Inhibition of lipoprotein-associated phospholipase A2 diminishes the death-inducing effects of oxidised LDL on human monocyte-macrophages.

@article{Carpenter2001InhibitionOL,
  title={Inhibition of lipoprotein-associated phospholipase A2 diminishes the death-inducing effects of oxidised LDL on human monocyte-macrophages.},
  author={Keri Carpenter and Ian F. Dennis and Iain R Challis and David Pj Osborn and Colin H. Macphee and David S. Leake and Mark J Arends and Malcolm J Mitchinson},
  journal={FEBS letters},
  year={2001},
  volume={505 3},
  pages={357-63}
}
The death of macrophages contributes to atheroma formation. Oxidation renders low-density lipoprotein (LDL) cytotoxic to human monocyte-macrophages. Lipoprotein-associated phospholipase A2 (Lp-PLA2), also termed platelet-activating factor acetylhydrolase, hydrolyses oxidised phospholipids. Inhibition of Lp-PLA2 by diisopropyl fluorophosphate or Pefabloc (broad-spectrum serine esterase/protease inhibitors), or SB222657 (a specific inhibitor of Lp-PLA2) did not prevent LDL oxidation, but… CONTINUE READING

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