کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1945022 | 1053249 | 2009 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A possible role of lysophospholipids produced by calcium-independent phospholipase A2 in membrane-raft budding and fission A possible role of lysophospholipids produced by calcium-independent phospholipase A2 in membrane-raft budding and fission](/preview/png/1945022.png)
Phospholipase A2 (PLA2) not only plays a role in the membrane vesiculation system but also mediates membrane-raft budding and fission in artificial giant liposomes. This study aimed to demonstrate the same effects in living cells. Differentiated Caco-2 cells were cultured on filter membranes. MDCK cells were challenged with Influenza virus. The MDCK cultures were harvested for virus titration with a plaque assay. Alkaline phosphatase (ALP), a membrane-raft associated glycosylphosphatidylinositol (GPI)-anchored protein, was 70% released by adding 0.2 mmol/l lysophosphatidylcholine, which was abolished by treatment with a membrane-raft disrupter, methyl-β-cyclodextrin. Activation of calcium-independent PLA2 (iPLA2) by brefeldin A increased the apical release of ALP by approximately 1.5-fold (p < 0.01), which was blocked by PLA2 inhibitor bromoenol lactone (BEL). BEL also reduced Influenza virus production into the media (< 10%) in the MDCK culture. These results suggest that cells utilize inverted corn-shaped lysophospholipids generated by PLA2 to modulate plasma membrane structure and assist the budding of raft-associated plasma membrane particles, which virus utilizes for its budding. Brush borders are enriched with membrane-rafts and undergo rapid turnover; thus, PLA2 may be involved in the regulatory mechanism in membrane dynamism. Further, iPLA2 may provide a therapeutic target for viral infections.
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1788, Issue 10, October 2009, Pages 2222–2228