{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nGroup V secretory phospholipase A₂, encoded by the PLA2G5 gene, is widely expressed in innate immune cells. In human neutrophils this enzyme is stored in both azurophilic and specific granules and is promptly secreted in response to bacterial peptides, where it hydrolyzes plasma membrane phospholipids to generate bioactive lipids that directly contribute to antibacterial defense—even though it does not significantly drive leukotriene B₄ production. Exogenously added PLA₂G5 in neutrophils and eosinophils liberates arachidonic acid from the outer plasma membrane, thereby triggering cytosolic phospholipase A₂ activation, elevating intracellular calcium, and promoting the synthesis of proinflammatory lipid mediators (e.g., LTB₄ and LTC₄). Moreover, in T cells and IL‑4–activated macrophages, PLA₂G5 contributes to the regulation of calcium entry and selective phospholipid metabolization, which in turn modulates downstream eicosanoid production and inflammatory signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the vasculature, PLA2G5 plays multifaceted roles in atherogenesis and cardiovascular pathology. By hydrolyzing phospholipids in low‐density lipoprotein particles, PLA₂G5 modifies LDL to yield products that promote macrophage foam cell formation—a critical step in plaque development. Genetic studies reveal that PLA2G5 polymorphisms are associated with altered lipid profiles (elevated LDL and total cholesterol, changes in oxidized LDL/LDL ratios) and premature coronary artery disease. In addition, PLA₂G5 modulates vascular smooth muscle cell proliferation and eicosanoid release, and its action toward oxidized phospholipids likely contributes to processes such as aortic valve calcification and myocardial injury."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nWithin the pulmonary compartment, PLA2G5 contributes both to innate antiviral defense and the modulation of inflammatory barrier function. Its catalytic activity impedes adenoviral entry by hydrolyzing plasma membrane phospholipids to generate lysophosphatidylcholine—a lipid product that retards endosomal uptake of the virus. In lung endothelial cells, inflammatory stimuli (e.g., lipopolysaccharide) upregulate PLA₂G5 expression, leading to cytoskeletal remodeling and disruption of intercellular junctions, which in turn increases vascular permeability. Furthermore, inducible expression of PLA₂G5 in airway macrophages is essential for the recruitment of effector T cells during Th2-mediated pulmonary inflammation, and its regulated clearance via autophagy appears to resolve inflammatory signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nGenetic studies have also linked PLA2G5 to ocular physiology. Mutations and biallelic variants in PLA2G5 have been identified in patients with benign familial fleck retina, a disorder characterized by widespread retinal lesions but without overt visual deficits. These findings suggest that PLA₂G5 plays an essential role in the phagocytosis of photoreceptor outer-segment discs by the retinal pigment epithelium, thereby maintaining retinal homeostasis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in inflammation and vascular biology, PLA2G5 is expressed in the liver and can influence coagulation pathways. It mediates a process known as EPCR encryption by altering the phospholipid composition of the endothelial protein C receptor, thereby impairing the binding and cytoprotective activity of activated protein C. Such events may contribute to a proinflammatory and prothrombotic state in diseases such as rheumatoid arthritis, while its hepatic expression is implicated in tissue injury associated with liver disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nEpigenetic regulation of PLA2G5 has been observed in various cancer cells. In multiple tumor cell lines, hypermethylation of distinct CpG sites in the PLA2G5 promoter is associated with reduced transcript levels. Notably, exogenous PLA₂G5 can diminish colony formation in certain cancer models, indicating that its expression may exert cell-type–dependent anti-tumorigenic effects."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent studies have highlighted that PLA2G5 is trafficked through cellular lipid rafts and internalized via a flotillin‑dependent pathway. This targeted internalization not only regulates its availability at the plasma membrane to prevent excessive phospholipid hydrolysis but also directs its intracellular signaling functions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Norbert Degousee, Farideh Ghomashchi, Eva Stefanski, et al. 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