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Heparan sulfate and chondroitin sulfate proteoglycans inhibit E‐selectin binding to endothelial cells
Author(s) -
Luo Jianying,
Kato Masato,
Wang Huiming,
Bernfield Merton,
Bischoff Joyce
Publication year - 2001
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/1097-4644(20010315)80:4<522::aid-jcb1006>3.0.co;2-h
Subject(s) - heparan sulfate , chondroitin sulfate , chemistry , endothelial stem cell , ectodomain , chondroitin , angiogenesis , cell adhesion molecule , cell adhesion , microbiology and biotechnology , perlecan , endothelium , selectin , biochemistry , heparin , in vitro , cell , biology , glycosaminoglycan , cancer research , receptor , endocrinology
E‐selectin is a cell adhesion molecule involved in the initial rolling and adhesion of leukocytes to the endothelium during inflammation. In addition, in vitro studies have suggested that an interaction between E‐selectin and binding sites such as sialyl Lewis X‐containing oligosaccharides on endothelial cells may be important for angiogenesis. In order to investigate the binding of E‐selectin to endothelial cells, we developed an ELISA assay using chimeric E‐selectin‐Ig molecules and endothelial cells fixed on poly‐L‐lysine coated plates. Our results indicate that E‐selectin‐Ig binds to both bovine capillary endothelial cells and human dermal microvascular endothelial cells in a calcium‐dependent and saturable manner. The binding is inhibited markedly by heparin and by syndecan‐1 ectodomain, and moderately by chondroitin sulfate, but not by sialyl Lewis X‐containing oligosaccharides. These results suggest that heparan sulfate and chondroitin sulfate proteoglycans on endothelial cells are potential ligands for E‐selectin. J. Cell. Biochem. 80:522–531, 2001. © 2001 Wiley‐Liss, Inc.