title: Novel N-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine.
abstract: The linkage unit to protein of N-linked carbohydrate in eukaryotic glycoproteins consists of N-acetylglucosamine, coupled to the amido nitrogen of asparagine. Additional N-glycosyl linkage units have been unequivocally proven to exist only in the cell surface glycoproteins of various bacteria. Based on immunological analyses, isolation and chemical characterization, we report that one of these units, namely glucose linked to asparagine, exists in the mammalian protein laminin, an extracellular basement membrane component. This finding and the occurrence of identical disaccharide structures in archaebacterial cell surface glycoproteins and mammalian basement membrane protein complexes points towards a conserved and distinct function of these extracellular structural elements. In addition, a method is described to uncover a masked epitope in fixed tissues by chemical O-deglycosylation. This has allowed to morphologically localize the antigen beta-Glc-Asn by immunofluorescence to the basement membranes of kidney glomeruli.
authors.affiliation: Baylor Research Institute, Dallas, Texas 75226.
authors.forename: R
authors.initials: R
authors.lastname: Schreiner
authors.forename: E
authors.initials: E
authors.lastname: Schnabel
authors.forename: F
authors.initials: F
authors.lastname: Wieland
mesh_terms: D000818:Animals; D000918:Antibody Specificity; D001216:Asparagine / Q000031:analogs & derivatives* / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D001485:Basement Membrane / Q000737:chemistry; D015153:Blotting, Western; D005455:Fluorescent Antibody Technique; D006031:Glycosylation; D007678:Kidney Glomerulus / Q000737:chemistry*; D007797:Laminin / Q000737:chemistry*; D051381:Rats
chemical_list: D007797:Laminin; C086316:glucosylasparagine; D001216:Asparagine