||Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids.
|Gene References into Functions
- Stable isotope kinetics revealed that in non-failing human hearts, cPLA2zeta metabolically channels arachidonic acid into EETs, whereas in failing hearts, increased iPLA2gamma activity channels AA into toxic HETEs. These results mechanistically identify the sequelae of pathological remodeling of human mitochondrial phospholipases in failing myocardium. PMID: 29158256
- iPLA2gamma plays an important role in in vivo Thromboxane A2 production accompanied by thrombus formation. PMID: 25313821
- iPLA2gamma plays a cardioprotective role during the acute stage of Chagas' disease. PMID: 23429536
- Thus, complement-mediated activation of iPLA(2)gamma is mediated via ERK and p38 pathways, and phosphorylation of Ser-511 and/or Ser-515 plays a key role in the catalytic activity and signaling of iPLA(2)gamma. PMID: 23258543
- These results suggest distinct roles for iPLA2beta and iPLA2gamma in cellular homeostasis and signaling, a functional link between peroxisomal AA release and eicosanoid generation, and a potential contribution of iPLA2gamma to tumorigenesis. PMID: 15695510
- iPLA2 activation is not sufficient for SOCE activation. iPLA2 may regulate basal phosphoinositide metabolism PMID: 18680539
|Involvement in disease
||Mitochondrial myopathy with lactic acidosis (MMLA)
||Endoplasmic reticulum membrane, Single-pass membrane protein, Golgi apparatus membrane, Single-pass membrane protein, Cytoplasm, perinuclear region
||Expressed in parenchymal tissues including heart, skeletal muscle, placenta, brain, liver and pancreas. Also expressed in bronchial epithelial cells and kidney. Highest expression is observed in skeletal muscle and heart.