http://purl.uniprot.org/citations/20837471 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20837471 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20837471 | http://www.w3.org/2000/01/rdf-schema#comment | "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 proteins known to affect lipid metabolism for potential sites glycosylated by GalNAc-T2 led to identification of Thr(226) adjacent to the proprotein convertase processing site in ANGPTL3. We demonstrated that GalNAc-T2 glycosylation of Thr(226) in a peptide with the RAPR(224)↓TT processing site blocks in vitro furin cleavage. The study demonstrates that ANGPTL3 activation is modulated by O-glycosylation and that this step is probably controlled by GalNAc-T2."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.156950"xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.156950"xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Yin W."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Yin W."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Bennett E.P."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Bennett E.P."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Clausen H."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Clausen H."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Levery S.B."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Levery S.B."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Blixt O."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Blixt O."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Schjoldager K.T."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Schjoldager K.T."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Schwientek T."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Schwientek T."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Vester-Christensen M.B."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/author | "Vester-Christensen M.B."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/20837471 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |