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Site-specific -glycosylation of members of the low-density lipoprotein receptor superfamily enhances ligand interactions.

J. Biol. Chem.. 2018; 
Wang Shengjun,Mao Yang,Narimatsu Yoshiki,Ye Zilu,Tian Weihua,Goth Christoffer K,Lira-Navarrete Erandi,Pedersen Nis B,Benito-Vicente Asier,Martin Cesar,Uribe Kepa B,Hurtado-Guerrero Ramon,Christoffersen Christina,Seidah Nabil G,Nielsen Rikke,Christensen Erik I,Hansen Lars,Bennett Eric P,Vakhrushev Sergey Y,Schjoldager Katrine T,Clausen He
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摘要

The low-density lipoprotein receptor (LDLR) and related receptors are important for the transport of diverse biomolecules across cell membranes and barriers. Their functions are especially relevant for cholesterol homeostasis and diseases, including neurodegenerative and kidney disorders. Members of the LDLR-related protein family share LDLR class A (LA) repeats providing binding properties for lipoproteins and other biomolecules. We previously demonstrated that short linker regions between these LA repeats contain conserved -glycan sites. Moreover, we found that -glycan modifications at these sites are selectively controlled by the GalNAc-transferase isoform, GalNAc-T11. However, the effects of GalNAc-... More

关键词

GALNT,O-glycosylation,glycosylation,glycosyltransferase,lipid metabolism,lipophorin receptor,lipoprotein receptor,low-density lipoprotein (