ArticleGlycoconjugate journal2014
Determination of major sialylated N-glycans and identification of branched sialylated N-glycans that dynamically change their content during development in the mouse cerebral cortex.
Article in Glycoconjugate journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- Divergent Enzymatic Synthesis of a Comprehensive Type‑1 Glycan Determinant Library.ACS catalysis · 2025Article
- Identification of a free-N-glycan with difucosylated type-1 lactosamine in cancerous tissue and its validation for cancer diagnosis by urinary testing.Scientific reports · 2025Article
- Unique Glycans in Synaptic Glycoproteins in Mouse Brain.ACS chemical neuroscience · 2024Article
- Small but big leaps towards neuroglycomics: exploring N-glycome in the brain to advance the understanding of brain development and function.Neural regeneration research · 2024Article
- Human-specific features and developmental dynamics of the brain N-glycome.Science advances · 2023Article
- The dynamic brain N-glycome.Glycoconjugate journal · 2022Review
- Towards Mapping of the Human Brain N-Glycome with Standardized Graphitic Carbon Chromatography.Biomolecules · 2022Article
- Activity-dependent Golgi satellite formation in dendrites reshapes the neuronal surface glycoproteome.eLife · 2021Article
- Toward robust N-glycomics of various tissue samples that may contain glycans with unknown or unexpected structures.Scientific reports · 2021Article
- Site-specific analysis of N-glycans from different sheep prion strains.PLoS pathogens · 2021Article
- A Potential SerumInternational journal of molecular sciences · 2020Article
- Spatial and temporal diversity of glycome expression in mammalian brain.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Depolarization-dependent Induction of Site-specific Changes in Sialylation onMolecular & cellular proteomics : MCP · 2020Article
- The manifold roles of sialic acid for the biological functions of endothelial glycoproteins.Glycobiology · 2020Review
- Glycosylation at an evolutionary nexus: the brittle starThe Journal of biological chemistry · 2020Article
- Differential expression of N-linked oligosaccharides in methotrexate-resistant primary central nervous system lymphoma cells.BMC cancer · 2019Article
- GlcNAc6ST-1 regulates sulfation of N-glycans and myelination in the peripheral nervous system.Scientific reports · 2017Article
- Glycan susceptibility factors in autism spectrum disorders.Molecular aspects of medicine · 2016Review
- Monosaccharide profiling of silkworm (Bombyx mori L.) nervous system during development and aging.Invertebrate neuroscience : IN · 2016Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oligosaccharides of glycoproteins expressed on the cell surface play important roles in cell-cell interactions, particularly sialylated N-glycans having a negative charge, which interact with sialic acid-binding immunoglobulin-like lectins (siglecs). The entire structure of sialylated N-glycans expressed in the mouse brain, particularly the linkage type of sialic acid residues attached to the backbone N-glycans, has not yet been elucidated. An improved method to analyze pyridylaminated sugar chains using high performance liquid chromatography (HPLC) was developed to determine the entire structure of sialylated N-linked sugar chains expressed in the adult and developing mouse cerebral cortices. Three classes of sialylated sugar chains were prevalent: 1) N-glycans containing α(2-3)-sialyl linkages on a type 2 antennary (Galβ(1-4)GlcNAc), 2) sialylated N-glycans with α(2-6)-sialyl linkages on a type 2 antennary, and 3) a branched sialylated N-glycan with a [Galβ(1-3){NeuAcα(2-6)}GlcNAc-] structure, which was absent at embryonic day 12 but then increased during development. This branched type sialylated N-glycan structure comprised approximately 2 % of the total N-glycans in the adult brain. Some N-glycans (containing type 2 antennary) were found to change their type of sialic acid linkage from α(2-6)-Gal to α(2-3)-Gal. Thus, the linkages and expression levels of sialylated N-glycans change dramatically during brain development.
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