Description
Cytosolic Phospholipase A2a (PLA2G4A) belongs to the group IV phospholipase A2 family (1). These enzymes hydrolyze the ester bond at the second position (sn-2) of membrane glycerophospholipids. The group IV phospholipase A2 (PLA2G4) family is comprised of six intracellular enzymes (2). PLA2G4A has a preference for arachidonic acid in the sn-2 position of phospholipids indicating its involvement in the metabolism of eicosanoids. Its active site is characterized by a serine and aspartic acid dyad. The overall structural feature displays two domains, a lipid binding C2 domain and a catalytic a/b hydrolase domain. PLA2G4A translocation to the membrane and activation is facilitated by a calcium-ion dependent conformational change in its C2 domain. In addition, phosphorylation of serine residues in PLA2G4A by protein kinases may be another regulatory mechanism for promoting the release of arachidonic acid. The knockout mouse studies of this enzyme indicate that the enzyme may play a major role in inflammatory diseases. Genetic ablation or reduction of PLA2G4A protected human amyloid precursor protein (APP) related pathogenesis from a mouse model (3). Mouse model studies of brain and lung cancer indicates that PLA2G4A may play a key regulatory role in angiogenesis of these tumors (4).
Recombinant corresponding to aa1-749 from Human PLA2G4A fused with 6-His-tag at C-terminal expressed in Sf21 cells (NP_077734)