A glycoproteomic approach to identify novel glycomarkers for cancer stem cells

Sawanobori, Atsuko; Moriwaki, Kazuo; Takamatsu, Shinji; Kamada, Y.; Miyoshi, Eiji

doi:10.1002/pmic.201500472

Cited by 6 publications

(3 citation statements)

References 62 publications

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“…On the other side, a general increase of fucosylation was also reported in colorectal cancer, as suggested by the binding of Aleuria aurantia lectin [89], that preferentially recognizes fucose α1,2/3/6 linked to lactosamine units [90]. Increased fucosylation levels were also reported in cancer stem cells of the pancreas and associated to chemoresistance in pancreatic cell lines [91]. …”

Section: Regulation Of Slea and Slexmentioning

confidence: 99%

Selectin Ligands Sialyl-Lewis a and Sialyl-Lewis x in Gastrointestinal Cancers

Trinchera

Aronica

Dall’Olio

2017

Biology

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The tetrasaccharide structures Siaα2,3Galβ1,3(Fucα1,4)GlcNAc and Siaα2,3Galβ1,4(Fucα1,3)GlcNAc constitute the epitopes of the carbohydrate antigens sialyl-Lewis a (sLea) and sialyl-Lewis x (sLex), respectively, and are the minimal requirement for selectin binding to their counter-receptors. Interaction of sLex expressed on the cell surface of leucocytes with E-selectin on endothelial cells allows their arrest and promotes their extravasation. Similarly, the rolling of cancer cells ectopically expressing the selectin ligands on endothelial cells is potentially a crucial step favoring the metastatic process. In this review, we focus on the biosynthetic steps giving rise to selectin ligand expression in cell lines and native tissues of gastrointestinal origin, trying to understand whether and how they are deregulated in cancer. We also discuss the use of such molecules in the diagnosis of gastrointestinal cancers, particularly in light of recent data questioning the ability of colon cancers to express sLea and the possible use of circulating sLex in the early detection of pancreatic cancer. Finally, we reviewed the data dealing with the mechanisms that link selectin ligand expression in gastrointestinal cells to cancer malignancy. This promising research field seems to require additional data on native patient tissues to reach more definitive conclusions.

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Section: Regulation Of Slea and Slexmentioning

confidence: 99%

Selectin Ligands Sialyl-Lewis a and Sialyl-Lewis x in Gastrointestinal Cancers

Trinchera

Aronica

Dall’Olio

2017

Biology

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“…The development of LC-MS/MS techniques in glycoproteomics makes it more widely used for studying the pathogenesis of several different diseases including cancer − and neurological diseases . In addition, glycoproteomics research can now be conducted on various types of biological samples such as blood, − urine, cell lines, − and other tissues. , Many of these studies focus on the biomarker discovery for a specific disease by quantifying glycopeptides and determining glycosite occupancies. − Other studies expand the glycoproteome with regard to unique organisms .…”

Section: Ms Methods For Glycoproteomicsmentioning

confidence: 99%

Mass Spectrometry Approaches to Glycomic and Glycoproteomic Analyses

et al. 2018

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Glycomic and glycoproteomic analyses involve the characterization of oligosaccharides (glycans) conjugated to proteins. Glycans are produced through a complicated nontemplate driven process involving the competition of enzymes that extend the nascent chain. The large diversity of structures, the variations in polarity of the individual saccharide residues, and the poor ionization efficiencies of glycans all conspire to make the analysis arguably much more difficult than any other biopolymer. Furthermore, the large number of glycoforms associated with a specific protein site makes it more difficult to characterize than any post-translational modification. Nonetheless, there have been significant progress, and advanced separation and mass spectrometry methods have been at its center and the main reason for the progress. While glycomic and glycoproteomic analyses are still typically available only through highly specialized laboratories, new software and workflow is making it more accessible. This review focuses on the role of mass spectrometry and separation methods in advancing glycomic and glycoproteomic analyses. It describes the current state of the field and progress toward making it more available to the larger scientific community.

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“…Increased fucosylation has been linked to development and progression of prostate cancer [22] and certain subpopulations of pancreatic cancer cells [23]. On the contrary, fucosylation deficiency led to adenocarcinoma in mice [24], and decreased core-fucosylation has been shown to be clinically associated with malignancy of gastric cancer [25].…”

Section: Introductionmentioning

confidence: 99%

Marine Lectins DlFBL and HddSBL Fused with Soluble Coxsackie-Adenovirus Receptor Facilitate Adenovirus Infection in Cancer Cells BUT Have Different Effects on Cell Survival

Mei

Cui

et al. 2017

Marine Drugs

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Cancer development and progression are usually associated with glycosylation change, providing prognostic and diagnostic biomarkers, as well as therapeutic targets, for various cancers. In this work, Dicentrarchus labrax fucose binding lectin (DlFBL) and Haliotis discus discus sialic acid binding lectin (HddSBL) were genetically fused with soluble coxsackie-adenovirus receptor (sCAR), and produced through a bacterial expression system. Results showed that recombinant sCAR-DlFBL not only facilitated adenovirus Ad-EGFP infection in K562/ADR and U87MG cells, but also enhanced the cytotoxicity of adenovirus harboring gene encoding Pinellia pedatisecta agglutinin (PPA) or DlFBL (Ad-PPA or Ad-DlFBL) on U87MG cells through inducing apoptosis. Recombinant sCAR-HddSBL facilitated Ad-EGFP infection, but dramatically counteracted the cytotoxicity of both Ad-PPA and Ad-DlFBL in U87MG cells. Further analysis revealed that sCAR-HddSBL, but not sCAR-DlFBL, significantly upregulated transcription factor E2F1 levels in U87MG cells, which might be responsible for the adverse effect of sCAR-HddSBL on Ad-PPA and Ad-DlFBL. Taken together, our data suggested that sCAR-DlFBL could be further developed to redirect therapeutic adenoviruses to infect cancer cells such as U87MG, and the sCAR-lectin fusion proteins for adenoviral retargeting should be carefully examined for possible survival signaling induced by lectins, such as HddSBL.

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A glycoproteomic approach to identify novel glycomarkers for cancer stem cells

Cited by 6 publications

References 62 publications

Selectin Ligands Sialyl-Lewis a and Sialyl-Lewis x in Gastrointestinal Cancers

Selectin Ligands Sialyl-Lewis a and Sialyl-Lewis x in Gastrointestinal Cancers

Mass Spectrometry Approaches to Glycomic and Glycoproteomic Analyses

Marine Lectins DlFBL and HddSBL Fused with Soluble Coxsackie-Adenovirus Receptor Facilitate Adenovirus Infection in Cancer Cells BUT Have Different Effects on Cell Survival

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