Novel N-glycosylation in eukaryotes: Laminin contains the linkage unit β-glucosylasparagine

36Citations
Citations of this article
14Readers
Mendeley users who have this article in their library.
Get full text

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 β-Glc-Asn by immunofluorescence to the basement membranes of kidney glomeruli.

Cite

CITATION STYLE

APA

Schreiner, R., Schnabel, E., & Wieland, F. (1994). Novel N-glycosylation in eukaryotes: Laminin contains the linkage unit β-glucosylasparagine. Journal of Cell Biology, 124(6), 1071–1081. https://doi.org/10.1083/jcb.124.6.1071

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free