Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I.

@article{Shao2006MyeloperoxidaseIA,
  title={Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I.},
  author={Baohai Shao and Michael N Oda and Constanze Bergt and Xiaoyun Fu and Pattie S. Green and Nathan Brot and John F. Oram and Jay W. Heinecke},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 14},
  pages={
          9001-4
        }
}
High density lipoprotein (HDL) isolated from human atherosclerotic lesions and the blood of patients with established coronary artery disease contains elevated levels of 3-chlorotyrosine. Myeloperoxidase (MPO) is the only known source of 3-chlorotyrosine in vivo, indicating that MPO oxidizes HDL in humans. We previously reported that Tyr-192 is the major site that is chlorinated in apolipoprotein A-I (apoA-I), the chief protein in HDL, and that chlorinated apoA-I loses its ability to promote… CONTINUE READING
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