E-selectin prefers fatty-sweet receptors on rolling neutrophils

摘要

In this issue of Blood, Nimrichter and colleagues have defined the structure and function of distinct E-selectin ligands on the plasma membrane of neutrophils. They demonstrate that as few as 60 receptors/mum~2 of these sialylated and fuco-sylated glycolipids facilitate neutrophil capture and rolling at sites of acute inflammation.Selectins constitute a highly conserved family of glycoproteins that, as their lec-tin surname suggests, bind terminal sugars expressed on lipid and protein receptors to mediate adhesive interactions and transmem-brane signaling between leukocytes, platelets, and inflamed endothelium. It has long been known that all 3 selectin family members exploit a common biochemical recognition strategy in binding proteins decorated with fucosy-lated sialyl Lewis sugars. What has remained elusive is the discovery of the E-selectin binding partners on human neutrophils that confer selectivity and affinity and facilitate trafficking at sites of inflammation.