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http://purl.uniprot.org/citations/32460355http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32460355http://www.w3.org/2000/01/rdf-schema#comment"As an immune checkpoint, programmed cell death 1 (PD-1) and its ligand (PD-L1) pathway plays a crucial role in CD8+ cytotoxic T lymphocytes (CTL) activation and provides antitumor responses. The N-glycans of PD-1 and PD-L1 are highly core fucosylated, which are solely catalyzed by the core fucosyltransferase (Fut8). However, the precise biological mechanisms underlying effects of core fucosylation of PD-1 and PD-L1 on CTL activation have not been fully understood. In this study, we found that core fucosylation was significantly upregulated in lung adenocarcinoma. Compared to those of Fut8+/+ OT-I mice, the lung adenocarcinoma formation induced by urethane was markedly reduced in Fut8-/- OT-I mice. De-core fucosylation of PD-1 compromised its expression on Fut8-/- CTL, resulted in enhanced Fut8-/- CTL activation and cytotoxicity, leading to more efficient tumor eradication. Indeed, loss of core fucosylation significantly enhanced the PD-1 ubiquitination and in turn led to the degradation of PD-1 in the proteasome. Our current work indicates that inhibition of core fucosylation is a unique strategy to reduce PD-1 expression for the antilung adenocarcinoma immune therapy in the future."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.org/dc/terms/identifier"doi:10.1002/eji.202048543"xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Gu J."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Liu Y."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Fukuda T."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Li M."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Li W."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Zhao M."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Xu X."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Zhang N."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/author"Jin X."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/name"Eur J Immunol"xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/pages"1820-1833"xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/title"Loss of core fucosylation enhances the anticancer activity of cytotoxic T lymphocytes by increasing PD-1 degradation."xsd:string
http://purl.uniprot.org/citations/32460355http://purl.uniprot.org/core/volume"50"xsd:string
http://purl.uniprot.org/citations/32460355http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32460355
http://purl.uniprot.org/citations/32460355http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/32460355
http://purl.uniprot.org/uniprot/#_A0A0M3M0G7-mappedCitation-32460355http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32460355
http://purl.uniprot.org/uniprot/#_B2X2D7-mappedCitation-32460355http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32460355
http://purl.uniprot.org/uniprot/#_B2X2D8-mappedCitation-32460355http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32460355