Functional Roles of the Bisecting GlcNAc in Integrin-Mediated Cell Adhesion

摘要: N-acetylglucosaminyltransferase III (GnT-III) transfers N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to core mannose with a beta1,4 linkage, so-called bisecting GlcNAc, in N-glycans. The GlcNAc is found various hybrid and complex GnT-III generally regarded as key glycosyltransferase N-glycan biosynthetic pathways. Introduction of suppresses further processing elongation N-glycans catalyzed by other transferases form branching structures, such V (GnT-V), since GnT-V cannot utilize the bisected oligosaccharide substrate. Considering that expression enzyme leads remarkable structural alteration on cell surface, it has been postulated associated biological events adhesion, migration, growth, differentiation, tumor invasion. Integrin major carrier In fact, overexpression reduced beta1,6 conjunction increase integrins, resulted an inhibition integrin-mediated spreading cellular phosphorylation levels. Conversely, knockdown endogenous increased concomitant GlcNAc-branched integrins. Thus, could be considered either positive or negative regulator for functions integrin.