Eselectine

Eselectine is a cell-surface adhesion molecule belonging to the selectin family. In humans it is commonly known as E-selectin, CD62E, or ELAM-1, and is encoded by the SELE gene. The spelling “Eselectine” appears in some texts as an alternate form.

The protein is a type I transmembrane glycoprotein. Its extracellular region contains a calcium-dependent C-type lectin domain that recognizes carbohydrate ligands, followed by an EGF-like domain and a stalk region with short consensus repeats. The cytoplasmic tail participates in intracellular signaling and endocytosis, contributing to the regulation of cell-surface expression.

Expression of Eselectine is induced on activated vascular endothelium by inflammatory signals such as interleukin-1 and tumor necrosis factor. Upregulation occurs rapidly in response to inflammation, enabling leukocyte interactions with the endothelium during immune responses.

Functionally, Eselectine mediates the initial tethering and rolling of leukocytes on the vascular surface, an early step in leukocyte extravasation. Its ligands are carbohydrate structures on leukocytes, including sialylated Lewis antigens; binding is calcium-dependent and forms part of the multistep adhesion cascade that also involves other selectins and integrins.

Clinical and research relevance is focused on inflammation and vascular disease. Soluble E-selectin can be measured as a biomarker of endothelial activation, and alterations in SELE expression or function have been studied in conditions such as sepsis and atherosclerosis. Therapeutic approaches have included antibodies and other inhibitors aimed at blocking E-selectin–ligand interactions, with ongoing research to evaluate clinical utility.