The PLA2 substrate DBPC, is a sensitive probe for a continuous fluorogenic detection applicable to both /in vitro/ and cell-based /in situ/ screening assays. Phospholipase A2 (PLA2) is the enzyme which cleaves phospholipids to produce lysophospholipids and free fatty acids. The PLA2 family of enzymes is known to be at least 10 distinct members. sPLA2-V and sPLA2-X are selectively expressed in human airway epithelium and sPLA2-X in various immune cells. The basal expression of a third enzyme, sPLA2-IIA is low but becomes highly expressed during inflammation and sepsis. This enzyme has become associated with allergic rhinitis, rheumatoid arthritis, septic shock and ARDS. PLA2-IIA represents a target for the treatment of inflammatory disease.
Featured in Publications
1) Zhao, X., D. Wang, et al. (2006). "Caspase-3-dependent activation of calcium-independent phospholipase A2 enhances cell migration in non-apoptotic ovarian cancer cells." J Biol Chem 281(39): 29357-68.
2) Manna, D., W. Cho, et al. (2007). Real-Time Cell Assays of Phospholipase A2s Using Fluorogenic Phospholipids. Methods in Enzymology, Academic Press. Volume 434: 15.
3) Cai, Q., Z. Zhao, et al. (2012). "Elevated and secreted phospholipase A2 activities as new potential therapeutic targets in human epithelial ovarian cancer." The FASEB Journal 26(8): 3306-3320.