{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Loke I"],"funding":["Cancer Institute NSW"],"pagination":["1507-1527"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5546201"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(8)"],"pubmed_abstract":["Human neutrophil elastase (HNE) is an important <i>N</i>-glycosylated serine protease in the innate immune system, but the structure and immune-modulating functions of HNE <i>N</i>-glycosylation remain undescribed. Herein, LC-MS/MS-based glycan, glycopeptide and glycoprotein profiling were utilized to first determine the heterogeneous <i>N</i>-glycosylation of HNE purified from neutrophil lysates and then from isolated neutrophil granules of healthy individuals. The spatiotemporal expression of HNE during neutrophil activation and the biological importance of its <i>N</i>-glycosylation were also investigated using immunoblotting, cell surface capture, native MS, receptor interaction, protease inhibition, and bacteria growth assays. Site-specific HNE glycoprofiling demonstrated that unusual"],"journal":["Molecular & cellular proteomics : MCP"],"pubmed_title":["Paucimannose-Rich <i>N</i>-glycosylation of Spatiotemporally Regulated Human Neutrophil Elastase Modulates Its Immune Functions."],"pmcid":["PMC5546201"],"funding_grant_id":["13/ECF/1–02"],"pubmed_authors":["Packer NH","Ostergaard O","Heegaard NHH","Loke I","Thaysen-Andersen M"],"additional_accession":[]},"is_claimable":false,"name":"Paucimannose-Rich <i>N</i>-glycosylation of Spatiotemporally Regulated Human Neutrophil Elastase Modulates Its Immune Functions.","description":"Human neutrophil elastase (HNE) is an important <i>N</i>-glycosylated serine protease in the innate immune system, but the structure and immune-modulating functions of HNE <i>N</i>-glycosylation remain undescribed. Herein, LC-MS/MS-based glycan, glycopeptide and glycoprotein profiling were utilized to first determine the heterogeneous <i>N</i>-glycosylation of HNE purified from neutrophil lysates and then from isolated neutrophil granules of healthy individuals. The spatiotemporal expression of HNE during neutrophil activation and the biological importance of its <i>N</i>-glycosylation were also investigated using immunoblotting, cell surface capture, native MS, receptor interaction, protease inhibition, and bacteria growth assays. Site-specific HNE glycoprofiling demonstrated that unusual","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Aug","modification":"2026-05-03T03:48:51.984Z","creation":"2019-03-26T23:48:39Z"},"accession":"S-EPMC5546201","cross_references":{"pubmed":["28630087"],"doi":["10.1074/mcp.M116.066746","10.1074/mcp.m116.066746"]}}