Direct inhibition of the N -methyl-D -aspartate receptor channel by dopamine and (+)-SKF38393
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چکیده
منابع مشابه
Combined Therapy for Anti-N-methyl D-aspartate Receptor Encephalitis
Background Anti-N-methyl- d-aspartate receptor (anti-NMDAR) encephalitis is an autoimmune neurological disorder that usually occurs as a paraneoplastic syndrome and is particularly associated with ovarian teratoma. Standard therapy for severe cases is not established and the prognosis in patients who do not respond to first-line treatment is poor. Case Report An 11-year-old boy complained ps...
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background: learning and memory are the most intensively studied subjects in neuroscience. two sites of mammalian brain which are important in learning and memory are ca1 region of hippocampus and purkinje cell layer of cerebellum. so, the aim of present investigation was to study of the effect of ovariectomy and passive avoidance learning on nr1 subunit of n-methyl-d-aspartate (nmda) receptor ...
متن کاملVoltage-dependent block of N-methyl-D-aspartate receptors by dopamine D1 receptor ligands.
Accumulating evidence indicates that dopamine and D1 receptor ligands modulate N-methyl D-aspartate (NMDA) receptors through a variety of D1 receptor-dependent mechanisms. In this study, we reveal a distinct D1 receptor-independent mechanism by which NMDA receptors are modulated. Using the human embryonic kidney (HEK) cell recombinant system and dissociated neurons, we have discovered that dopa...
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The compound 4-(5-(4-bromophenyl)-3-(6-methyl-2-oxo-4-phenyl-1,2-dihydroquinolin-3-yl)-4,5-dihydro-1H-pyrazol-1-yl)-4-oxobutanoic acid (DQP-1105) is a representative member of a new class of N-methyl-d-aspartate (NMDA) receptor antagonists. DQP-1105 inhibited GluN2C- and GluN2D-containing receptors with IC(50) values that were at least 50-fold lower than those for recombinant GluN2A-, GluN2B-, ...
متن کاملK+ Occupancy of the N-Methyl-d-Aspartate Receptor Channel Probed by Mg2+ Block
The single-channel kinetics of extracellular Mg(2+) block was used to probe K(+) binding sites in the permeation pathway of rat recombinant NR1/NR2B NMDA receptor channels. K(+) binds to three sites: two that are external and one that is internal to the site of Mg(2+) block. The internal site is approximately 0.84 through the electric field from the extracellular surface. The equilibrium dissoc...
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ژورنال
عنوان ژورنال: British Journal of Pharmacology
سال: 1999
ISSN: 0007-1188
DOI: 10.1038/sj.bjp.0702479