SELE Gene: Selectin E - Function, Expression, and Clinical Significance

The SELE gene encodes E-selectin, a cell adhesion molecule expressed on cytokine-activated endothelial cells. It mediates the rolling and tethering of leukocytes on the vascular surface during inflammation by binding to sialyl-Lewis X and related glycans. SELE is a key player in the recruitment of neutrophils, monocytes, and memory T cells to sites of injury or infection.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Reactome: R-HSA-202733 – Cell surface interactions at the vascular wall

• Reactome: R-HSA-198933 – Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell

• KEGG: hsa04514 – Cell adhesion molecules (CAMs)

• KEGG: hsa04670 – Leukocyte transendothelial migration

E-selectin (CD62E) is a 610-amino acid transmembrane glycoprotein with an N-terminal C-type lectin domain, an EGF-like domain, six short consensus repeats (SCRs), a transmembrane region, and a short cytoplasmic tail. It is stored in Weibel-Palade bodies and rapidly translocated to the cell surface upon endothelial activation by inflammatory cytokines (TNF-α, IL-1β) or bacterial endotoxin. The lectin domain binds sialyl-Lewis X (sLe^x) and related fucosylated glycans on leukocyte surface proteins such as PSGL-1 and ESL-1. E-selectin mediates the initial tethering and rolling of leukocytes along the endothelium, a prerequisite for firm adhesion and transmigration into tissues. Soluble E-selectin (sE-selectin) shed from activated endothelium serves as a biomarker of endothelial dysfunction in inflammatory and cardiovascular diseases.