Selectins: functional importance as cell adhesion molecule in immune system
Journal of Biomedical Translational Research
Selectins are cell membrane glycoproteins that recognize specific glycoconjugates expressed on the surface of cells. Then, selectins adjust cell-cell interactions that are important in inflammation, hemostasis and cancer metastasis. Selectins mediate leukocyte calls to move into the site of inflammation through interactions with activated endothelial cells or endogenous selectin ligands expressed in high endothelial venules. Types of selectins are divided into L-selectin, E-selectin and
... in, which are called to CD62L, CD62E, and CD62P, respectively. Each selectin is composed of four regions; the C-type lectin region of N-terminal, the epidermal growth factor (EGF) region, the intracellular C-terminal region, and the hydrophobic transmembrane region. They have similar structures but differ in their binding specificities and tissue distributions. The selectin family commonly recognizes the sialyl Lewis X (sLeX) on carbohydrate structures. Although biological ligands bound to each selectin are different from each other, they commonly bind to P-selectin glycoprotein ligand-1 (PSGL-1) ligand. The PSGL-1 ligand is a glycoprotein promoting cell adhesion in inflammatory responses. If the absence of selectins and their ligands in humans and animals are, should lead to persistent infections and diseases. Selectin family must be considered as a key subject for drug discovery since they have various functions depending on the ligand which they bind to.