A Peptide Found by Phage Display Discriminates a Specific Structure of a Trisaccharide in Heparin

A number of recent studies have shown that heparan sulfate can control several important biological events on the cell surface through changes in sulfation pattern. The in vivo modification of sugar chains with sulfates, however, is complicated, and the discrimination of different sulfation patterns...

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Bibliographic Details
Published in:The Journal of biological chemistry 2011-04, Vol.286 (14), p.12397-12406
Main Authors: Yabe, Tomio, Hosoda-Yabe, Ritsuko, Kanamaru, Yoshihiro, Kiso, Makoto
Format: Article
Language:English
Subjects:
Animals
Anticoagulant Effect
Antithrombin
Cell Differentiation - drug effects
Chromatography, Affinity
Fibroblast Growth Factor 1 - pharmacology
Fibroblast Growth Factor 2 - pharmacology
Glycobiology and Extracellular Matrices
Glycosaminoglycan
Heparan Sulfate
Heparin
Heparin - chemistry
Heparin - metabolism
Heparitin Sulfate - chemistry
Heparitin Sulfate - metabolism
Humans
PC12 Cells
Peptide Interactions
Peptide Library
Peptides - chemistry
Peptides - metabolism
Phage Display
Rats
Trisaccharides - chemistry
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Summary:A number of recent studies have shown that heparan sulfate can control several important biological events on the cell surface through changes in sulfation pattern. The in vivo modification of sugar chains with sulfates, however, is complicated, and the discrimination of different sulfation patterns is difficult. Heparin, which is primarily produced by mast cells, is closely approximated by the structural analog heparan sulfate. Screening of heparin-associating peptides using phage display and antithrombin-bound affinity chromatography identified a peptide, heparin-associating peptide Y (HappY), that acts as a target of immobilized heparin. The peptide consists of 12 amino acid residues with characteristic three arginines and exclusively binds to heparin and heparan sulfate but does not associate with other glycosaminoglycans. HappY recognizes three consecutive monosaccharide residues in heparin through its three arginine residues. HappY should be a useful probe to detect heparin and heparan sulfate in studies of glycobiology.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M110.172155