{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["285(47)"],"submitter":["Schjoldager KT"],"funding":["Howard Hughes Medical Institute"],"pubmed_abstract":["The angiopoietin-like protein 3 (ANGPTL3) is an important inhibitor of the endothelial and lipoprotein lipases and a promising drug target. ANGPTL3 undergoes proprotein convertase processing (RAPR(224)↓TT) for activation, and the processing site contains two potential GalNAc O-glycosylation sites immediately C-terminal (TT(226)). We developed an in vivo model system in CHO ldlD cells that was used to show that O-glycosylation in the processing site blocked processing of ANGPTL3. Genome-wide SNP association studies have identified the polypeptide GalNAc-transferase gene, GALNT2, as a candidate gene for low HDL and high triglyceride blood levels. We hypothesized that the GalNAc-T2 transferase performed critical O-glycosylation of proteins involved in lipid metabolism. Screening of a panel of"],"journal":["The Journal of biological chemistry"],"pagination":["36293-303"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2978557"],"repository":["biostudies-literature"],"pubmed_title":["O-glycosylation modulates proprotein convertase activation of angiopoietin-like protein 3: possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipids."],"pmcid":["PMC2978557"],"pubmed_authors":["Schjoldager KT","Vester-Christensen MB","Yin W","Bennett EP","Clausen H","Schwientek T","Blixt O","Levery SB"],"additional_accession":[]},"is_claimable":false,"name":"O-glycosylation modulates proprotein convertase activation of angiopoietin-like protein 3: possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipids.","description":"The angiopoietin-like protein 3 (ANGPTL3) is an important inhibitor of the endothelial and lipoprotein lipases and a promising drug target. ANGPTL3 undergoes proprotein convertase processing (RAPR(224)↓TT) for activation, and the processing site contains two potential GalNAc O-glycosylation sites immediately C-terminal (TT(226)). We developed an in vivo model system in CHO ldlD cells that was used to show that O-glycosylation in the processing site blocked processing of ANGPTL3. Genome-wide SNP association studies have identified the polypeptide GalNAc-transferase gene, GALNT2, as a candidate gene for low HDL and high triglyceride blood levels. We hypothesized that the GalNAc-T2 transferase performed critical O-glycosylation of proteins involved in lipid metabolism. Screening of a panel of","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Nov","modification":"2026-04-29T21:42:07.792Z","creation":"2019-03-27T00:36:32Z"},"accession":"S-EPMC2978557","cross_references":{"pubmed":["20837471"],"doi":["10.1074/jbc.m110.156950","10.1074/jbc.M110.156950"]}}