Rat P-Selectin (SELP) Protein

Background

Selectin P (SELP), also known as P-selectin, is a cell adhesion molecule that plays a key role in inflammation, hemostasis, and immune response by mediating the interaction between platelets, endothelial cells, and leukocytes. P-selectin is primarily stored in the alpha granules of platelets and the Weibel-Palade bodies of endothelial cells and is rapidly mobilized to the cell surface upon cellular activation. The SELP gene, which encodes P-selectin, is located on chromosome 1q24.2. It belongs to the selectin family, which includes L-selectin (SELL), E-selectin (SELE), and P-selectin (SELP), all of which are involved in the early stages of leukocyte trafficking during inflammatory responses. P-selectin functions in the rolling and adhesion of leukocytes to the endothelium, a critical step in immune surveillance and the recruitment of immune cells to sites of tissue damage or infection. In the context of inflammation, it facilitates the rapid interaction between leukocytes and the vascular wall, allowing for their migration into the affected tissue. Its ligands include P-selectin glycoprotein ligand-1 (PSGL-1), which is found on the surface of leukocytes. P-selectin's involvement in thrombus formation is also crucial, as it mediates interactions between activated platelets and the endothelium, contributing to thrombosis.