PXD002813

PXD002813 is an original dataset announced via ProteomeXchange.

Title	Human prion disease iTRAQ
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.
HostingRepository	PRIDE
AnnounceDate	2015-10-01
AnnouncementXML	Submission_2015-10-01_00:24:40.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Xiaoping Dong
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iTRAQ8plex-116 reporter+balance reagent acylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2015-08-28 03:32:18	ID requested
⏵ 1	2015-10-01 00:24:42	announced

Chen LN, Shi Q, Zhang BY, Zhang XM, Wang J, Xiao K, Lv Y, Sun J, Yang XD, Chen C, Zhou W, Han J, Dong XP, Proteomic Analyses for the Global S-Nitrosylated Proteins in the Brain Tissues of Different Human Prion Diseases. Mol Neurobiol, 53(8):5079-96(2016) [pubmed]

curator keyword: Biomedical

submitter keyword: Human prion diseases, S-nitrosylation, proteomic analysis, isobaric tags for relative and absolute quantitation

Xiaoping Dong
contact affiliation	State Key Laboratory for Infectious Disease Prevention and Control, Prion disease department, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing, People’s Republic of China
contact email	dongxp238@sina.com
lab head
Xiaoping Dong
contact affiliation	Chinese center for disease control and prevention
contact email	dongxp238@sina.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD002813
     1. Label: PRIDE project
     2. Name: Human prion disease iTRAQ