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Papers In Press, published online ahead of print January 23, 2002
Medicine, University of Utah, Salt Lake City, UT 84103-5330
Corresponding Author: tom.mcintyre{at}hmbg.utah.edu
LDL oxidation and monocyte infiltration of the vessel wall underlie atherogenesis. These cells express cyclooxygenase-2, but the way oxidized LDL stimulates cyclooxygenase-2 transcription is unknown. Oxidized LDL, oxidatively-fragmented phospholipids isolated from oxidized LDL, a synthetic oxidized alkyl phospholipid (azPC) that is a potent PPAR
J. Biol. Chem, 10.1074/jbc.M109546200
Submitted on October 3, 2001
Revised on January 9, 2002
Accepted on January 23, 2002
Cyclooxygenase-2 is induced in monocytes by PPAR
and oxidized alkyl phospholipids from oxidized LDL
agonist, or the PPAR agonist rosiglitazone all induced cyclooxygenase-2 expression and enhanced PGE2 secretion in primary human monocytes. The cyclooxygenase-2 inhibitor NS398 blocked PPAR-induced PGE2 secretion. Phospholipase A1 and A2 digestion shows oxidized alkyl phospholipids, and not oxidized fatty acids, were the relevant agonists. The upstream PPAR-responsive element (PPRE) of cyclooxygenase-2 was required for induction of a luciferase reporter by oxidized phospholipids, azPC and rosiglitazone, and a (Cox-2 PPRE)3-luciferase reporter was responsive to these PPAR agonists. Circulating human monocytes do not contain PPAR, but PPAR was rapidly (<4h) induced in monocytes upon ligation of surface ICAM-3, but not P-selectin glycoprotein-1 even though both interactions prime cytokine secretion. Cyclooxygenase-2 induction by oxidized phospholipids only occurred in monocytes containing PPAR. Thus PPAR was rapidly induced in primary monocytes by appropriate outside-in signaling, sensitizing them to previously undetectable agonists in oxidized LDL. Cyclooxygenase-2 and PGE2 secretion are induced —not inhibited— by selective PPAR agonists that includes oxidatively-fragmented phospholipids in oxidized LDL.
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