Comprehensive glycomics comparison between colon cancer cell cultures and tumours: Implications for biomarker studies

Chik, Jenny H. L.; Zhou, Jerry; Moh, Edward S. X.; Christopherson, Richard I.; Clarke, Stephen; Molloy, Mark P.; Packer, Nicolle H.

doi:10.1016/j.jprot.2014.05.002

Cited by 61 publications

(79 citation statements)

References 70 publications

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“…The presence of core 1-4 has been reported in gastric tissue (15,26,27). In this study, reducing end with sequence of Hex-HexNAcol and retention time (RT) shorter than 8 min on PGC column was assumed be to core 1 disaccharide, Hex-(HexNAc-)HexNAcol as core 2 trisaccharide, HexNAc-HexNAcol as core 3 and 5 disaccharides with core 3 having shorter RT on PGC column (28), and HexNAc-(HexNAc-)HexNAcol as core 4 trisaccharide.…”

Section: Methodsmentioning

confidence: 93%

“…by the genotype of the individual. The terminal structures of mucin oligosaccharides are heterogeneous and vary between/within species and even with tissue location within a single individual (12,15). Possibly, this structural diversity allows us to cope with diverse and rapidly changing pathogens, as reflected by the observation that susceptibility to specific pathogens differs between people with different histo-blood groups (16).…”

mentioning

confidence: 99%

“…Possibly, this structural diversity allows us to cope with diverse and rapidly changing pathogens, as reflected by the observation that susceptibility to specific pathogens differs between people with different histo-blood groups (16). Mucins appear to be the major carrier of aberrant glycosylation in carcinomas, and incomplete glycosylation, leading to expression of Tn and T antigens, and/or sialylation/sulfation are common (15,17). The sLe x and sLe a are frequently overexpressed in carcinomas, and expression of these antigens by epithelial carcinomas correlates with tumor progression, metastatic spread and poor prognosis (17).…”

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confidence: 99%

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Structural Diversity of Human Gastric Mucin Glycans

Jin

Kenny

Skoog

et al. 2017

Mol Cell Proteomics

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The mucin O-glycosylation of 10 individuals with and without gastric disease was examined in depth in order to generate a structural map of human gastric glycosylation. In the stomach, these mucins and their O-glycosylation protect the epithelial surface from the acidic gastric juice and provide the first point of interaction for pathogens such as Helicobacter pylori, reported to cause gastritis, gastric and duodenal ulcers and gastric cancer. The rational of the present study was to map the O-glycosylation that the pathogen may come in contact with. An enormous diversity in glycosylation was found, which varied both between individuals and within mucins from a single individual: mucin glycan chain length ranged from 2-13 residues, each individual carried 34 -103 O-glycan structures and in total over 258 structures were identified. The majority of gastric O-glycans were neutral and fucosylated. Blood group I antigens, as well as terminal ␣1,4-GlcNAc-like and GalNAc␤1-4GlcNAc-like (LacdiNAc-like), were common modifications of human gastric O-glycans. Gastric cancer is the second most common cause of cancer-associated death and fourth most commonly diagnosed cancer worldwide (1). Annually, 0.7 million patients with gastric cancer die globally (2). The cancer is associated with glycosylation changes, but how alteration of gastric mucins relates to gastric cancer pathogenesis remains unknown. Despite the protection by mucins and the acidic gastric juice and proteolytic enzymes, the bacterium Helicobacter pylori manage to thrive in the gastric lining, infecting about half of the world's population (3). There is a direct correlation between infection and gastric cancer, where 0.1-3% of infected individuals develop gastric adenocarcinoma or mucosa-associated lymphoid tissue lymphoma and another 10 -15% develop symptomatic gastritis or gastric and duodenal ulcers, whereas the majority show no symptoms (4).In the stomach, MUC5AC and MUC6 are the major secreted mucins, whereas MUC1 is the dominant membraneassociated mucin. MUC5AC is produced by the surface epithelium, whereas MUC6 is secreted from the deep glands of the gastric mucosa (5, 6). Both MUC5AC and MUC6 are large oligomeric mucins that occur as distinct glycoforms (7). In gastric precancerous lesions and cancer, altered expression of MUC5AC, MUC6, MUC2, and MUC5B has been described, with MUC2 being a marker for intestinal metaplasia (8, 9). The gastric surface and foveolar epithelium are formed by a single layer of tall columnar mucin-producing cells that have a basal nucleus below an apical cup of mucin. These cells have a turnover rate of 3-6 days, but the mucus layer produced in these cells have an even shorter life span: the production rate from start of glycosylation until release at the apical side is about 6 h (10), demonstrating that both the mucin repertoire and glycosylation theoretically can change rapidly. The carbohydrate structures present on mucosal surfaces vary according to cell lineage, tissue location, and developmental stage (11). The massive...

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Section: Methodsmentioning

confidence: 93%

mentioning

confidence: 99%

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confidence: 99%

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Structural Diversity of Human Gastric Mucin Glycans

Jin

Kenny

Skoog

et al. 2017

Mol Cell Proteomics

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“…19 It was observed that the membrane glycosylation of the cell lines differed from the glycosylation of the tumor cells, indicating that cell lines may not always provide biologically relevant glycosylation patterns. Therefore, further studies toward the characterization of differential glycosylation patterns of tumor tissue compared to non-malignant tissue are highly desirable.…”

Section: Introductionmentioning

confidence: 99%

Differential N-Glycosylation Patterns in Lung Adenocarcinoma Tissue

Ruhaak¹,

Taylor²,

Stroble

et al. 2015

J. Proteome Res.

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To decrease the mortality of lung cancer, better screening and diagnostic tools as well as treatment options are needed. Protein glycosylation is one of the major post-translational modifications that is altered in cancer, but it is not exactly clear which glycan structures are affected. A better understanding of the glycan structures that are differentially regulated in lung tumor tissue is highly desirable and will allow us to gain greater insight into the underlying biological mechanisms of aberrant glycosylation in lung cancer. Here, we assess differential glycosylation patterns of lung tumor tissue and nonmalignant tissue at the level of individual glycan structures using nLC–chip–TOF–MS. Using tissue samples from 42 lung adenocarcinoma patients, 29 differentially expressed (FDR < 0.05) glycan structures were identified. The levels of several oligomannose type glycans were upregulated in tumor tissue. Furthermore, levels of fully galactosylated glycans, some of which were of the hybrid type and mostly without fucose, were decreased in cancerous tissue, whereas levels of non- or low-galactosylated glycans mostly with fucose were increased. To further assess the regulation of the altered glycosylation, the glycomics data was compared to publicly available gene expression data from lung adenocarcinoma tissue compared to nonmalignant lung tissue. The results are consistent with the possibility that the observed N-glycan changes have their origin in differentially expressed glycosyltransferases. These results will be used as a starting point for the further development of clinical glycan applications in the fields of imaging, drug targeting, and biomarkers for lung cancer.

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“…The well known, previously reported, pan-carcinoma glycan markers in CCA tissues-sialyl-Tn (STn) antigen and sLea (Juntavee et al, 2005) -were not detected in the 5 CCA cell lines. The differential expression of O- glycans structures might have been regulated by many factors, including: mRNA turnover, the availability of substrate, nucleotide sugar transporter, and/or relevant glycosyltransferase (Chik et al, 2014). …”

Section: Discussionmentioning

confidence: 99%