Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 57, Issue 11, Pages 1535-1541Publisher
SPRINGER BASEL AG
DOI: 10.1007/PL00000638
Keywords
NMDA receptor; redox; DTT; nitric oxide; S-nitrosylation; cysteine
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Funding
- NEI NIH HHS [R01 EY09024, R01 EY05477] Funding Source: Medline
- NICHD NIH HHS [P01 HD29587] Funding Source: Medline
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Redox modulation has been recognized to be an important mechanism of regulation for the N-methyl-D-aspartate (NMDA) receptor. Sulfhydryl reducing agents enhance, whereas oxidizing agents decrease, NMDA-evoked currents. Multiple cysteine residues located in different NMDA receptor subunits have been identified as molecular determinants underlying redox modulation. The NMDA receptor is also regulated by nitric oxide (NO)-related species directly, not involving cyclic GMP, but the molecular mechanism of this action has heretofore not been entirely clear. The confusion arose at least partly due to the fact that various redox forms of NO (NO+, NO., NO-, each having an additional electron compared with the previous) have distinct mechanisms of action. Recently, a critical cysteine residue (Cys 399) on the NR2A subunit has been shown to react under physiological conditions with NO by S-nitrosylation (transfer of the NO+ to cysteine thiol) or by reaction with NO- (nitroxyl anion) to underlie this form of modulation.
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