PubMed:1420598 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/1420598","sourcedb":"PubMed","sourceid":"1420598","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/1420598","text":"Glycosylation of the interleukin-1 receptor type I is required for optimal binding of interleukin-1.\nThe two types of cell surface receptors for interleukin-1 (IL-1) are glycoproteins that contain N-glycosidic chains on their extracellular portions. To determine the role of glycosylation of the IL-1 receptor type I (IL-1RtI) in the binding and function of IL-1, we used four plant lectins and glycosidase treatment on two different T-cell lines (EL4-6.1 and D10S) and expressing high number of binding sites for IL-1. The lectins wheat germ agglutinin, phytohemagglutinin, and concanavalin A inhibited in a dose-response manner the IL-1-induced proliferation of D10S cells. Binding of IL-1 was blocked and radioactive IL-1 was displaced from these cells by these lectins. Specific sugars (GlcNAc, NeuAc, Gal-GlcNAc-Man, Man, or alpha-MeMan) did not themselves affect IL-1 binding but reversed the blocking effects of the lectins. The two cell lines differed in their responses to the lectin-mediated inhibition of IL-1 binding. Digestion by N-glycosidase significantly decreased the capacity of cells to bind IL-1, and reduced by approximately 20,000 D the M(r) of the IL-1RtI. Neuraminidase and O-glycanase treatment did not alter the binding of IL-1 to D10S or EL4-6.1 cells. This study demonstrates that glycosylation of the extracellular domain of the IL-1RtI is due to N-linked carbohydrates, that the degree of glycosylation can vary in cells of different lineage, and that this N-linked glycosylation appears to be essential for optimal binding and activity of IL-1 to its type I receptor.","tracks":[{"project":"bionlp-st-epi-2011-training","denotations":[{"id":"T1","span":{"begin":21,"end":50},"obj":"Protein"},{"id":"T2","span":{"begin":296,"end":316},"obj":"Protein"},{"id":"T3","span":{"begin":318,"end":325},"obj":"Protein"},{"id":"T4","span":{"begin":579,"end":593},"obj":"Protein"},{"id":"T5","span":{"begin":1171,"end":1178},"obj":"Protein"},{"id":"T6","span":{"begin":1358,"end":1365},"obj":"Protein"}],"attributes":[{"subj":"T1","pred":"source","obj":"bionlp-st-epi-2011-training"},{"subj":"T2","pred":"source","obj":"bionlp-st-epi-2011-training"},{"subj":"T3","pred":"source","obj":"bionlp-st-epi-2011-training"},{"subj":"T4","pred":"source","obj":"bionlp-st-epi-2011-training"},{"subj":"T5","pred":"source","obj":"bionlp-st-epi-2011-training"},{"subj":"T6","pred":"source","obj":"bionlp-st-epi-2011-training"}]},{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":791,"end":797},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":810,"end":816},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"attributes":[{"subj":"PD-NGLY1-deficiency-B_T1","pred":"source","obj":"NGLY1-deficiency"},{"subj":"PD-NGLY1-deficiency-B_T2","pred":"source","obj":"NGLY1-deficiency"}]},{"project":"ngly1-sample1","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":791,"end":797},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":810,"end":816},"obj":"chem:24139"}],"attributes":[{"subj":"PD-NGLY1-deficiency-B_T1","pred":"source","obj":"ngly1-sample1"},{"subj":"PD-NGLY1-deficiency-B_T2","pred":"source","obj":"ngly1-sample1"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"bionlp-st-epi-2011-training","color":"#bd93ec","default":true},{"id":"NGLY1-deficiency","color":"#93eca3"},{"id":"ngly1-sample1","color":"#ec939d"}]}]}}