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Description
Annexin V, also known as PAP-1 or Lipocortin V, is a ~30 kDa protein that binds to phospholipids in a calcium-dependent manner . All annexins contain a putative PKC binding site, but only annexin V has been identified as an inhibitor of this pathway . It may also signal, by direct interaction with VEGFR2 receptor, in the regulation of vascular endothelial cell proliferation . Annexin V preferentially binds phosphatidylserine, in competition with prothrombin, leading to inhibition of blood coagulation at sites of injury preceding contact between lipid components and coagulation factors that initiate thrombosis . The ability of Annexin V to bind specifically and robustly to phosphatidylserine makes it an attractive reagent in detecting apoptotic cells . Annexin V is inducible by glucocorticoids and can be phosphorylated by tyrosine and serine/threonine kinases . It is thought to block production of mediators of inflammation, such as prostaglandins and leukotrienes by inhibiting the release of arachidonic acid from membranes by phospholipase A2 . Synonyms: ANX5, ENX2, PP4,