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Titolo:
D-serine is an endogenous ligand for the glycine site of the N-methyl-D-aspartate receptor
Autore:
Mothet, JP; Parent, AT; Wolosker, H; Brady, RO; Linden, DJ; Ferris, CD; Rogawski, MA; Snyder, SH;
Indirizzi:
Johns Hopkins Univ, Sch Med, Dept Neurosci, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 urosci, Baltimore, MD 21205 USA Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205USA Johns Hopkins Univ Baltimore MD USA 21205 Mol Sci, Baltimore, MD 21205USA Johns Hopkins Univ, Sch Med, Dept Psychiat, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 ychiat, Baltimore, MD 21205 USA NINDS, Epilepsy Res Branch, NIH, Bethesda, MD 20892 USA NINDS Bethesda MDUSA 20892 lepsy Res Branch, NIH, Bethesda, MD 20892 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 9, volume: 97, anno: 2000,
pagine: 4926 - 4931
SICI:
0027-8424(20000425)97:9<4926:DIAELF>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
CULTURED HIPPOCAMPAL-NEURONS; AMINO-ACID OXIDASE; NMDA-RECEPTORS; RAT-BRAIN; EXTRACELLULAR CONCENTRATION; GLUTAMATE RECEPTORS; MAMMALIAN BRAIN; BINDING-SITE; NR1 SUBUNIT; ASTROCYTES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Snyder, SH Johns Hopkins Univ, Sch Med, Dept Neurosci, 725 N Wolfe St, Baltimore, MD 21205 USA Johns Hopkins Univ 725 N Wolfe St Baltimore MD USA 21205 05 USA
Citazione:
J.P. Mothet et al., "D-serine is an endogenous ligand for the glycine site of the N-methyl-D-aspartate receptor", P NAS US, 97(9), 2000, pp. 4926-4931

Abstract

Functional activity of N-methyl-D-aspartate (NMDA) receptors requires bothglutamate binding and the binding of an endogenous coagonist that has beenpresumed to be glycine, although D-serine is a more potent agonist, Localizations of D-serine and it biosynthetic enzyme serine racemase approximate the distribution of NMDA receptors more closely than glycine, We now show that selective degradation of D-serine with D-amino acid oxidase greatly attenuates NMDA receptor-mediated neurotransmission as assessed by using whole-cell patch-clamp recordings or indirectly by using biochemical assays of the sequelae of NMDA receptor-mediated calcium flux. The inhibitory effects of the enzyme are fully reversed by exogenously applied D-serine, which by itself did not potentiate NMDA receptor-mediated synaptic responses. Thus, D-serine is an endogenous modulator of the glycine site of NMDA receptors and fully occupies this site at some functional synapses.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/10/20 alle ore 04:12:33