Abstract:
:Nitrogen dioxide (NO2), an environmental oxidant, alters the plasma membrane structure and function of pulmonary artery endothelial cells through peroxidative injury. Because perioxidative injury can activate membrane phospholipases and alter phospholipid composition of membranes, we evaluated the effects of NO2 exposure on phospholipase A1 (PLA1), phospholipase A2 (PLA2), and diacylglycerol lipase (DG lipase) activities in pulmonary artery endothelial cell plasma, mitochondrial, and microsomal membranes. We also evaluated the effect of NO2 exposure on the phospholipid composition of plasma membranes of these cells. Exposure to 5 ppm NO2 for 48 hr resulted in a significant (p less than 0.01) increase in PLA1 activity in plasma membranes but not in mitochondrial or microsomal membranes of pulmonary artery endothelial cells, whereas PLA2 and DG lipase activities were comparable to controls in all membranes. As a result of PLA1 activation, the total phospholipid content of the plasma membranes of NO2-exposed cells was significantly (p less than 0.01) reduced compared to controls. Phosphatidylethanolamine (PE) content was reduced (p less than 0.05), whereas lyso-PE (LPE), a product of PLA1 hydrolysis of PE, as well as phosphatidylserine (PS) contents were increased (p less than 0.01 for both LPE and PS) in the plasma membranes of NO2-exposed cells. Incorporation of exogenous PS into pulmonary artery endothelial cells mimicked the stimulatory effect of NO2 on PLA1 activity. These results demonstrate that NO2 specifically reacts with the plasma membrane component of pulmonary artery endothelial cells, causing specific activation of PLA1. The NO2-induced increase of PS in the plasma membranes appears to be responsible for the specific activation of PLA1 in pulmonary artery endothelial cells.
journal_name
Toxicol Appl Pharmacoljournal_title
Toxicology and applied pharmacologyauthors
Sekharam KM,Patel JM,Block ERdoi
10.1016/0041-008x(91)90317-8subject
Has Abstractpub_date
1991-03-01 00:00:00pages
545-54issue
3eissn
0041-008Xissn
1096-0333journal_volume
107pub_type
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