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Acrolein Modifies Apolipoprotein A‐I in the Human Artery Wall
Author(s) -
SHAO BAOHAI,
O'BRIEN KEVIN D.,
MCDONALD THOMAS O.,
FU XIAOYUN,
ORAM JOHN F.,
UCHIDA KOJI,
HEINECKE JAY W.
Publication year - 2005
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1333.046
Subject(s) - acrolein , chemistry , lysine , cholesterol , apolipoprotein b , biochemistry , lipoprotein , amino acid , catalysis
A bstract : Carbonyl stress is implicated in accelerated vascular disease, but little is known about the factors that control the reactions of carbonyls with proteins. Acrolein is a reactive carbonyl generated by the oxidation of lipids and amino acids. It also forms during cigarette smoking. We therefore investigated the possibility that acrolein might react with apolipoprotein A‐I (apoA‐I), the major protein of high‐density lipoprotein (HDL), which plays a critical role in mobilizing cholesterol from artery wall macrophages. Tandem mass spectrometric analysis demonstrated that lysine residues were the only amino acids in apoA‐I that were modified by acrolein. Immunohistochemical studies with a monoclonal antibody revealed that acrolein adducts colocalized with apoA‐I in human atherosclerotic lesions. Moreover, the ability of apoA‐I to remove cholesterol from cultured cells was impaired after exposure to acrolein, suggesting that the carbonyl might interfere with apoA‐I's normal function of promoting cholesterol efflux from artery wall cells. Our observations suggest that acrolein may interfere with normal HDL cholesterol transport by modifying apoA‐I. This structural damage might play a critical role in atherogenesis by impairing cholesterol removal from artery wall cells.