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Novel N-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine

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...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1994
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119980/
https://www.ncbi.nlm.nih.gov/pubmed/8132707
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description 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.
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spelling pubmed-21199802008-05-01 Novel N-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine J Cell Biol Articles 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. The Rockefeller University Press 1994-03-02 /pmc/articles/PMC2119980/ /pubmed/8132707 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Novel N-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine
title Novel N-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine
title_full Novel N-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine
title_fullStr Novel N-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine
title_full_unstemmed Novel N-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine
title_short Novel N-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine
title_sort novel n-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119980/
https://www.ncbi.nlm.nih.gov/pubmed/8132707