Dataset Information

O-glycoproteomic datasets on the serum samples from patients with colorectal cancer

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: PXD035279 | JPOST Repository | Thu Jul 13 00:00:00 BST 2023

REPOSITORIES: jPOST

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Dataset's files

Source:

			Action	DRS
	Serum_CRC_Oglycopep_Patient1_NCE27.raw	Raw
	Serum_CRC_Oglycopep_Patient1_NCE27_Byonic.xlsx	Xlsx
	Serum_CRC_Oglycopep_Patient1_NCE35.raw	Raw
	Serum_CRC_Oglycopep_Patient1_NCE35_Byonic.xlsx	Xlsx
	Serum_CRC_Oglycopep_Patient2_NCE27.raw	Raw

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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:Changes in IgG glycosylation have been reported to be associated with colorectal cancer (CRC), but the alteration in specific subclass of IgG is unknown. Herein, we optimized five common IgG glycopeptides enrichment methods to acquire comprehensive profiling of IgG glycoproteomics in CRC. Notably, incomplete tryptic digestion of IgG occurred when using ordinary ratio of protease to protein, which significantly impacted the final statistical analysis of association between IgG glycosylation and CRC. We introduced a method based on two-step enzymatic digestion, enabling the complete digestion of IgG glycopeptides and further improving the detection intensity of the target glycopeptides. By this approach, total 47 IgG glycopeptides can be identified by nanoLC-ESI-MS/MS. Following rapid and automatic data processing through the self-developed program, we observed that IgG1_H3N4F1 and IgG1_H3N4 were substantially increased in CRC, while IgG1_H5N5F1, IgG1_H5N4F1S1and IgG2_H5N4F1 were markedly decreased. Strikingly, these four glycopeptides were continually significantly changed in early and late stages of CRC. Further evaluation of the diagnostic performance showed they all obtained a fair performance in discriminating the patients from the normal. In terms of the glycan features, it demonstrated that CRC progression associates with the increased agalactosylation, and the decreased digalactosylation and galactosylation per antenna on diantennay glycans of IgG1 and IgG2. Concurrently, the decreased sialylation of IgG1 was strongly correlated with CRC. Moreover, tumor-specific glycosylation analysis showed that the alterations of subclass-specific IgG glycosylation were more significant in colon cancer, and no obvious difference between colon and rectal cancer was found. More importantly, all these findings were validated in an independent cohort. This two-step enzymatic approach is crucial to explore the relationship between the disease progression and IgG glycosylation.