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Identification of Endothelial Cell Surface Carbohydrate-Binding Receptors by Carbohydrate Ligand Mimicry Peptides

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Book cover Biochemical Roles of Eukaryotic Cell Surface Macromolecules

Part of the book series: Advances in Experimental Medicine and Biology ((volume 749))

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Abstract

Substantial evidence suggests that cell surface carbohydrate antigens, particularly those containing fucose residues, are related to cancer malignancy. To investigate the mechanisms underlying cell surface carbohydrate-dependent cancer metastasis, we developed a 7-mer peptide, designated as I-peptide, which is capable of inhibiting FUT3-transfected B16 cell colonization of lung in the mouse. I-peptide inhibited lung colonization of FUT3-B16 cells in E-/P-selectin doubly deficient mutant mice, suggesting the existence of an as yet unidentified carbohydrate-binding endothelial receptor distinct from E-/P-selectins. Subsequently, we isolated the endothelial receptors by I-peptide affinity chromatography and identified them by proteomics. Thus, I-peptide receptors were identified to be pre-mRNA splicing factor (Sfrs) proteins. We also found a fragment of annexin A1 (Anxa1) bound to I-peptide. Our study demonstrated the usefulness of carbohydrate-ligand mimicry peptide for the identification of novel carbohydrate-binding proteins.

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Correspondence to Michiko N. Fukuda .

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Fukuda, M.N. (2012). Identification of Endothelial Cell Surface Carbohydrate-Binding Receptors by Carbohydrate Ligand Mimicry Peptides. In: Sudhakaran, P., Surolia, A. (eds) Biochemical Roles of Eukaryotic Cell Surface Macromolecules. Advances in Experimental Medicine and Biology, vol 749. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-3381-1_5

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