Linked Life Data

11292060

Source:http://linkedlifedata.com/resource/pubmed/id/11292060

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pubmed-article:11292060pubmed:abstractTextNMDA receptors are glutamate-regulated ion channels of critical importance for many neurophysiological and neuropathological processes. Mg2+ blocks the NMDA receptor by binding to the channel pore with an apparent affinity that depends on the membrane potential. We have investigated the effect of NMDA and the required co-agonist glycine on the affinity of the Mg2+ block site in NR1-1a/NR2A NMDA receptors expressed in Xenopus oocytes. We found that NMDA and glycine increase the IC50 value of the Mg2+-block site at pH 7.4 and in the presence of physiological concentration of Ca2+. The increase the IC50 value may correspond to a decrease in Mg2+-block affinity. This effect may result in an increased influx of Ca2+, and this influx may constitute up to a third of the total Ca2+ influx induced by NMDA. At high pH, or at low concentrations of Ca2+, NMDA and glycine have an opposite effect and instead decreased the IC50 value of the Mg2+-block. These results indicate that glutamate and glycine can regulate the affinity of the Mg2+-block site. This effect may have implications for the understanding the role of NMDA receptors both under physiological and pathophysiological conditions.lld:pubmed
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pubmed-article:11292060pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:11292060pubmed:articleTitleNMDA and glycine regulate the affinity of the Mg2+-block site in NR1-1a/NR2A NMDA receptor channels expressed in Xenopus oocytes.lld:pubmed
pubmed-article:11292060pubmed:affiliationDepartment of Neuroscience, Karolinska Institutet, Stockholm, Sweden.lld:pubmed
pubmed-article:11292060pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11292060pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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