​Secretory phospholipase A₂ (sPLA₂) catalyzes the hydrolysis of sn-2 acyl bond of membrane-bound phospholipids yielding a free fatty acid and a lysophospholipid. The sPLA₂ family contains 10 catalytically active (IB, IIA, IID, IIE, IIF, III, V, X, and XIIA) and one inactive isoform (XIIB) in mammals. This family of enzymes are disulfide-rich, low molecular weight, Ca²⁺-requiring lipolytic enzymes with a His-Asp catalytic dyad. Individual mammalian sPLA₂s have distinct enzymatic properties and display distinct tissue expression patterns, suggesting that each enzyme acts on a distinct phospholipid membrane. 

Here we describe the comparative activity of sPLA₂-IIA, sPLA₂-IID, sPLA₂-IIE, sPLA₂-V, and sPLA₂-X in the presence and absence of inhibitors. 

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To cite this poster: De Silva, A.J., Muzzarelli, K.M., Good, P.D., et al. Biochemical and biophysical characterization of human secretory phospholipases. Poster presented at: 20^th Annual Discovery on Target Conference; September 25-28, 2023. Boston, MA.