Lecithin : cholesterol acyltransferase reduces the adverse effects of oxidized low-density lipoprotein while incurring damage itself

In this study, we tried to determine (a) whether there is an permanent effe ct of oxLDL on the LCAT molecule and its activator lipoprotein apoA-I, and (b) the fate of oxLDL after its exposure to LCAT and apoA-I. Purified LCAT and LDL/oxLDL was incubated at 37 degreesC for 1h, and separated by gel-per meation chromatography. Its activity was significantly less (30% less) afte r separating from oxLDL compared to that of LDL. Cofactor activity of isola ted apoA-I (incubated with LDL/oxLDL) was found affected by oxLDL. These re sults indicate modification of the LCAT and apoA-1 molecule. But LCAT was f ound more affected compared to apoA-I in terms of LCAT activity. We are als o reporting a novel function of LCAT. It was found to reduce the adverse ef fects of oxLDL, for example, ability to affect the LCAT activity and TBARS value. This ability of LCAT to repair oxLDL was dose-dependent. But there w as no change in its REM values or fluorescence intensity.