Glycomic Profiling Highlights Increased Fucosylation in Pseudomyxoma Peritonei.

{"sci_version": "1.2", "schema": "https://corpus.bntrg.co.uk/sci/1.0/sci.schema.json", "id": "pmid:30072579", "kind": "science-record", "revision": 2, "content_hash": "sha256:139db4c962eca8b0d3cf27a0a2c90b8bd8fdad98c1bc525aeaae249c67aac1af", "created_at": "2026-11-01T15:40:36Z", "updated_at": "2026-11-01T18:49:43Z", "generator": {"name": "corpus-assay-engine", "run_id": "reading-sci-2026-11-01"}, "paper": {"state": "complete", "title": "Glycomic Profiling Highlights Increased Fucosylation in Pseudomyxoma Peritonei.", "doi": "10.1074/mcp.RA118.000615", "pmid": "30072579", "authors": ["Lilli Saarinen", "Pirjo Nummela", "Hannele Leinonen", "Annamari Heiskanen", "Alexandra Thiel", "Caj Haglund", "Anna Lepistö", "Tero Satomaa", "Sampsa Hautaniemi", "Ari Ristimäki"], "journal": "Molecular & cellular proteomics : MCP", "year": 2018, "abstract": "Pseudomyxoma peritonei (PMP) is a subtype of mucinous adenocarcinoma that most often originates from the appendix, and grows in the peritoneal cavity filling it with mucinous ascites. KRAS and GNAS mutations are frequently found in PMP, but other common driver mutations are infrequent. As altered glycosylation can promote carcinogenesis, we compared N-linked glycan profiles of PMP tissues to those of normal appendix. Glycan profiles of eight normal appendix samples and eight low-grade and eight high-grade PMP specimens were analyzed by mass spectrometry. Our results show differences in glycan profiles between PMP and the controls, especially in those of neutral glycans, and the most prominent alteration was increased fucosylation. We further demonstrate up-regulated mRNA expression of four fucosylation-related enzymes, the core fucosylation performing fucosyltransferase 8 and three GDP-fucose biosynthetic enzymes in PMP tissues when compared with the controls. Up-regulated protein expression of the latter three enzymes was further observed in PMP cells by immunohistochemistry. We also demonstrate that restoration of fucosylation either by salvage pathway or by introduction of an expression of intact GDP-mannose 4,6-dehydratase enhance expression of MUC2, which is the predominant mucin molecule secreted by the PMP cells, in an intestinal-derived adenocarcinoma cell line with defective fucosylation because of deletion in the GDP-mannose 4,6-dehydratase gene. Thus, altered glycosylation especially in the form of fucosylation is linked to the characteristic mucin production of PMP. Glycomic data are available via ProteomeXchange with identifier PXD010086.", "claims": [{"id": "claim-target-result", "statement": "The paper found that altered glycosylation, especially increased fucosylation, is linked to the characteristic mucin production of PMP; glycan profiles were analyzed by mass spectrometry, and the glycomic data are available through ProteomeXchange (PXD010086). No numerical result for the statistical method is stated in the provided text.", "kind": "qualitative", "target": null, "evidence": [{"asset": "source:pmid:30072579", "locator": "sections[0] \"Abstract\" paragraph 1", "quote": "Thus, altered glycosylation especially in the form of fucosylation is linked to the characteristic mucin production of PMP."}, {"asset": "source:pmid:30072579", "locator": "sections[0] \"Abstract\" paragraph 1", "quote": "Glycan profiles of eight normal appendix samples and eight low-grade and eight high-grade PMP specimens were analyzed by mass spectrometry."}, {"asset": "source:pmid:30072579", "locator": "sections[0] \"Abstract\" paragraph 1", "quote": "Glycomic data are available via ProteomeXchange with identifier PXD010086."}], "state": "complete"}], "gaps": []}, "experiment": {"state": "partial", "objective": "The paper found that altered glycosylation, especially increased fucosylation, is linked to the characteristic mucin production of PMP; glycan profiles were analyzed by mass spectrometry, and the glycomic data are available through ProteomeXchange (PXD010086). 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