Selectin GMP-140 (CD62; PADGEM) binds to sialosyl-Lea and sialosyl-Lex, and sulfated glycans modulate this binding

doi:10.1016/0006-291X(91)92069-V

Biochemical and Biophysical Research Communications

Volume 181, Issue 3, 31 December 1991, Pages 1223-1230

https://doi.org/10.1016/0006-291X(91)92069-V Get rights and content

Abstract

GMP-140 (CD62; PADGEM) is a member of the selectin family expressed highly at the surface of platelets and endothelial cells by agonists such as thrombin or phorbol esters. Previous studies indicate that the lectin domain of GMP-140 recognizes sialosyl-Le^x (SLe^x) and to a lesser extent Le^x (Polley MJ, et al., $Proc Natl Acad Sci USA$ 88:6224, 1991). We now report that GMP-140 binds to sialosyl Le^a (SLe^a) and to SLe^x, and that degree of binding to SLe^a is greater than that to SLe^x under our experimental conditions. Binding of activated platelets to SLe^a or SLe^x was inhibited to various degrees in the presence of sulfated glycans, suggesting that sulfated glycans induce conformational change in the lectin domain of GMP-140 and modulates its binding affinity to SLe^a and SLe^x.

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Selectin GMP-140 (CD62; PADGEM) binds to sialosyl-Lea and sialosyl-Lex, and sulfated glycans modulate this binding

Abstract

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J. Biol. Chem

Biochem. Biophys. Res. Commun

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Nature

Selectin GMP-140 (CD62; PADGEM) binds to sialosyl-Le^a and sialosyl-Le^x, and sulfated glycans modulate this binding