Literature DB >> 1722400

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

K Handa1, E D Nudelman, M R Stroud, T Shiozawa, S Hakomori.   

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) (SLex) 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 Lea (SLea) and to SLex, and that degree of binding to SLea is greater than that to SLex under our experimental conditions. Binding of activated platelets to SLea or SLex 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 SLea and SLex.

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Year:  1991        PMID: 1722400     DOI: 10.1016/0006-291x(91)92069-v

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  28 in total

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Authors:  A Varki
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Review 5.  Selectins.

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9.  Higher-affinity oligosaccharide ligands for E-selectin.

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10.  Self-recognition of high-mannose type glycans mediating adhesion of embryonal fibroblasts.

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