Structural Diversity of Human Gastric Mucin Glycans.

Autor:	Jin C; From the ‡Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Box 440, Medicinaregatan 9A, 405 30 Gothenburg, Sweden., Kenny DT; From the ‡Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Box 440, Medicinaregatan 9A, 405 30 Gothenburg, Sweden., Skoog EC; From the ‡Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Box 440, Medicinaregatan 9A, 405 30 Gothenburg, Sweden., Padra M; From the ‡Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Box 440, Medicinaregatan 9A, 405 30 Gothenburg, Sweden., Adamczyk B; From the ‡Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Box 440, Medicinaregatan 9A, 405 30 Gothenburg, Sweden., Vitizeva V; From the ‡Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Box 440, Medicinaregatan 9A, 405 30 Gothenburg, Sweden., Thorell A; §Karolinska Institute, Department for Clinical Science and Department of Surgery, Ersta Hospital, Stockholm, Sweden., Venkatakrishnan V; From the ‡Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Box 440, Medicinaregatan 9A, 405 30 Gothenburg, Sweden., Lindén SK; From the ‡Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Box 440, Medicinaregatan 9A, 405 30 Gothenburg, Sweden., Karlsson NG; From the ‡Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Box 440, Medicinaregatan 9A, 405 30 Gothenburg, Sweden; niclas.karlsson@medkem.gu.se.
Jazyk:	angličtina
Zdroj:	Molecular & cellular proteomics : MCP [Mol Cell Proteomics] 2017 May; Vol. 16 (5), pp. 743-758.
DOI:	10.1074/mcp.M116.067983
Abstrakt:	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.)
Databáze:	MEDLINE
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