Cloning of cDNA for the glutamate-binding subunit of an NMDA receptor complex

• Published in: Nature (London) Vol. 354; no. 6348; pp. 70 - 73
• Main Authors: Kumar Tilakaratne, Keshava N. Nanda, Johnson, Peter S, Alien, Annette E, Michaelis, Elias K
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 07.11.1991
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Brain - metabolism; Cloning, Molecular; Fundamental and applied biological sciences. Psychology; genes; Genes. Genome; Glutamates - metabolism; glutamic acid; Ion Channels; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; N-methyl-d-aspartic acid; Rats; Receptors, Glutamate; Receptors, N-Methyl-D-Aspartate - genetics; Receptors, Neurotransmitter - genetics; Rat; Nucleotide sequence; Synaptic membrane; Rodentia; Tissue specificity; Glutamate receptor; Binding site; Gene expression; Glutamate; Subunit; Vertebrata; Mammalia; Complementary DNA; Molecular cloning; NMDA receptor; Brain (vertebrata)
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/354070a0

The amino acids L-glutamic and L-aspartic acids form the most widespread excitatory transmitter network in mammalian brain. The excitation produced by L-glutamic acid is important in the early development of the nervous system, synaptic plasticity and memory formation, seizures and neuronal degeneration. The receptors activated by L-glutamic acid are a target for therapeutic intervention in neurodegenerative diseases, brain ischaemia and epilepsy. There are two types of receptors for the excitatory amino acids, those that lead to the opening of cation-selective channels and those that activate phospholipase C (ref. 11). The receptors activating ion channels are NMDA (N-methyl-D-aspartate) and kainate/AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate)-sensitive receptors. The complementary DNAs for the kainate/AMPA receptor and for the metabotropic receptor have been cloned. We report here on the isolation and characterization of a protein complex of four major proteins that represents an intact complex of the NMDA receptor ion channel and on the cloning of the cDNA for one of the subunits of this receptor complex, the glutamate-binding protein.