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http://purl.uniprot.org/citations/34844667http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34844667http://www.w3.org/2000/01/rdf-schema#comment"Tumors frequently exhibit aberrant glycosylation, which can impact cancer progression and therapeutic responses. The hexosamine biosynthesis pathway (HBP) produces uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), a major substrate for glycosylation in the cell. Prior studies have identified the HBP as a promising therapeutic target in pancreatic ductal adenocarcinoma (PDA). The HBP requires both glucose and glutamine for its initiation. The PDA tumor microenvironment is nutrient poor, however, prompting us to investigate how nutrient limitation impacts hexosamine synthesis. Here, we identify that glutamine limitation in PDA cells suppresses de novo hexosamine synthesis but results in increased free GlcNAc abundance. GlcNAc salvage via N-acetylglucosamine kinase (NAGK) is engaged to feed UDP-GlcNAc pools. NAGK expression is elevated in human PDA, and NAGK deletion from PDA cells impairs tumor growth in mice. Together, these data identify an important role for NAGK-dependent hexosamine salvage in supporting PDA tumor growth."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.org/dc/terms/identifier"doi:10.7554/elife.62644"xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Campbell S."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Blenis J."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Blair I.A."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Noji M."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Sun K."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Mesaros C."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Wellen K.E."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Izzo L."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Schaffer B.E."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Tsang T."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Trefely S."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Affronti H."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/author"Kruijning S."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/pages"e62644"xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/title"Glutamine deprivation triggers NAGK-dependent hexosamine salvage."xsd:string
http://purl.uniprot.org/citations/34844667http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/34844667http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34844667
http://purl.uniprot.org/citations/34844667http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34844667
http://purl.uniprot.org/uniprot/#_A0A384N6G7-mappedCitation-34844667http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34844667
http://purl.uniprot.org/uniprot/#_C9JEV6-mappedCitation-34844667http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34844667