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Analysis of site and structure specific core fucosylation in liver disease

ABSTRACT: Analysis of site and structure specific core fucosylation in liver disease progression using exoglycosidase-assisted data-independent LC-MS/MS

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Miloslav Sanda

PROVIDER: PXD020678 | JPOST Repository | Sun Aug 01 00:00:00 BST 2021

REPOSITORIES: jPOST

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			Action	DRS
	DataMS%2070%20corefuco%20SWATH_BV1_Fn.wiff	Wiff
	DataMS%2070%20corefuco%20SWATH_BV1_Fn.wiff.scan	Wiff
	DataMS%2070%20corefuco%20SWATH_BV1_Fn_2.wiff	Wiff
	DataMS%2070%20corefuco%20SWATH_BV1_Fn_2.wiff.scan	Wiff
	DataMS%2070%20corefuco%20SWATH_BV2_Fn.wiff	Wiff

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Analysis of site and structure specific core fucosylation in liver disease ID

Project description:Analysis of site and structure specific core fucosylation in liver disease progression using exoglycosidase-assisted data-independent LC-MS/MS

2022-09-17 | PXD028610 | JPOST Repository

A “Two birds One Stone” Strategy for Site-specific Analysis of the Core Fucosylation and O-GlcNAcylation

Project description:Core fucosylation and O-GlcNAcylation are two most famous protein glycosylations and regulate diverse physiological and pathological processes in living organism. Core fucosylation is a protein glycosylation in which a L-fucose residue attaches to the innermost N-acetylglucosamine (GlcNAc) of N-glycan through α1, 6 linkage. O-GlcNAcylation is a dy-namic protein glycosylation where D-GlcNAc moieties attaches to serine or threonine residues of proteins. Here, a “two-birds one stone” strategy is described for site-specific analysis of the core fucosylation and O-GlcNAcylation. The de-scribed strategy allows the simultaneously profiling of core-fucosylated glycoproteome and O-GlcNAcylated glycoprote-ome from one complex sample.

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Aberrant L-Fucose accumulation and increased core fucosylation are specific metabolic liabilities in mesenchymal glioblastoma

Project description:Dysregulated metabolism in glioblastoma (GBM), the deadliest brain tumor of adults, offers an opportunity to deploy metabolic interventions as precise therapeutic strategies. To identify the molecular drivers and the modalities by which different molecular subgroups of GBM exploit metabolic rewiring to sustain tumor progression, we interrogated the transcriptome, the metabolome and the glycoproteome of human subgroup-specific GBM stem cells (GSCs). Here we report that L-Fucose abundance and core fucosylation activation are more highly enhanced in mesenchymal (MES) than in proneural (PN) GSCs; this pattern is retained in subgroup-specific xenografts and, most significantly, retrieved in subgroup-affiliated human patients’ samples. Genetic and pharmacological inhibition of core fucosylation in MES GBM preclinical models results in significant reduction in tumor burden. LC/MS-based glycoproteomic screening indicates that most MES-restricted core fucosylated proteins are involved in therapeutically relevant GBM pathological processes, such as extracellular matrix interaction, cell adhesion and integrin-mediated signaling. Notably, selective L-Fucose accumulation in MES GBMs is demonstrated by pre-clinical minimally-invasive positron emission tomography (PET), implying this metabolite as a potential subgroup-restricted biomarker. Overall, these findings indicate that L-Fucose pathway activation in MES GBM offers subgroup-specific, GSC-restricted dependencies to be exploited as diagnostic markers and actionable therapeutic targets.

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Analysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent LC-MS/MS.

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