Analysis of site and structure specific core fucosylation in liver disease ID
Ontology highlight
ABSTRACT:
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: Miloslav Sanda
PROVIDER: PXD028610 | JPOST Repository | Sat Sep 17 00:00:00 BST 2022
REPOSITORIES: jPOST
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| MS_07_PSMS_GP_IDs.xlsx | Xlsx | |||
| MS_07_corefuco01_Neu_H1.raw | Raw | |||
| MS_07_corefuco02_Neu_H2.raw | Raw | |||
| MS_07_corefuco03_Neu_C1.raw | Raw | |||
| MS_07_corefuco04_Neu_C2.raw | Raw |
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Project description:Overexpression of fucosyltransferase 8 (FUT8) is found in many cancers including liver, ovarian, thyroid, colorectal and non-small cell lung cancers. Unlike other FUTs which are functionally redundant, FUT8 is the only enzyme responsible for the alpha1,6-linked fucosylation (core fucosylation) by adding fucose to the innermost GlcNAc residue of an N-linked glycan. A growing body of evidence indicates that core fucosylation is important for regulating protein functions, such as EGFR, TGF beta receptor and integrins. To understand the downstream molecular events in response to the global alteration of core fucosylation during cancer progression, microarray analysis was employed to profile the changes in gene expression following FUT8 silencing. The genes significantly (2-fold, P<0.01) changed in CL1-5/shFUT8 cells were selected for functional annotations using a Gene Ontology database. The result revealed that many genes involved in cell adhesion, motility, growth, angiogenesis, and inflammation were under the control of core fucosylation. In this experiment, the gene expression profile of two stable FUT8 knockdown clones of CL1-5 cells, CL1-5/shFUT8-1 and CL1-5/shFUT8-2, were compare with CL1-5/Control cells. A total of eight samples were analyzed, including four CL1-5/Control vs. CL1-5/shFUT8-1 and four CL1-5/Control vs. C1-5/shFUT8-2. The biological replicates for each cell lines were four.
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Project description:Core fucosylation, the attachment of α1,6-fucose to the innermost GlcNAc residue of N-glycans, is a unique protein glycosylation in living organisms. It plays significant roles in diverse physiological and pathological processes, and its upregulation has been observed in many cancers. Core fucosylation has a strong relationship with tumor growth, inva-sion, metastasis, prognosis, and immune evasion. Yet, the details are still largely unknown due to the lack of an effec-tive analytical method. Here, a site-specific and reversible labeling strategy for rapid and sensitive probing core fucosyla-tion was developed. Taking the newly developed strategy, core-fucosylated proteins located on the cell-surface were selectively labeled and analyzed. The profile of cell-surface glycoproteins provides an in-depth understanding of the biological functions of core fucosylation.
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