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Jin C, Kenny DT, Skoog EC, Padra M, Adamczyk B, Vitizeva V, Thorell A, Venkatakrishnan V, Lindén SK, Karlsson NG
Mol. Cell Proteomics 16 (5) 743-758 [2017-05-00; online 2017-05-04]
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 α1,4-GlcNAc-like and GalNAcβ1-4GlcNAc-like (LacdiNAc-like), were common modifications of human gastric O-glycans. Furthemore, each individual carried 1-14 glycan structures that were unique for that individual. The diversity and alterations in gastric O-glycosylation broaden our understanding of the human gastric O-glycome and its implications for gastric cancer research and emphasize that the high individual variation makes it difficult to identify gastric cancer specific structures. However, despite the low number of individuals, we could verify a higher level of sialylation and sulfation on gastric O-glycans from cancerous tissue than from healthy stomachs.
Affinity Proteomics Uppsala [Service]
Glycoproteomics and MS Proteomics [Service]
PLA and Single Cell Proteomics [Service]
PubMed 28461410
DOI 10.1074/mcp.M116.067983
Crossref 10.1074/mcp.M116.067983
pii: 16/5/743
pmc: PMC5417818