Proteomics

Dataset Information

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Peroxynitrite-mediated post-translational modification of human glutamine synthetase

ABSTRACT: The aim of the project was to understand the mechanisms that underlie the oxidative inactivation of human glutamine synthetase (HsGS). For that purpose, we expressed and purified recombinant HsGS, exposed it in phosphate buffer to peroxynitrite (ONOO-) and assessed the functional and structural consequences. To characterize the oxidative post-translational modifications induced by ONOO-, several approaches were carried out (e.g. SDS-PAGE, western-blot, amino acid quantification by LC, etc). The most detailed characterization was performed through LC-MS/MS analysis after trypsin digestion of the ONOO--treated protein, which allowed us to identify the amino acid residues that are modified and to estimate the extent of such modifications.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Nicolás Campolo  

LAB HEAD: Rafael Radi

PROVIDER: PXD037583 | Pride | 2023-05-10

REPOSITORIES: Pride

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20180928_FS_MM_GSONOOH1.raw Raw
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20180928_FS_MM_GSONOOH2.raw Raw
20180928_FS_MM_GSONOOH2I.raw Raw
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Publications

Multiple oxidative post-translational modifications of human glutamine synthetase mediate peroxynitrite-dependent enzyme inactivation and aggregation.

Campolo Nicolás N   Mastrogiovanni Mauricio M   Mariotti Michele M   Issoglio Federico M FM   Estrin Darío D   Hägglund Per P   Grune Tilman T   Davies Michael J MJ   Bartesaghi Silvina S   Radi Rafael R  

The Journal of biological chemistry 20230123 3

Glutamine synthetase (GS), which catalyzes the ATP-dependent synthesis of L-glutamine from L-glutamate and ammonia, is a ubiquitous and conserved enzyme that plays a pivotal role in nitrogen metabolism across all life domains. In vertebrates, GS is highly expressed in astrocytes, where its activity sustains the glutamate-glutamine cycle at glutamatergic synapses and is thus essential for maintaining brain homeostasis. In fact, decreased GS levels or activity have been associated with neurodegene  ...[more]

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