Nitroxyl anion regulation of the NMDA receptor

C. A. Colton, M. Gbadegesin, D. A. Wink, K. M. Miranda, M. G. Espey, S. Vicini

Research output: Contribution to journalArticle

41 Scopus citations

Abstract

Nitric oxide (NO) is an important regulator of NMDA channel function in the CNS. Recent findings suggest that nitroxyl anion (NO-) may also be generated by nitric oxide synthase, which catalyzes production of NO. Using recombinant NMDA receptors (NMDA-r) transfected into human embryonic kidney cells, our data demonstrate that the nitroxyl anion donor, Angeli's salt (AS; Na2N2O3) dramatically blocked glycine-independent desensitization in NMDA-r containing NR1-NR2A subunits. AS did not affect glycine-dependent desensitization, calcium dependent inactivation or glutamate affinity for the NMDA-r. This effect could be mimicked by treatment with DPTA, a metal chelator and was not evident under hypoxic conditions. In contrast, receptors containing the NR1-NR2B subunits demonstrated an approximate 25% reduction in whole cell currents in the presence of AS with no apparent change in desensitization. Our data suggest that the regulation of NMDA-r function by nitroxyl anion is distinctly different from NO and may result in different cellular outcomes compared with NO.

Original languageEnglish (US)
Pages (from-to)1126-1134
Number of pages9
JournalJournal of neurochemistry
Volume78
Issue number5
DOIs
StatePublished - Sep 17 2001
Externally publishedYes

Keywords

  • Angeli's salt
  • Glycine independent desensitization
  • Hypoxia
  • N-methyl-D-aspartate
  • Nitroxyl anion

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Fingerprint Dive into the research topics of 'Nitroxyl anion regulation of the NMDA receptor'. Together they form a unique fingerprint.

  • Cite this

    Colton, C. A., Gbadegesin, M., Wink, D. A., Miranda, K. M., Espey, M. G., & Vicini, S. (2001). Nitroxyl anion regulation of the NMDA receptor. Journal of neurochemistry, 78(5), 1126-1134. https://doi.org/10.1046/j.1471-4159.2001.00509.x