Dataset Information

O-glycoproteomic datasets on the serum samples from healthy individuals

ABSTRACT: Clinical O-glycoproteomics for the development of diagnostic marker for colorectal cancer based on changes in O-glycosylation of serum protein.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Daisuke Takakura

PROVIDER: PXD035280 | JPOST Repository | Thu Jul 13 00:00:00 BST 2023

REPOSITORIES: jPOST

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Publications

Targeted O-glycoproteomics for the development of diagnostic markers for advanced colorectal cancer.

Takakura Daisuke D Ohashi Shoko S Kobayashi Noritoshi N Tokuhisa Motohiko M Ichikawa Yasushi Y Kawasaki Nana N

Frontiers in oncology 20230209

Aberrant glycosylation is a prominent feature of cancer, that can be used as targets to improve the existing cancer biomarkers, and help to assess metastasis risks, and therapeutic effects. We developed a targeted O-glycoproteomics method using serum specimens, and evaluated its utility in identifying advanced colorectal cancer (CRC) markers. To this end, we combined consecutive lectin affinity purification using <i>Maclura pomifera</i> lectin (MPL), jacalin, and <i>Sambucus nigra</i> lectin, wh ...[more]

PMID: 36845686

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Project description:Colorectal cancer, one of the most frequent types of malignancy in the Western world, develops through a multi-step process. The main pathways establishing transformation of normal mucosa to invasive carcinoma include chromosomal instability (CIN), microsatellite instability (MSI) or epigenetic silencing through the CpG Island Methylator Phenotype (CIMP). These pathways have distinct clinical, pathological and genetic characteristics. In general, altered cell surface glycosylation has been linked to colorectal cancer progression, however the impact of MSI-specific pathways on the glycosylation machinery of MSI colon cancer cells has not been investigated yet. In a recent study (Patsos et al., 2009) we have shown that MSI-specific mutations induce marked alterations in cell surface glycosylation, indicating specific changes in the expression of glyco-genes. Therefore the purpose of our experiment is to define these changes by glyco-gene chip analysis. Biallelic mutational inactivation of MSI target genes is believed to drive MSI tumorigenesis. TGFBR2, ACVR2 and AIM2 are among the most frequently mutated genes in MSI colorectal adenomas and carcinomas and functional studies indicate their contribution to MSI-carcinogenesis. A first general screening approach by lectin FACS analysis indicated a correlation between functional inactivation of these genes and cell surface glycosylation of the MSI colon cell line HCT116 (Patsos et al., 2009). For detailed analysis of the altered glycosylation pattern and the underlying molecular mechanisms we have established HCT116 double stable transfectants that allow doxycycline-inducible expression of the three MSI target genes TGFBR2, ACVR2 and AIM2 in a reversible manner. Thus we can experimentally control the expression of the MSI-genes and analyze short and long-term effects on different cell functions, including glycosylation. From the application of the glyco-gene chip for analysis of the transfectants we expect to gain seminal information on the influence of MSI-target genes on glycan expression and function in MSI tumor cells. Correlating loss-of-function of MSI target genes not yet linked with glycosylation to the regulation of the glycophenotype is a novel approach to investigate the glycobiology of tumor cells. In addition it is also suitable to detect new MSI-(glyco)markers for clinical applications, including diagnostic tumor markers and specific targets for immunotherapies.

Dataset Information

O-glycoproteomic datasets on the serum samples from healthy individuals

Publications

Targeted O-glycoproteomics for the development of diagnostic markers for advanced colorectal cancer.

Similar Datasets

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