PLA2G2D Protein, Human (His-SUMO)

PLA2G2D is a secretory calcium-dependent phospholipase A2 with a primary focus on extracellular lipids, showcasing anti-inflammatory and immunosuppressive functions. This protein hydrolyzes the ester bond of the fatty acyl group at the sn-2 position of phospholipids, displaying a preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. Particularly in draining lymph nodes, it selectively hydrolyzes diacyl and alkenyl forms of phosphatidylethanolamines, releasing omega-3 polyunsaturated fatty acids like eicosapentaenoate and docosahexaenoate. These compounds act as precursors for the synthesis of anti-inflammatory lipid mediators known as resolvins. During the resolution phase of acute inflammation, PLA2G2D drives the synthesis of resolvin D1 derived from docosahexaenoate, suppressing dendritic cell activation and the T-helper 1 immune response. Beyond its catalytic activity, PLA2G2D, via mechanisms independent of its enzymatic functions, promotes the differentiation of regulatory T cells (Tregs) and contributes to maintaining immune tolerance. Additionally, it may play a role in lipid remodeling of cellular membranes and participate in the generation of lipid mediators crucial for pathogen clearance, exhibiting bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids in the bacterial membrane.