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Regulation of brain glutamate metabolism by nitric oxide and S-nitrosylation
Journal article   Peer reviewed

Regulation of brain glutamate metabolism by nitric oxide and S-nitrosylation

Karthik Raju, Paschalis-Thomas Doulias, Perry Evans, Elizabeth N. Krizman, Joshua G. Jackson, Oksana Horyn, Yevgeny Daikhin, Ilana Nissim, Marc Yudkoff, Itzhak Nissim, …
Science signaling, v 8(384), pp ra68-ra68
07 Jul 2015
PMID: 26152695
url
https://doi.org/10.1126/scisignal.aaa4312View
Published, Version of Record (VoR) Restricted

Abstract

Biochemistry & Molecular Biology Cell Biology Life Sciences & Biomedicine Science & Technology
Nitric oxide (NO) is a signaling intermediate during glutamatergic neurotransmission in the central nervous system (CNS). NO signaling is in part accomplished through cysteine S-nitrosylation, a posttranslational modification by which NO regulates protein function and signaling. In our investigation of the protein targets and functional impact of S-nitrosylation in the CNS under physiological conditions, we identified 269 S-nitrosocysteine residues in 136 proteins in the wild-type mouse brain. The number of sites was significantly reduced in the brains of mice lacking endothelial nitric oxide synthase (eNOS(-/-)) or neuronal nitric oxide synthase (nNOS(-/-)). In particular, nNOS(-/-) animals showed decreased S-nitrosylation of proteins that participate in the glutamate/glutamine cycle, a metabolic process by which synaptic glutamate is recycled or oxidized to provide energy. N-15-glutamine-based metabolomic profiling and enzymatic activity assays indicated that brain extracts from nNOS(-/-) mice converted less glutamate to glutamine and oxidized more glutamate than those from mice of the other genotypes. GLT1 [also known as EAAT2 (excitatory amino acid transporter 2)], a glutamate transporter in astrocytes, was S-nitrosylated at Cys(373) and Cys(561) in wild-type and eNOS-/- mice, but not in nNOS-/- mice. A form of rat GLT1 that could not be S-nitrosylated at the equivalent sites had increased glutamate uptake compared to wild-type GLT1 in cells exposed to an S-nitrosylating agent. Thus, NO modulates glutamatergic neurotransmission through the selective, nNOS-dependent S-nitrosylation of proteins that govern glutamate transport and metabolism.

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Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
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