期刊
JOURNAL OF NEUROCHEMISTRY
卷 78, 期 5, 页码 1126-1134出版社
BLACKWELL SCIENCE LTD
DOI: 10.1046/j.1471-4159.2001.00509.x
关键词
Angeli's salt; glycine independent desensitization; hypoxia; nitroxyl anion; N-methyl-D-aspartate
资金
- NIA NIH HHS [R03 AG16026] Funding Source: Medline
- NIMH NIH HHS [KO2MH01680, R01MH58946] Funding Source: Medline
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.
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