RRC ID 18546
Author Yabe T, Hosoda-Yabe R, Kanamaru Y, Kiso M.
Title A peptide found by phage display discriminates a specific structure of a trisaccharide in heparin.
Journal J Biol Chem
Abstract 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.
Volume 286(14)
Pages 12397-406
Published 2011-4-8
DOI 10.1074/jbc.M110.172155
PII S0021-9258(20)51619-0
PMID 21335559
PMC PMC3069443
MeSH Animals Cell Differentiation / drug effects Chromatography, Affinity Fibroblast Growth Factor 1 / pharmacology Fibroblast Growth Factor 2 / pharmacology Heparin / chemistry* Heparin / metabolism* Heparitin Sulfate / chemistry Heparitin Sulfate / metabolism Humans PC12 Cells Peptide Library* Peptides / chemistry* Peptides / metabolism* Rats Trisaccharides / chemistry*
IF 4.238
Times Cited 4
Human and Animal Cells PC-12(RCB0009)