Structural Elements Of Lipidic Inhibitors Of Phospholipase A2

ASU Author/Contributor (non-ASU co-authors, if there are any, appear on document)
James Foley (Creator)
Appalachian State University (ASU )
Web Site:
Mark Venable

Abstract: Phospholipases A2 (PLA2) are a family of enzymes that release fatty acids from phospholipids and play varied and important roles in the biology of all organisms. Secreted phospholipases A2 (sPLA2) are the largest subfamily of PLA2. sPLA2 expression levels have been positively correlated to the severity of multiple inflammatory diseases. Many sPLA2 inhibitors have been developed and tested, however, none have shown to be clinically effective and specific against individual enzymes within this family. In this study we discovered an inhibition phenomenon in a widely used sPLA2 enzymatic assay. The enzymatic rate of reaction of sPLA2 group IIA from Crotalus adamanteus was significantly reduced when negatively charged lipids were added at very low mole fractions. This inhibition phenomenon did not occur if the lipid added was either positively charged or polar but neutral. These results suggest that the standard assay should be re-optimized to prevent this nonspecific inhibition and that the literature may need to be reevaluated.

Additional Information

Foley, J. (2018). "Structural Elements Of Lipidic Inhibitors Of Phospholipase A2." Unpublished Master’s Thesis. Appalachian State University, Boone, NC.
Language: English
Date: 2018
Phospholipases, sPLA2, Enzymatic assay, PLA2 group IIA

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