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• W2078751804 abstract "E-selectin is a member of the selectin family of proteins that recognize carbohydrate ligands in a Ca2+-dependent manner. In order to better understand the role of Ca2+ in E-selectin-ligand interactions, we examined the E-selectin structure by limited proteolysis. Apo-Lec-EGF-CR6, a Ca2+-free form of soluble E-selectin containing the entire extracellular domain, was sensitive to limited proteolysis by Glu-C endoproteinase. Amino-terminal sequencing analysis of the proteolytic fragments revealed that the major cleavage site is at Glu98 which is in the loop (residues 94-103) adjacent to the Ca2+ binding region of the lectin domain. Upon Ca2+ binding, Lec-EGF-CR6 was protected from proteolysis. This Ca2+-dependent protection was further augmented upon sialyl Lewis × (sLex) ligand binding. These results implied that Ca2+ binding to E-selectin induces a conformational change and perhaps facilitates ligand binding. The sLex-bound complex in turn stabilizes Ca2+ binding. Lec-EGF-CR6 contains only one high-affinity Ca2+ site (Kd = ≈3.5 μM) as determined by equilibrium dialysis. In addition, we found that Ba2+ was a potent antagonist in blocking Lec-EGF-CR6-mediated HL-60 cell adhesion. By competitive equilibrium dialysis and proteolysis analysis, we demonstrated that Ba2+ bound to apo-Lec-EGF-CR6 5-fold tighter than Ca2+ and abolished ligand binding activity. Sr2+ also bound to apo-Lec-EGF-CR6 tighter than Ca2+. However, Sr2+-regenerated Lec-EGF-CR6 showed 50% ligand binding activity. Mg2+ bound to apo-Lec-EGF-CR6 with much weaker affinity than Ca2+ and did not show any activity. Thus, E-selectin function can be modulated by different metal ions. E-selectin is a member of the selectin family of proteins that recognize carbohydrate ligands in a Ca2+-dependent manner. In order to better understand the role of Ca2+ in E-selectin-ligand interactions, we examined the E-selectin structure by limited proteolysis. Apo-Lec-EGF-CR6, a Ca2+-free form of soluble E-selectin containing the entire extracellular domain, was sensitive to limited proteolysis by Glu-C endoproteinase. Amino-terminal sequencing analysis of the proteolytic fragments revealed that the major cleavage site is at Glu98 which is in the loop (residues 94-103) adjacent to the Ca2+ binding region of the lectin domain. Upon Ca2+ binding, Lec-EGF-CR6 was protected from proteolysis. This Ca2+-dependent protection was further augmented upon sialyl Lewis × (sLex) ligand binding. These results implied that Ca2+ binding to E-selectin induces a conformational change and perhaps facilitates ligand binding. The sLex-bound complex in turn stabilizes Ca2+ binding. Lec-EGF-CR6 contains only one high-affinity Ca2+ site (Kd = ≈3.5 μM) as determined by equilibrium dialysis. In addition, we found that Ba2+ was a potent antagonist in blocking Lec-EGF-CR6-mediated HL-60 cell adhesion. By competitive equilibrium dialysis and proteolysis analysis, we demonstrated that Ba2+ bound to apo-Lec-EGF-CR6 5-fold tighter than Ca2+ and abolished ligand binding activity. Sr2+ also bound to apo-Lec-EGF-CR6 tighter than Ca2+. However, Sr2+-regenerated Lec-EGF-CR6 showed 50% ligand binding activity. Mg2+ bound to apo-Lec-EGF-CR6 with much weaker affinity than Ca2+ and did not show any activity. Thus, E-selectin function can be modulated by different metal ions." @default.
• W2078751804 created "2016-06-24" @default.
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• W2078751804 date "1995-04-01" @default.
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• W2078751804 title "Modulation of E-selectin Structure/Function by Metal Ions" @default.
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• W2078751804 doi "https://doi.org/10.1074/jbc.270.14.8138" @default.
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