[HTML][HTML] Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein AI
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 AI (apoA-I), the chief protein in HDL, and that
chlorinated apoA-I loses its ability to promote cholesterol efflux from cells by the ATP-binding …
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 AI (apoA-I), the chief protein in HDL, and that
chlorinated apoA-I loses its ability to promote cholesterol efflux from cells by the ATP-binding …