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Literature DB >> 7524561

Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor.

J M Sullivan¹, S F Traynelis, H S Chen, W Escobar, S F Heinemann, S A Lipton.

Abstract

Modulation of NMDA-mediated responses by oxidizing and reducing reagents has been described in a variety of neuronal preparations. Here, we report that NMDA-gated currents of oocytes expressing heteromeric NMDA receptors are also modulated by sulfhydryl redox reagents. Each cysteine residue in the NMDAR1 (NR1) subunit and each conserved NMDAR2 (NR2) cysteine residue in a prototypical subunit (NR2B) was tested for its role in redox modulation. We have identified 2 cysteines in the NR1 subunit that are required for redox modulation of NMDA-gated currents in oocytes expressing NR1-NR2B, NR1-NR2C, or NR1-NR2D receptors. Mutation of these same 2 cysteines also eliminated potentiation by spermine and shifted the IC50 for H+ inhibition and the EC50 for NMDA. Redox modulation of heteromeric NR1-NR2A receptors appeared to be different from that of the other heteromeric receptors, indicating the presence of one or more unique redox modulatory sites on NR1-NR2A receptors.

Entities: Chemical Gene

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Year: 1994 PMID： 7524561 DOI： 10.1016/0896-6273(94)90258-5

Source DB: PubMed Journal: Neuron ISSN： 0896-6273 Impact factor: 17.173

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Cited

66 in total

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Authors: P Paoletti; P Ascher; J Neyton
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2. Modulation of neuronal and recombinant GABAA receptors by redox reagents.

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Journal: J Physiol Date: 1999-05-15 Impact factor: 5.182

3. Redox modulation of basal and beta-adrenergically stimulated cardiac L-type Ca(2+) channel activity by phenylarsine oxide.

Authors: Carl Sims; Robert D Harvey
Journal: Br J Pharmacol Date: 2004-06-01 Impact factor: 8.739

10. The Inhibition of TREK2 Channel by an Oxidizing Agent, 5,5'-dithio-bis (2-nitrobenzoic acid), via Interaction with the C-terminus Distal to the 353rd Amino Acid.

Authors: Kyoung Sun Park; Hyoweon Bang; Eun-Young Shin; Chan Hyung Kim; Yangmi Kim
Journal: Korean J Physiol Pharmacol Date: 2008-08-31 Impact factor: 2.016

Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor.

1. High-affinity zinc inhibition of NMDA NR1-NR2A receptors.

2. Modulation of neuronal and recombinant GABAA receptors by redox reagents.

3. Redox modulation of basal and beta-adrenergically stimulated cardiac L-type Ca(2+) channel activity by phenylarsine oxide.

4. GluN1-specific redox effects on the kinetic mechanism of NMDA receptor activation.

Review 5. Glutamate receptor ion channels: structure, regulation, and function.

6. Novel role for the NMDA receptor redox modulatory site in the pathophysiology of seizures.

7. Reducing agents sensitize C-type nociceptors by relieving high-affinity zinc inhibition of T-type calcium channels.

8. Modulation of the dimer interface at ionotropic glutamate-like receptor delta2 by D-serine and extracellular calcium.

9. Neuronal growth on L- and D-cysteine self-assembled monolayers reveals neuronal chiral sensitivity.

10. The Inhibition of TREK2 Channel by an Oxidizing Agent, 5,5'-dithio-bis (2-nitrobenzoic acid), via Interaction with the C-terminus Distal to the 353rd Amino Acid.