Neuroscience 2002 Abstract
| Presentation Number: | 640.3 |
|---|---|
| Abstract Title: | EVIDENCE FOR AN INTERACTION BETWEEN N-TERMINAL REDOX SENSITIVE CYSTEINES AND A POLYAMINE MODULATORY SITE OF THE NR1/NR2A NMDA RECEPTOR. |
| Authors: |
Herin, G. A.*1
; Zheng, F.2
; Le, P.2
; Aizenman, E.1
1Neurobiology, University of Pittsburgh School of Medicine, Pittsburgh, PA 2Pharmacology, Emory University School of Medicine, Atlanta, GA |
| Primary Theme and Topics |
Synaptic Transmission and Excitability - Ligand Gated Ion Channels -- Glutamate receptors: NMDA receptors |
| Session: |
640. Ligand gated ion channels: glutamate receptors--NMDA receptors: receptor pharmacology Poster |
| Presentation Time: | Wednesday, November 6, 2002 10:00 AM-11:00 AM |
| Location: | Hall A2-B3 C-87 |
| Keywords: | spermine, DTT, GLUTAMATE RECEPTOR |
The NMDA subtype of glutamate receptor is sensitive to reducing and oxidizing agents in a subtype specific-manner. Cysteines 744 and 798 on NR1a are responsible for most of the redox sensitivity of NR1a/NR2B and NR1a/NR2C receptors. However, NR1a(c744a/c798a)/NR2A receptors remain sensitive to redox modulation. This has been attributed to cysteines in the amino terminal domain (ATD) of NR1 and NR2A (Choi et al., J. Neurosci. 21:392;2001). We have previously shown that 30uM spermine blocks the effects of DTT in NR1a(c744a,c798a)/NR2A receptors (Herin et al., SFN Abstracts 703.12; 2001), in a tricine-insensitive manner. This suggests a zinc-independent effect of spermine on redox modulation at the N-terminal redox-sensitive cysteines. Evidence exists that spermine alone modulates NR1a/NR2B (but not NR1a/NR2A) receptors via the N-terminal regulatory domain of NR1a. We hypothesized that spermine block of DTT potentiation in NR1a(c744a/c798a)/NR2A could be modified by alterations of the ATD of NR1a. Mutation of cys79 in NR1a(c744a/c798a)/NR2A receptors resulted in a decrease of DTT potentiation of NMDA-induced currents, as reported earlier (Choi et al., ibid.). In support of our hypothesis, the inhibitory actions of spermine on DTT potentiation were markedly attenuated in this construct. These results suggest an interaction between cys79 of NR1a and a spermine modulatory site in NR1a/NR2A receptors.
Supported by NIH NS29365 (EA), Charitable Leadership Foundation (EA), and NIH NS39418 (FZ)
Sample Citation:
[Authors]. [Abstract Title]. Program No. XXX.XX. 2002 Neuroscience Meeting Planner. Orlando, FL: Society for Neuroscience, 2002. Online.
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