckner N.W., and Dingledine R. Requirement for glycine in activation of NMDA-receptors expressed in Xenopus oocytes. Science 241 (1988) 835-837
    • (1988) Science , vol.241 , pp. 835-837
    • Kleckner, N.W.1    Dingledine, R.2
  • 96
    • 0027385331 scopus 로고
    • The developmental onset of NMDA receptor-channel activity during neuronal migration
    • Rossi D.J., and Slater N.T. The developmental onset of NMDA receptor-channel activity during neuronal migration. Neuropharmacology 32 (1993) 1239-1248
    • (1993) Neuropharmacology , vol.32 , pp. 1239-1248
    • Rossi, D.J.1    Slater, N.T.2


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