Production of AA by iPLA2 upon FCGR activation

Stable Identifier
Reaction [omitted]
Homo sapiens
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Several members of phospholipase A (PLA) are involved in phagocytosis. Macrophages express three classes of PLA2: secreted Ca-dependent (sPLA2), cytosolic Ca-dependent (cPLA2) and cytosolic Ca-independent (iPLA2) of which iPLA2 is involved in FCGR mediated arachidonic acid (AA) production. Aggregation of FCGR triggers phosphorylation and membrane translocation of iPLA2. Protein kinase C (PKC), ERK and p38MAPK seems to regulate iPLA2 in monocytes, neutrophils and macrophages. Phosphorylated iPLA2 then mediates production of AA and lysoophospholipids from phosphatidylcholine. iPLA2 inhibitors (bromoenol lactone) block AA release and phagocytosis which can be restored upon addition of exogenous AA, suggesting a critical role for iPLA2 in FCGR phagocytosis. Release of AA by activated iPLA2 changes the physical characteristic of the membrane which may facilitate pseudopod extension (Lennartz et al. 1993, Virgilio FD et al. 1988; Karimi K et al. 1999).
Literature References
PubMed ID Title Journal Year
10380910 Protein kinase C and a calcium-independent phospholipase are required for IgG-mediated phagocytosis by Mono-Mac-6 cells

Lennartz, MR, Gemmill, TR, Karimi, K

J Leukoc Biol 1999
3346321 Fc receptor-mediated phagocytosis occurs in macrophages at exceedingly low cytosolic Ca2+ levels

Silverstein, SC, Greenberg, S, Meyer, BC, Di Virgilio, F

J Cell Biol 1988
8228618 Immunoglobulin G-mediated phagocytosis activates a calcium-independent, phosphatidylethanolamine-specific phospholipase

Lennartz, MR, Brown, EJ, Bromley, FA, Lefkowith, JB

J Leukoc Biol 1993
Catalyst Activity

hydrolase activity of PLA2G6 [cytosol]

Orthologous Events
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