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2017 ; 16
(5
): 743-758
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Structural Diversity of Human Gastric Mucin Glycans
#MMPMID28461410
Jin C
; Kenny DT
; Skoog EC
; Padra M
; Adamczyk B
; Vitizeva V
; Thorell A
; Venkatakrishnan V
; Lindén SK
; Karlsson NG
Mol Cell Proteomics
2017[May]; 16
(5
): 743-758
PMID28461410
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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. 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.
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