We are analyzing https://link.springer.com/article/10.1007/s11064-010-0379-9.

Title:
Regulation of Epidermal Growth Factor Receptor Through Interaction of Ganglioside GM3 with GlcNAc of N-Linked Glycan of the Receptor: Demonstration in ldlD Cells | Neurochemical Research
Description:
We investigated interaction of GM3 with N-acetylglucosamine (GlcNAc) termini of N-linked glycans of epidermal growth factor receptor (EGFR), as the underlying mechanism for inhibitory effect of GM3 on EGFR activation, using ldlD cells transfected with EGFR gene. These cells, defective in UDP-Gal/UDP-GalNAc 4-epimerase, are incapable of synthesizing galactose (Gal)-containing glycans, unless Gal is provided in culture (+Gal). Key observations: (1) Expression of GlcNAc termini was high in −Gal cells, and strongly reduced in +Gal cells. (2) Comparative study of inhibitory effect of exogenously-added GM3 on EGFR activation in +Gal versus −Gal cells indicated that higher level of GlcNAc termini on EGFR is correlated with greater inhibitory effect of GM3. (3) GM3-, but not GM1-, coated beads bound to EGFR in lysate of −Gal cells, which have highly exposed GlcNAc termini. Such binding was inhibited in the presence of EDTA, similarly to other carbohydrate-carbohydrate interactions.
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Keywords {🔍}

google, scholar, article, cas, pubmed, cell, receptor, growth, cells, biol, chem, epidermal, factor, interaction, hakomori, glcnac, egfr, handa, usa, ganglioside, gal, research, regulation, termini, access, sci, nlinked, ldld, gene, binding, kinase, proc, natl, acad, tyrosine, privacy, cookies, function, content, guan, phosphorylation, specific, motility, information, publish, search, senitiroh, effect, expression, open,

Topics {✒️}

terminal n-acetyl-d-glucosamine structure n-acetyl-d-glycosamine binding lectin udp-gal/udp-galnac 4-epimerase kazuko handa & sen-itiroh hakomori insulin/transferrin/selenium ldld/egfr month download article/chapter insulin-dependent cell growth n-linked glcnac termini laminin-5-dependent cell motility n-linked glycan related subjects gene transfection-mediated overexpression growth factor binding sen-itiroh hakomori carbohydrate-carbohydrate interactions tyrosine kinase activity carbohydrate-carbohydrate interaction asparagine-linked oligosaccharides o-linked glycosylation full article pdf protein-bound oligosaccharides insulin receptor function ldld cells transfected freire-de-lima receptor-receptor interaction embryonal carcinoma cells n-linked glycans privacy choices/manage cookies hamster cell line tumor cell motility cell growth regulation trends biochem sci regulates receptor function glioma cell line multivalent glcnac termini cell adhesion based tumour cells based allosteric receptor oligomerization erythroagglutinating phytohemagglutinin lectin bladder cancer cells receptor-mediated endocytosis check access instant access cell density-dependent ganglioside-mediated modulation article guan b16 mouse melanoma ldl receptor expression f9 teratocarcinoma cells gm3-mediated interaction

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         description:We investigated interaction of GM3 with N-acetylglucosamine (GlcNAc) termini of N-linked glycans of epidermal growth factor receptor (EGFR), as the underlying mechanism for inhibitory effect of GM3 on EGFR activation, using ldlD cells transfected with EGFR gene. These cells, defective in UDP-Gal/UDP-GalNAc 4-epimerase, are incapable of synthesizing galactose (Gal)-containing glycans, unless Gal is provided in culture (+Gal). Key observations: (1) Expression of GlcNAc termini was high in −Gal cells, and strongly reduced in +Gal cells. (2) Comparative study of inhibitory effect of exogenously-added GM3 on EGFR activation in +Gal versus −Gal cells indicated that higher level of GlcNAc termini on EGFR is correlated with greater inhibitory effect of GM3. (3) GM3-, but not GM1-, coated beads bound to EGFR in lysate of −Gal cells, which have highly exposed GlcNAc termini. Such binding was inhibited in the presence of EDTA, similarly to other carbohydrate-carbohydrate interactions.
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      description:We investigated interaction of GM3 with N-acetylglucosamine (GlcNAc) termini of N-linked glycans of epidermal growth factor receptor (EGFR), as the underlying mechanism for inhibitory effect of GM3 on EGFR activation, using ldlD cells transfected with EGFR gene. These cells, defective in UDP-Gal/UDP-GalNAc 4-epimerase, are incapable of synthesizing galactose (Gal)-containing glycans, unless Gal is provided in culture (+Gal). Key observations: (1) Expression of GlcNAc termini was high in −Gal cells, and strongly reduced in +Gal cells. (2) Comparative study of inhibitory effect of exogenously-added GM3 on EGFR activation in +Gal versus −Gal cells indicated that higher level of GlcNAc termini on EGFR is correlated with greater inhibitory effect of GM3. (3) GM3-, but not GM1-, coated beads bound to EGFR in lysate of −Gal cells, which have highly exposed GlcNAc termini. Such binding was inhibited in the presence of EDTA, similarly to other carbohydrate-carbohydrate interactions.
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