| First Author | Yoda E | Year | 2014 |
| Journal | PLoS One | Volume | 9 |
| Issue | 10 | Pages | e109409 |
| PubMed ID | 25313821 | Mgi Jnum | J:223561 |
| Mgi Id | MGI:5649500 | Doi | 10.1371/journal.pone.0109409 |
| Citation | Yoda E, et al. (2014) Group VIB calcium-independent phospholipase A2 (iPLA2gamma) regulates platelet activation, hemostasis and thrombosis in mice. PLoS One 9(10):e109409 |
| abstractText | In platelets, group IVA cytosolic phospholipase A2 (cPLA2alpha) has been implicated as a key regulator in the hydrolysis of platelet membrane phospholipids, leading to pro-thrombotic thromboxane A2 and anti-thrombotic 12-(S)-hydroxyeicosatetranoic acid production. However, studies using cPLA2alpha-deficient mice have indicated that other PLA2(s) may also be involved in the hydrolysis of platelet glycerophospholipids. In this study, we found that group VIB Ca2+-independent PLA2 (iPLA2gamma)-deficient platelets showed decreases in adenosine diphosphate (ADP)-dependent aggregation and ADP- or collagen-dependent thromboxane A2 production. Electrospray ionization mass spectrometry analysis of platelet phospholipids revealed that fatty acyl compositions of ethanolamine plasmalogen and phosphatidylglycerol were altered in platelets from iPLA2gamma-null mice. Furthermore, mice lacking iPLA2gamma displayed prolonged bleeding times and were protected against pulmonary thromboembolism. These results suggest that iPLA2gamma is an additional, long-sought-after PLA2 that hydrolyzes platelet membranes and facilitates platelet aggregation in response to ADP. |
