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HETEROMERIC NMDA RECEPTORS - MOLECULAR AND FUNCTIONAL DISTINCTION OF SUBTYPES
Author(s): MONYER H, SPRENGEL R, SCHOEPFER R, HERB A, HIGUCHI M, LOMELI H, BURNASHEV N, SAKMANN B, SEEBURG PH
Source: SCIENCE    Volume: 256    Issue: 5060    Pages: 1217-1221    Published: MAY 22 1992  
Times Cited: 1,795     References: 54     
Abstract: The N-methyl D-aspartate (NMDA) receptor subtype of glutamate-gated ion channels possesses high calcium permeability and unique voltage-dependent sensitivity to magnesium and is modulated by glycine. Molecular cloning identified three complementary DNA species of rat brain, encoding NMDA receptor subunits NMDAR2A (NR2A), NR2B, and NR2C, which are 55 to 70% identical in sequence. These are structurally related, with less than 20% sequence identity to other excitatory amino acid receptor subunits, including the NMDA receptor subunit NMDAR1 (NR1). Upon expression in cultured cells, the new subunits yielded prominent, typical glutamate- and NMDA-activated currents only when they were in heteromeric configurations with NR1. NR1-NR2A and NR1-NR2C channels differed in gating behavior and magnesium sensitivity. Such heteromeric NMDA receptor subtypes may exist in neurons, since NR1 messenger RNA is synthesized throughout the mature rat brain, while NR2 messenger RNA show a differential distribution.
Document Type: Article
Language: English
Addresses:
1. UNIV HEIDELBERG, CTR MOLEC BIOL, NEUENHEIMER FELD 282, W-6900 HEIDELBERG, GERMANY
2. MAX PLANCK INST MED RES, W-6900 HEIDELBERG 1, GERMANY
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005
Subject Category: Multidisciplinary Sciences
IDS Number: HV192
ISSN: 0036-8075
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