Dataset Information

Human Intestinal biopsy tissue LC-MS

ABSTRACT: This is the first report of proteomic analysis for the identification of novel drug targets based on intestinal biopsy tissue, which is significant to hypotheses for mechanistic investigation that are responsible for non-response to IFX and the development of clinical new pharmaceutical drugs. All 12 UC patients were divided into responders to IFX (UCinfG), non-responders to IFX (UCinfL), severe UC (UCsevere) without IFX treatment history and mild UC (UCmild) without IFX treatment history.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Colon

SUBMITTER: lu liu

LAB HEAD: lu liu

PROVIDER: PXD030121 | Pride | 2022-08-12

REPOSITORIES: Pride

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Publications

Proteomic Analysis of Potential Targets for Non-Response to Infliximab in Patients With Ulcerative Colitis.

Liu Lu L Pu Dan D Wang Dandan D Zhang Muhan M Zhou Chuan C Zhang Zhe Z Feng Baisui B

Frontiers in pharmacology 20220613

<b>Background:</b> Infliximab (IFX) is a potent therapeutic agent used for the treatment of conventional refractory ulcerative colitis (UC). However, the high non-response rate of IFX brings difficulties to clinical applications. In the context of proteomics research, our study of differentially expressed proteins (DEPs) is essential for non-response to IFX in UC patients and provides powerful insights into underlying drug resistance mechanisms. <b>Methods:</b> A total of 12 UC patients were div ...[more]

PMID: 35770079

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Project description:Cystic echinococcosis (CE) is a chronic zoonosis caused by infection with the larval stage(protoscoleces, PSCs) of the cestode Echinococcus granulosus. A unique characteristic of the PSC is an ability to develop bidirectionally into an adult worm in the definitive host or into a secondary hydatid cyst in the intermediate host. Furmore, the cestode has a complex life-cycle involving different development stages but the mechanisms underpinning this development. Many studies have demonstrated that some matrix proteins undergo posttranslational modifications, including phosphorylation and glycosylation, which have important regulatory effects on the functional properties of the proteins. Systematic analysis of the proteome, the phosphorylated modified proteome and the glycosylated modified proteome of the PSCs and adult worms was performed using a proteomics strategy. A total of 6407 phosphorylation sites and 1757 proteins were quantifiable. Of those, 2032 phosphorylation sites and 770 proteins were up-regulated, and 2993 phosphorylation sites and 1217 proteins were down-regulated in the PSCs compared with the adult worms. A total of 612 N-glycosylation sites within 392 N-glycoproteins were identified. Of which, 355 N-glycosylation sites and 212 N-glycoproteins were quantifiable. Of those, 90 N-glycosylation sites and 64 N-glycoproteins were up-regulated, and 171 N-glycosylation sites and 126 N-glycoproteins were down-regulated 6407 in the PSCs compared with the adult worms. GO enrichment analysis indicated that the differently expressed phosphoproteins were mainly enriched in regulation of oxidoreduction coenzyme metabolic process, myelin sheath and RNA helicase activity, while the differently expressed N-glycoproteins were enriched in the cellular response to unfolded protein, endoplasmic reticulum lumen and nucleic acid binding. KEGG enrichment analysis indicated that the differently expressed phosphoproteins were mainly enriched in RNA transport, Hypertrophic cardiomyopathy (HCM), Glycolysis/Gluconeogenesis, HIF-1 signaling pathway and Pyruvate metabolism. while the differently expressed N-glycoproteins were enriched in PI3K-Akt signaling pathway, ECM-receptor interaction and Protein processing in endoplasmic reticulum.

Dataset Information

Human Intestinal biopsy tissue LC-MS

Publications

Proteomic Analysis of Potential Targets for Non-Response to Infliximab in Patients With Ulcerative Colitis.

Similar Datasets

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