| First Author | Meguro H | Year | 1992 |
| Journal | Nature | Volume | 357 |
| Issue | 6373 | Pages | 70-4 |
| PubMed ID | 1374164 | Mgi Jnum | J:17924 |
| Mgi Id | MGI:65947 | Doi | 10.1038/357070a0 |
| Citation | Meguro H, et al. (1992) Functional characterization of a heteromeric NMDA receptor channel expressed from cloned cDNAs. Nature 357(6373):70-4 |
| abstractText | 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. |
