Nitroxyl anion regulation of the NMDA receptor.


Journal Article

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; Na(2)N(2)O(3)) 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.

Full Text

Duke Authors

Cited Authors

  • Colton, CA; Gbadegesin, M; Wink, DA; Miranda, KM; Espey, MG; Vicini, S

Published Date

  • September 2001

Published In

Volume / Issue

  • 78 / 5

Start / End Page

  • 1126 - 1134

PubMed ID

  • 11553686

Pubmed Central ID

  • 11553686

International Standard Serial Number (ISSN)

  • 0022-3042


  • eng

Conference Location

  • England