Abstract
Cytosolic phospholipase A2‐alpha (cPLA2α) has been a protein of interest for over 16 years because of its presence in inflammatory diseases, including asthma and rheumatoid arthritis. cPLA2α is composed of two domains, a catalytic domain that generates arachidonic acid by cleaving phospholipids, and a C2 domain responsible for anchoring the protein to the lipid membrane. Ceramide‐1‐phosphate (C1P) is a sphingolipid found in inflamed tissue that previous research demonstrates to significantly upregulate the activity of cPLA2α. cPLA2α's C2 domain contains a debated binding site for C1P, and the goal of this study is to culture 15N‐tagged cPLA2α C2 domain for structural investigation by NMR. In addition, binding studies utilizing large unilamellar vesicles (LUV) and increasing concentrations of C1P will help us construct a binding curve, thus better understand C2 binding to C1P. Preliminary results of the NMR study and LUV assay support our hypothesis that C1P and cPLA2α interact. This interaction is likely significant in inflammatory disease processes and is potentially a novel drug target. Funding provided by American Heart Association SDG0735350N.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
