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PMID:1374164
| Citation |
Meguro, H, Mori, H, Araki, K, Kushiya, E, Kutsuwada, T, Yamazaki, M, Kumanishi, T, Arakawa, M, Sakimura, K and Mishina, M (1992) Functional characterization of a heteromeric NMDA receptor channel expressed from cloned cDNAs. Nature 357:70-4 |
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| Abstract |
The glutamate receptor (GluR) channel plays a key part in brain function. Among GluR channel subtypes, the NMDA (N-methyl-D-aspartate) receptor channel which is highly permeable to Ca2+ is essential for the synaptic plasticity underlying memory, learning and development. Furthermore, abnormal activation of the NMDA receptor channel may trigger the neuronal cell death observed in various brain disorders. A complementary DNA encoding a subunit of the rodent NMDA receptor channel (NMDAR1 or zeta 1) has been cloned and its functional properties investigated. Here we report the identification and primary structure of a novel mouse NMDA receptor channel subunit, designated as epsilon 1, after cloning and sequencing the cDNA. The epsilon 1 subunit shows 11-18% amino-acid sequence identity with rodent GluR channel subunits that have been characterized so far and has structural features common to neurotransmitter-gated ion channels. Expression from cloned cDNAs of the epsilon 1 subunit together with the zeta 1 subunit in Xenopus oocytes yields functional GluR channels with high activity and characteristics of the NMDA receptor channel. Furthermore, the heteromeric NMDA receptor channel can be activated by glycine alone. |
| Links |
PubMed Online version:10.1038/357070a0 |
| Keywords |
Amino Acid Sequence; Animals; Brain Chemistry; Cloning, Molecular; Glutamates; Ion Channels/chemistry; Ion Channels/physiology; Membrane Potentials/physiology; Mice; Molecular Sequence Data; Receptors, Glutamate; Receptors, N-Methyl-D-Aspartate/chemistry; Receptors, N-Methyl-D-Aspartate/physiology; Receptors, Neurotransmitter/physiology; Sequence Homology, Nucleic Acid |
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