TY - JOUR
T1 - A crucial effect of ligand clustering on the inhibition of binding by L-selectin in intercellular adhesion
AU - Yoshida, Tomoaki
AU - Toyama-Sorimachi, Noriko
AU - Miyasaka, Masayuki
AU - Lee, Yuan C.
PY - 1994/10/28
Y1 - 1994/10/28
N2 - Glucan sulfates were found to be potent ligands for L-selectin by a quantitative liquid phase analysis system (Yoshida, T. et al., Eur. J. Biochem., in press). The affinity of glucan sulfates to L-selectin-IgG chimera was dependent on the sizes of the glucan sulfates as well as on the inter-glucose linkages. In the current report, these glucan sulfates are shown to inhibit the interaction of an endothelial cell line with lymphocytes. The effect of ligand size appears to be more remarkable in the cell-cell binding than in the liquid phase analysis. The affinity of amylose sulfate continues to increase, as their size increases even beyond 12 kDa, at which its affinity reached a plateaux in the liquid phase analysis.
AB - Glucan sulfates were found to be potent ligands for L-selectin by a quantitative liquid phase analysis system (Yoshida, T. et al., Eur. J. Biochem., in press). The affinity of glucan sulfates to L-selectin-IgG chimera was dependent on the sizes of the glucan sulfates as well as on the inter-glucose linkages. In the current report, these glucan sulfates are shown to inhibit the interaction of an endothelial cell line with lymphocytes. The effect of ligand size appears to be more remarkable in the cell-cell binding than in the liquid phase analysis. The affinity of amylose sulfate continues to increase, as their size increases even beyond 12 kDa, at which its affinity reached a plateaux in the liquid phase analysis.
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U2 - 10.1006/bbrc.1994.2555
DO - 10.1006/bbrc.1994.2555
M3 - Article
C2 - 7526857
AN - SCOPUS:0028104440
SN - 0006-291X
VL - 204
SP - 969
EP - 974
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -