| Abstract: | The structure of low density lipoprotein (LDL) particles and, particularly, the enzymatic and oxidative modifications of their surface is crucial in the initiation of atherosclerosis. Due to the structural complexity of LDL, there is a lack of suitable methods for dynamic follow-up studies of the molecular mechanisms in native and modified particles in physiological conditions. Here, we report that phosphatidylcholine (PC), lysophosphatidylcholine (lyso-PC), and sphingomyelin (SM) can all be identified and quantified in LDL particles by (1)H NMR spectroscopy at 800 MHz. The signal assignment for the lyso-PC is novel and we illustrate the applicability of the methodology in the case of lipid peroxidation that is generally considered as one of the key proatherogenic modifications of LDL. It was found, somewhat surprisingly, that the LDL-associated phospholipase A(2) is activated in the very beginning of the formation of PC-hydroperoxides. The (patho)physiological rationale of the resulting lyso-PC generation is also briefly discussed. |
