Role of N-Linked Glycosylation in Human Osteonectin

Lecithin:cholesterol acyltransferase: role of N-linked glycosylation in enzyme function.

Lecithin:cholesterol acyltransferase (LCAT; phosphatidylcholine-sterol acyltransferase, EC 2.3.1.43) is a glycoprotein which is responsible for the formation of cholesteryl ester in plasma. The carbohydrate content has been estimated to be approx. 25% of the total LCAT mass, and four potential N-linked glycosylation sites have been predicted at residues 20, 84, 272 and 384 of the LCAT protein s...

Identification of an N-Linked Glycosylation

Structural determinants for N-linked glycosylation

Site selectivity of protein N-linked glycosylation is dependent on many factors, including accessibility of the modification site, amino acids that make up the glycosylation consensus sequence and cellular localization of target proteins. Previous studies have shown that the bacterial oligosaccharyltransferase, PglB, of Campylobacter jejuni favors acceptor proteins with consensus sequences (D/E...

Functional Divergence in the Role of N-Linked Glycosylation in Smoothened Signaling

The G protein-coupled receptor (GPCR) Smoothened (Smo) is the requisite signal transducer of the evolutionarily conserved Hedgehog (Hh) pathway. Although aspects of Smo signaling are conserved from Drosophila to vertebrates, significant differences have evolved. These include changes in its active sub-cellular localization, and the ability of vertebrate Smo to induce distinct G protein-dependen...

Role of N-linked glycosylation in the secretion and activity of endothelial lipase.

Human endothelial lipase (EL), a member of the triglyceride lipase gene family, has five potential N-linked glycosylation sites, two of which are conserved in both lipoprotein lipase and hepatic lipase. Reduction in molecular mass of EL after treatment with glycosidases and after treatment of EL-expressing cells with the glycosylation inhibitor tunicamycin demonstrated that EL is a glycosylated...