Serum amyloid P component conserved in all vertebrates and also found in distant invertebrates such as the horseshoe crab (Limulus polyphemus). Serum amyloid P component The serum amyloid P component (SAP) is the identical serum form of amyloid P component (AP), a 25kDa pentameric protein first identified as the pentagonal constituent of in vivo pathological deposits called "amyloid". APCS is its human gene. AP makes up 14% of the dry mass of amyloid deposits and is thought to be an important contributor to the pathogenesis of a related group of diseases called the Amyloidoses. These conditions are characterised by the ordered aggregation of normal
P-selectin glycoprotein ligand-1 is a glycoprotein found on white blood cells and endothelial cells that binds to P-selectin (P stands for platelet), which is one of a family of selectins that includes E-selectin (endothelial) and L-selectin (leukocyte). Selectins are part of the broader family of cell adhesion molecules. PSGL-1 can bind to all three members of the family but binds best (with the highest affinity) to P-selectin. PSGL-1 protein requires two distinct posttranslational modifications to gain its selectin binding activity: PSGL-1 is expressed on all white blood cells and plays an important role in the recruitment of white blood cells into inflamed tissue: