Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

S-nitrosoproteome of pancreatic ductal adenocarcinoma

ABSTRACT: NO performs its biological roles mainly through protein S-nitrosylation, but pathogenic roles of protein S-nitrosylation in PDAC remains largely unexplored. In this study, we identified large number of unique S-nitrosylation sites and proteins in PDAC patients and PANC-1 cells by a site-specific proteomics.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Pancreas

SUBMITTER: Jiliang Hu

LAB HEAD: Jiliang Hu

PROVIDER: PXD012512 | Pride | 2020-05-26

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Publications

Extensive protein S-nitrosylation associated with human pancreatic ductal adenocarcinoma pathogenesis.

Tan Chaochao C Li Yunfeng Y Huang Xiahe X Wei Meijin M Huang Ying Y Tang Zhouqin Z Huang He H Zhou Wen W Wang Yingchun Y Hu Jiliang J

Cell death & disease 20191204 12

NO (nitric oxide)-mediated protein S-nitrosylation has been established as one major signaling mechanism underlying cancer initiation and development, but its roles in PDAC (pancreatic ductal adenocarcinoma) pathogenesis still remain largely unexplored. In this study, we identified 585 unique S-nitrosylation sites among 434 proteins in PDAC patients and PANC-1 cell line by a site-specific proteomics. Larger number of S-nitrosylated proteins were identified in PDAC tissues and PANC-1 cells than a ...[more]

PMID: 31801946

Similar Datasets

Adaptation of CysPAT technique to characterize endogenous S-nitrosylation in RAW264.7 cells

Project description:The aim of the study was to adapt the CysPAT technique to efficiently identify and characterize endogenous S-nitrosylation in cells under physiological conditions of an experiment from a small amount of sample. Using a macrophage cell line RAW 264.7 we compared the efficacy of the method in the identification of total endogenous S-nitrosylation and the corresponding modification of the samples treated with exogenous SNO donor (GSNO) or with DTT. We identified 999 unique formerly S-nitrosylated peptides (SIA peptides) and 965 unique SNO sites from untreated RAW cells which belong to 569 endogenous nitrosylated proteins. We discovered 579 novel S-nitrosylation sites and identified 232 proteins as new S-nitrosylation targets. A total of 1450 S-nitrosylated peptides belonging to 795 proteins were identified in samples treated with GSNO (n = 3). Interestingly, we found a large overlap (>53%) of S-nitrosylated peptides in both subsets of samples, demonstrating a high sensitivity of the method to analyze endogenous S-nitrosylation. The large number of identified endogenous S-nitrosylated peptides allowed the identification of two nitrosylation consensus sites, and to highlight protein translation and redox processes as key S-nitrosylation targets in macrophages.

2022-02-22 | PXD008182 | Pride

Stress-induced changes in the S-palmitoylation and S-nitrosylation of proteins involved in synaptic plasticity

Project description:Summary The precise regulation of synaptic integrity is critical for neuronal network connectivity and proper brain function. Essential aspects of the activity and localization of synaptic proteins are regulated by posttranslational modifications. S-palmitoylation is a reversible covalent modification of the cysteine with palmitate. It modulates affinity of the protein for cell membranes and membranous compartments. Intracellular palmitoylation dynamics are regulated by other posttranslational modifications, such as S-nitrosylation. Still unclear, however, are the ways in which this crosstalk is affected in brain pathology, such as stress-related disorders. Using a newly developed mass spectrometry-based approach (Palmitoylation And Nitrosylation Interplay Monitoring), we analyzed the endogenous S-palmitoylation and S-nitrosylation of postsynaptic density proteins at the level of specific single cysteines in a mouse model of chronic stress. Our results suggest that atypical mechanism of crosstalk between the S-palmitoylation and S-nitrosylation of synaptic proteins might be one of the major events associated with chronic stress disorders.

2019-07-16 | PXD010822 | Pride

Proteomic analysis of S-nitrosylated nuclear proteins in rat cortical neurons

Project description:S-nitrosothiol Resin Assisted Capture(SNORAC) coupled with mass spectrometry analysis has been used to study S-nitrosylated proteins in rat cortical neurons. Proteins were captured on the resin by covalently attaching their former S-NO moiety. Then, nistrosylated proteins were eluted by on-bead digestion. Formerly S-nitrosylated peptides were also eluted from the beads in a second step, and analyzed separately for assessment of the nitrosylation site (qualitative analysis). Out of over 600 nitrosyltated proteins, 131 proteins have never been shown to be S-nitrosylated in any system and 612 are new targets of S-nitrosylation in cortical neurons. The site(s) of Snitrosylation were also identified for 59% of the targets.

2018-07-11 | PXD009071 | Pride

Cysteine nitrosylation analysis in SH-SY5Y cells

Project description:Cysteine nitrosylation is emerging as important player in cellular signaling and redox homeostasis. Here we applied Cys-BOOST for quantitative analysis of nitrosylated cysteine in SNAP-treated and non-treated SH-SY5Y human neuroblastoma cells.

2019-05-21 | PXD012485 | Pride

A protein microarray-based analysis of S-nitrosylation

Project description:Yeast protein microarrays were utilized to investigate determinants of S-nitrosylation by biologically relevant low-mass S-nitrosothiols (SNOs). Large numbers of S-nitrosylated yeast proteins were identified after treatment with SNOs, among which those with active-site Cys thiols residing at N termini of alpha-helices or within catalytic loops were particularly prominent. However, S-nitrosylation varied substantially even within these families of proteins (e.g., papain-related Cys-dependent hydrolases and rhodanese/Cdc25 phosphatases), suggesting that neither secondary structure nor intrinsic nucleophilicity of Cys thiols was sufficient to explain specificity. Further analyses revealed a substantial influence of NO-donor stereochemistry and structure on efficiency of S-nitrosylation as well as an unanticipated and important role for allosteric effectors. Thus, high-throughput screening and unbiased proteome coverage reveal multifactorial determinants of S-nitrosylation (which may be overlooked in alternative proteomic analyses), and support the idea that target specificity can be achieved through rational design of S-nitrosothiols Invitrogen yeast Protoarrays for kinase substrate identification (KSI) were treated with S-nitrosothiols and assayed for protein S-nitrosylation by using a modified biotin switch protocol. Slides were scanned and with a Genepix 4000b scanner (Molecular Devices) using Genepix Pro and analyzed by using Prospector Analyzer (Invitrogen). Results were validated using yeast cell lysates and recombinant, purified yeast proteins.

2010-05-19 | E-GEOD-19218 | biostudies-arrayexpress

S-Nitrosylation of the Virulence Regulator AphB Promotes Vibrio cholerae Pathogenesis

Project description:S-Nitrosylation of the Virulence Regulator AphB Promotes Vibrio cholerae Pathogenesis

2022-05-31 | PXD031615 | Pride

Nitric oxide synthase-dependent SNOome identification

Project description:This study aimed to identify proteins whose S-nitrosylation is mediated by each of the three human NOS isoforms.

2023-06-01 | PXD040633 | Pride

Microarray expression profile analysis of circular RNAs in human pancreatic ductal adenocarcinoma

Project description:To explore the potential involvement of circular RNAs (circRNAs) in pancreatic ductal adenocarcinoma (PDAC) oncogenesis, we conducted circRNA profiling in six pairs of human PDAC and adjacent normal tissue by microarray. Our results showed that clusters of circRNAs were aberrantly expressed in PDAC compared with normal samples, and provided potential targets for future treatment of PDAC and novel insights into PDAC biology. Analyze circular RNA expression in pancreatic ductal adenocarcinoma (PDAC) by microarray platform.

2015-11-20 | E-GEOD-69362 | biostudies-arrayexpress

microRNA profiling by array of paired samples tumor tissue/normal adjacent tissue from colon cancer patients

Project description:Ten arrays were performed on the RNA extracts from 10 patients' samples, each of them contained the paired samples tumor tissue/ normal adjacent tissue.

2018-01-17 | E-MTAB-5443 | biostudies-arrayexpress

FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions

Project description:Reversible protein S-nitrosylation regulates a wide range of biological functions and physiological activities in plants. However, it is challenging to quantitively determine the S-nitrosylation targets and dynamics in vivo. In this study, we developed a highly sensitive and efficient fluorous affinity tag-switch (FAT-switch) chemical proteomics approach for S-nitrosylation peptide enrichment and detection. We quantitatively compared the global S-nitrosylation profiles in wild-type Arabidopsis and gsnor1/hot5/par2 mutant using this approach, and identifyied 2,121 S-nitrosylation peptides in 1,595 protein groups, including many previously unrevealed S-nitrosylated proteins. These are 408 S-nitrosylated sites in 360 protein groups showing an accumulation in hot5-4 mutant when compared to wild type. Biochemical and genetic validation revealed that S-nitrosylation at Cys337 in ER OXIDOREDUCTASE 1 (ERO1) causes the rearrangement of disulfide, resulting in enhanced ERO1 activity. This study offersed a powerful and applicable tool for S-nitrosylation research, which provides valuable resources for studies on S-nitrosylation-regulated ER functions in plants.

2023-06-07 | PXD037504 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data