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The Ca 2+ -independent phospholipases A 2 (iPLA 2 s) are part of a diverse family of PLA 2 s, manifest activity in the absence of Ca 2+ , are ubiquitous, and participate in a variety of biological processes. Among the iPLA 2 s, the cytosolic iPLA 2 β has received considerable attention and ongoing studies from various laboratories suggest that dysregulation of iPLA 2 β can have a profound impact on the onset and/or progression of many diseases (e.g., cardiovascular, neurological, metabolic, autoimmune). Therefore, appropriate approaches are warranted to gain a better understanding of the role of iPLA 2 β in vivo and its contribution to pathophysiology. Given that iPLA 2 β is very labile, its basal expression is low in a number of cell systems, and that crystal structure of iPLA 2 β is not yet available, careful and efficient protocols are needed to appropriately assess iPLA 2 β biochemistry, dynamics, and membrane association. Here, step-by-step details are provided to (a) measure iPLA 2 β-specific activity in cell lines or tissue preparations (using a simple radiolabel-based assay) and assess the impact of stimuli and inhibitors on resting- and disease-state iPLA 2 β activity, (b) purify the iPLA 2 β to near homogeneity (via sequential chromatography) from cell line or tissue preparations, enabling concentration of the enzyme for subsequent analyses (e.g., proteomics), and (c) employ hydrogen/deuterium exchange mass spectrometry analyses to probe both the structure of iPLA 2 β and dynamics of its association with the membranes, substrates, and inhibitors.

Analyses of Calcium-Independent Phospholipase A2beta (iPLA2β) in Biological Systems