Human PLA2G2A Antibody

Secretory phopholipase A₂ is an enzyme that hydrolyzes the sn-2 ester bond of phospholipids, generating non-esterified free fatty acids and lysophospholipids (1‑4). Most secretory PLA₂s are stored in cytoplasmic granules and are released in the extracellular environment on appropriate cell activation. Thus, they are present at higher concentration in the plasma and biologic fluids of patients with systemic inflammatory, autoimmune, or allergic disease, such as acute pancreatitis, rheumatoid arthritis, bronchial asthma, and allergic rhinitis. PLA2G2A is a calcium dependent phospholipase expressed in many cell types associated with inflammation, including platelets, neutrophils, and mast cells. It has been recognized as an acute phase reactant and its concentration increases during systemic inflammation such as sepsis, rheumatoid arthritis, and cardiovascular disease (5). It may function as an enzymatic component of the host defense mechanism. For example, human tears contain a high concentration of PLA2G2A and this is the principal bactericidal factor against Gram-positive bacteria in this fluid (1). It may play a role in cell proliferation through binding a receptor on membrane surface or extracellular matrix components such as heparan sulfate proteoglycan and integrins (6). It has been shown to have pro-atherogenic properties both in the circulation and within the arterial wall (7). Circulating levels of PLA2G2A are higher in coronary artery disease (CAD) patients and are associated with increased risk of future CAD (8).