Dataset Information

S-nitrosoproteome of subsarcolemmal mitochondria and cytosolic subfractions from the heart of sedentary and exercise-trained rats.

ABSTRACT: This project is the study of S-nitrosylated proteins in SSM and cytosolic subfractions from heart of sedentary and exercise trained rats. Iodoacetyl Tandem Mass Tag (TMT) and TMT-peptide enrichment coupled with liquid chromatography-tandem mass spectrometry analysis have been used to analyze the modified cysteine residues. Comparisons were performed to reveal the impact of exercise training on protein S-nitrosylation.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Rattus Norvegicus (rat)

SUBMITTER: Jean ARMENGAUD

LAB HEAD: Jean Armengaud

PROVIDER: PXD023515 | Pride | 2022-04-23

REPOSITORIES: Pride

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Project description:Toxoplasma gondii transmitted via various route and rapidly duplicated during the acute infection, which caused the important zoonosis regarding to medicine and veterinary, toxoplasmosis. T. gondii possessed innate capability of producing nitric oxide (NO) and nitric oxide derivatives and S-nitrosylation not only participated in their signaling transduction, but also was a regulatory mechanism of protein post-translation. To date, S-nitrosylation proteome of T .gondii remains a mystery. In present study, we reported the first S-nitrosylated proteomic profile in T. gondii using mass spectrometry in combination with resin-assisted enrichment. 637 proteins were found to be S-nitrosylated and more than half of these S-nitrosylated proteins were localized in nucleus or cy-toplasm. Motif analysis identified seven motifs including five motifs containing lysine and two motif harboring isoleucine. GO enrichment revealed that S-nitrosylated proteins were mainly lo-cated in the mitochondrial inner membrane and organelle inner membrane in the cell. Those S-nitrosylated proteins were related with diverse biological and metabolic processes including or-ganic acid binding, carboxylic acid binding ribose and phosphate biosynthetic process. Glycoly-sis/gluconeogenesis and aminoacyl-tRNA biosynthesis were two remarkable pathways in which T. gondii S-nitrosylated proteins engaged. Twenty seven ribosomal proteins and eleven microneme proteins out of 22 secretory proteins were identified as S-nitrosylated proteins, which suggested that proteins in ribosome and microneme were S-nitrosylated with high proportion. PPI analysis identified three subnetworks with high relevancy ribosome, RNA transport and chaperonin com-plex component. These results implied that S-nitrosylated proteins in T. gondii were associated with protein translation in ribosome, gene transcription, invasion and proliferation of T. gondii. Our research firstly identified the S-nitrosylated proteomic profile of T. gondii and will provide a valuable resource for deep-going investigation of the functions of S-nitrosylation in T. gondii.

Project description:Human prion diseases are fatal neurodegenerative disorders characterized by neuronal damage in brain. Protein S-nitrosylation, the covalent adduction of a NO to cysteine, plays a role in human brain biology, and brain dysfunction is a prominent feature of pPrion disease, yet the direct brain targets of S-nitrosylation are largely unknown. We described the first proteomic analysis of global S-nitrosylation in brain tissues of sporadic Creutzfeldt–Jakob disease (sCJD), fatal familial insomnia (FFI) and genetic CJD with a substitution of valine for glycine at codon 114 of the prion protein gene (G114V gCJD) accompanying with normal control with isobaric tags for relative and absolute quantitation (iTRAQ) combined with a nano-HPLC/Q Exactive Mass spectrometry platform. In parallel, we used several approaches to provide quality control for the experimentally defined S-nitrosylated proteins. Total 1509 S-nitrosylated proteins (SNO-proteins) were identified, and cerebellum tissues appeared to contain more commonly differentially expressed SNO-proteins (DESPs) than cortex of sCJD, FFI and gCJD. Three selected SNO-proteins were verified by Western blots, consistent with proteomics assays. Gene ontology analysis showed that more up-regulated DESPs were involved in metabolism, cell cytoskeleton/structure and immune system both in cortex and cerebellum, while more down-regulated ones in both regions were involved in cell cytoskeleton/structure, cell-cell communication and miscelaneous function protein. Pathway analysis suggested that systemic lupus erythematosus, pathogenic Escherichia coli infection, extracellular matrix-receptor interaction were the most commonly affected pathways, which were identified from at least two different diseases. Using STRING database, the network of immune system and cell cytoskeleton and structure were commonly identified in the context of the up-regulated and down-regulated DESPs, respectively, both in cortex and cerebellum. Our study thus have implications for understanding the molecular mechanisms of human prion diseases related to abnormal protein S-nitrosylation and pave the way for future studies focused on potential biomarkers for the diagnosis and therapy of human prion diseases.

Dataset Information

S-nitrosoproteome of subsarcolemmal mitochondria and cytosolic subfractions from the heart of sedentary and exercise-trained rats.

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