<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>285(47)</volume><submitter>Schjoldager KT</submitter><funding>Howard Hughes Medical Institute</funding><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pagination>36293-303</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2978557</full_dataset_link><repository>biostudies-literature</repository><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.</pubmed_title><pmcid>PMC2978557</pmcid><pubmed_authors>Schjoldager KT</pubmed_authors><pubmed_authors>Vester-Christensen MB</pubmed_authors><pubmed_authors>Yin W</pubmed_authors><pubmed_authors>Bennett EP</pubmed_authors><pubmed_authors>Clausen H</pubmed_authors><pubmed_authors>Schwientek T</pubmed_authors><pubmed_authors>Blixt O</pubmed_authors><pubmed_authors>Levery SB</pubmed_authors></additional><is_claimable>false</is_claimable><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.</name><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</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Nov</publication><modification>2026-04-29T21:42:07.792Z</modification><creation>2019-03-27T00:36:32Z</creation></dates><accession>S-EPMC2978557</accession><cross_references><pubmed>20837471</pubmed><doi>10.1074/jbc.m110.156950</doi><doi>10.1074/jbc.M110.156950</doi></cross_references></HashMap>