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High prevalence of 2‐mono‐ and 2,6‐di‐substituted Manol‐terminating sequences among O‐glycans released from brain glycopeptides by reductive alkaline hydrolysis

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TLDR
There appears to be in higher eukaryotes a major alternative pathway related to the yeast-type protein O-mannosylation, the enzymatic basis and functional importance of which now require investigation.
Abstract
Di- to heptasaccharides isolated from total nondialyzable brain glycopeptides after release by alkaline borohydride treatment have been subjected to mass spectrometric and nuclear magnetic resonance spectroscopic analyses supplemented by TLC-MS analyses of derived neoglycolipids. A family of Manol-terminating oligosaccharides has been revealed which includes novel sequences with a 2, 6-disubstituted Manol: In contrast to the Manol-terminating HNK-1 antigen-positive chains described previously that occur as a minor population [Yuen, C.-T., Chai, W., Loveless, R.W., Lawson, A.M., Margolis, R.U. & Feizi, T. (1997) J. Biol. Chem. 272, 8924-8931], the above oligosaccharides are abundant. The ratio of these compounds to the classical N-acetylgalactosaminitol-terminating oligosaccharides is about 1 : 3. Thus, there appears to be in higher eukaryotes a major alternative pathway related to the yeast-type protein O-mannosylation, the enzymatic basis and functional importance of which now require investigation.

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Journal ArticleDOI

Role of Glycosylation in Development

TL;DR: A review of recent studies analyzing function of a variety of glycoconjugates, focusing on lessons learned from human disease and genetic studies in mice, Drosophila melanogaster, and Caenorhabditis elegans, suggests that O-fucose, O-mannose, N-glycans, mucin-type O-gly cans and proteoglycans are likely to play important roles in developmental processes.
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Oligosaccharide microarrays for high-throughput detection and specificity assignments of carbohydrate-protein interactions

TL;DR: In this article, the authors describe microarrays of oligosaccharides as neoglycolipids and their robust display on nitrocellulose, and show that carbohydrate-recognizing proteins single out their ligands not only in arrays of homogeneous oligosACcharides but also in array of heterogeneous oligo-charides.
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Glycoprotein structure determination by mass spectrometry

TL;DR: The power of ultrahigh-sensitivity mass spectrometric strategies for defining the primary structures of highly complex mixtures of glycoprotein glycoforms is set to revolutionize structural glycobiology in the coming postgenomic era.
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Glycans and neural cell interactions

TL;DR: Carbohydrate-carrying molecules in the nervous system have important roles during development, regeneration and synaptic plasticity and the tremendous structural diversity of glycan chains allows for immense combinatorial possibilities that might underlie the fine-tuning of cell–cell and cell–matrix interactions.
References
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Journal ArticleDOI

A simple and rapid method for the permethylation of carbohydrates

TL;DR: In this paper, a new method for the permethylation of sugars involving methyl iodide, a solid base (NaOH, KOH, or tert-BuOH/NaOH), and methyl sulphoxide was suggested.
Book ChapterDOI

High-Resolution, 1H-Nuclear Magnetic Resonance Spectroscopy as a Tool in the Structural Analysis of Carbohydrates Related to Glycoproteins

TL;DR: This chapter presents literature data on the high-resolution, 1H-NMR spectroscopy of carbohydrates derived from glycoconjugates and discusses the results for carbohydrates related to the glycoproteins of N-glycosylic type.
Journal ArticleDOI

Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin.

TL;DR: The major sialylated O-glycosidically-linked oligosaccharide of the α-dystroglycan was a novel O-mannosyl-type oligosACcharide, the structure of which was Siaα2-3Gal β1-4GlcNAcβ1-2Man-Ser/Thr (where Sia is sialic acid).
Journal ArticleDOI

Post-translational Modifications of Recombinant P-selectin Glycoprotein Ligand-1 Required for Binding to P- and E-selectin

TL;DR: It is demonstrated that PSGL-1 requires core 2 O-linked glycans that are sialylated and fucosylated to bind P- and E-selectin.
Journal ArticleDOI

Isolation and characterization of developmentally regulated chondroitin sulfate and chondroitin/keratan sulfate proteoglycans of brain identified with monoclonal antibodies.

TL;DR: A panel of monoclonal antibodies prepared to the chondroitin sulfate proteoglycans of rat brain was used for their immunocytochemical localization and isolation of individual proteoglycan species by immunoaffinity chromatography, finding that there is a developmental decrease in the branching and/or sulfation of the keratan sulfate chains.
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