sPLA2s hydrolyze the ester bond at the sn-2 position of membrane glycerophospholipids, generating free arachidonic acid. This acid is metabolized in a complex series of reactions involving COX or lipoxigenases (LOX), generating pro-inflammatory eicosanoids. TGase-catalyzed post-translational modifications activate sPLA2, potentially increasing eicosanoid production during acute inflammation. The new recombinant peptides contain a pro-elafin sequence that inhibits TGase and an antiflammin sequence that inhibits sPLA2. Thus they prevent TGase-induced sPLA2 activation.
