E-selectin ligand (ESL) (ESL)

E-selectin ligands are specialized carbohydrate-decorated glycoproteins, such as HCELL (Hematopoietic Cell E-selectin/L-selectin Ligand) and PSGL-1 (P-selectin glycoprotein ligand-1), that facilitate the initial tethering and rolling of cells on the vascular endothelium (Sackstein, 2004). These ligands are characterized by the presence of sialylated, fucosylated tetrasaccharides known as sialyl Lewis X (sLeX), which bind with high affinity to E-selectin (CD62E) expressed on activated endothelial cells (Dimitroff et al., 2001). In a therapeutic context, the engineering of these ligands onto the surface of cells—such as mesenchymal stem cells or hematopoietic stem cells—is a primary strategy to enhance their homing capabilities to the bone marrow or sites of inflammation (Sackstein, 2011). This process, often referred to as glycosyltransferase-programmed stereosubstitution (GPS), allows therapeutic cells to effectively exit the bloodstream and reach target tissues, thereby improving the efficacy of regenerative medicines. Conversely, the interaction between E-selectin and its ligands is a major target for pharmacological inhibition in diseases like sickle cell anemia, acute myeloid leukemia, and various inflammatory conditions where excessive cell recruitment or cancer metastasis occurs (GlycoMimetics, 2023). Drugs like uproleselan act as E-selectin antagonists to disrupt this binding, highlighting the ligand's importance as both a target for modification and a target for inhibition.

Other names

HCELLHematopoietic Cell E-selectin/L-selectin LigandPSGL-1P-selectin glycoprotein ligand-1Sialyl Lewis XsLeXCD44 glycoformESL-1E-selectin ligand-1

Mediates the initial tethering and rolling of cells on activated vascular endothelium by binding to E-selectin (CD62E).