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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

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			Action	DRS
	AnnotatedspectraofPANC-1.rar	Other
	AnnotatedspectraofPDAC.rar	Other
	Descriptionofrawdata.docx	Other
	HJL_C1-C8_MaxQuantoutputfiles.zip	Other
	HJL_C1_20181026.index	Other

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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

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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.

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