Mouse P-Selectin, also known as GMP-140, LECAM-3, PADGEM, or CD62P, is a member of the Selectin family of cell surface glycoproteins. It is expressed by activated platelets and endothelial cells. The cDNA for Mouse P-Selectin encodes a 768 amino acid (aa) type I transmembrane protein. This protein comprises a 41 aa signal peptide, a 668 aa extracellular domain, a transmembrane domain, and a short (35 aa) cytoplasmic domain.
The extracellular domain of Mouse P-Selectin features an NH2-terminal C-type lectin domain and an EGF-like domain, succeeded by a series of complement factor A repeat homology domains. There is approximately 73% sequence homology between the extracellular domains of human and mouse P-Selectin.
P-Selectin is crucial for the adhesion of leukocytes and neutrophils to the endothelium. In conjunction with L-Selectin, it mediates the initial interaction between circulating leukocytes and endothelial cells, resulting in a characteristic 'rolling' phenomenon of leukocytes along the endothelium. Following this initial interaction, a stronger bond forms, involving E-Selectin, and subsequently ICAM-1 and VCAM-1. This sequence of events ultimately facilitates the extravasation of white blood cells through the blood vessel wall and into the surrounding tissue matrix.
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