Structural Diversity of Human Gastric Mucin Glycans - PubMed (original) (raw)
. 2017 May;16(5):743-758.
doi: 10.1074/mcp.M116.067983.
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- PMID: 28461410
- DOI: 10.1074/mcp.M116.067983
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Structural Diversity of Human Gastric Mucin Glycans
Chunsheng Jin et al. Mol Cell Proteomics. 2017 May.
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Abstract
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.
© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.
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