Recombinant Human PLA2G7/PAF-AH/Lp-PLA2 Protein, CF

Secretory phopholipase A₂ is an enzyme that hydrolyses the Sn-2 ester bond of phospholipids, generating free fatty acids and lysophospholipids (1‑3). 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. Also known as Lp-PLA2, PLA2G-VII is a plasma enzyme bound to lipoproteins: 80% bound to LDL, 15%-20% to HDL, and the remainder to VLDL (4-6). It is produced in major by mature macrophages and activated platelets. In contrast to other classical sPLA₂s, PLA2G‑VII has poor specificity toward Sn-2 long chain fatty acids, unless heavily oxidized, and undergoes the catalysis of its substrates in the aqueous phase rather than at the interfacial surface of lipids. Thus, it has high specificity for water-soluble phospholipids in plasma including oxidatively‑modified phospholipids and platelet-activating factor (PAF). Because of the latter activity, it is also known as PAF acetylhydrolase (PAF-AH). Lack of human PLA2G‑VII is related to a higher risk for stroke and heart disease.