期刊
NEUROCHEMICAL RESEARCH
卷 36, 期 9, 页码 1645-1653出版社
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s11064-010-0379-9
关键词
Epidermal growth factor receptor (EGFR); ldlD cells; N-linked glycan; GlcNAc termini; Ganglioside GM3; Carbohydrate-carbohydrate interaction
资金
- NIH National Cancer Institute [2 R01 CA080054]
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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