Recombinant Mouse Calcium-dependent phospholipase A2 (Pla2g5)

Function

Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), preferentially releasing fatty acyl groups with a low degree of unsaturation such as oleoyl (C18:1) and linoleoyl (C18:2) groups (PubMed:14962950). Hydrolyzes low-density lipoprotein (LDL) phospholipids releasing unsaturated fatty acids that drive macrophage polarization toward an M2 phenotype (PubMed:14962950, PubMed:24910243). May act in an autocrine and paracrine manner. Contributes to lipid remodeling of cellular membranes at different subcellular locations and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of cardiolipin, a major component of the inner membrane of mitochondria and bacterial membranes (By similarity). Promotes phagocytosis of bacteria in macrophages through production of lysophosphatidylethanolamines (By similarity). Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing the phospholipids of the bacterial membrane (PubMed:11694541, PubMed:16407308). Promotes phagocytosis and killing of ingested fungi likely through controlling phagosome-lysosome fusion and phagosome maturation (PubMed:19342668). Plays a role in biosynthesis of cysteinyl leukotrienes (CysLTs) in myeloid cells (By similarity). In eosinophils, triggers perinuclear arachidonate release and LTC4 synthesis in a PLA2G4A-independent way (By similarity). In neutrophils, amplifies CysLTs biosynthesis initiated by PLA2G4A (By similarity). Promotes immune complex clearance in macrophages via stimulating synthesis of CysLTs, which act through CYSLTR1 to trigger phagocytosis (PubMed:20432503). May regulate antigen processing in antigen-presenting cells (PubMed:20817863). In pulmonary macrophages regulates IL33 production required for activation of group 2 innate lymphoid cells (PubMed:29346348). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity)

Subcellular Location

Secreted; Cell membrane; Cytoplasmic vesicle, phagosome; Recycling endosome; Golgi apparatus, cis-Golgi network; Golgi apparatus, trans-Golgi network

Tissue Specificity

Expressed in peritoneal macrophages (at protein level) (PubMed:16407308). Expressed in heart, skeletal muscle and white adipose tissue (PubMed:24910243)

Pathway

Lipid metabolism; leukotriene C4 biosynthesis

• Tischfield J.A. et al. Low-molecular-weight, calcium-dependent phospholipase A2 genes are linked and map to homologous chromosome regions in mouse and human. — Genomics (1996)
• Bingham C.O. III et al. Low molecular weight group IIA and group V phospholipase A(2) enzymes have different intracellular locations in mouse bone marrow-derived mast cells. — J. Biol. Chem. (1999)
• Koduri R.S. et al. Bactericidal properties of human and murine groups I, II, V, X, and XII secreted phospholipases A(2). — J. Biol. Chem. (2002)
• Wooton-Kee C.R. et al. Group V sPLA2 hydrolysis of low-density lipoprotein results in spontaneous particle aggregation and promotes macrophage foam cell formation. — Arterioscler. Thromb. Vasc. Biol. (2004)
• Balestrieri B. et al. Group V secretory phospholipase A2 translocates to the phagosome after zymosan stimulation of mouse peritoneal macrophages and regulates phagocytosis. — J. Biol. Chem. (2006)
• Balestrieri B. et al. Group V secretory phospholipase A2 modulates phagosome maturation and regulates the innate immune response against Candida albicans. — J. Immunol. (2009)
• Boilard E. et al. A novel anti-inflammatory role for secretory phospholipase A2 in immune complex-mediated arthritis. — EMBO Mol. Med. (2010)
• Giannattasio G. et al. Group V secretory phospholipase A2 reveals its role in house dust mite-induced allergic pulmonary inflammation by regulation of dendritic cell function. — J. Immunol. (2010)