Inflammation
Lp(a) carries an enzyme that degrades oxidized phospholipids, a review of lipoprotein-associated phospholipase A2 (Arterioscler Thromb Vasc Biol 2007)
Original title: New insights into the role of lipoprotein(a)-associated lipoprotein-associated phospholipase A2 in atherosclerosis and cardiovascular disease
This review by Tsimikas, Tsironis and Tselepis examines lipoprotein-associated phospholipase A2, an enzyme carried on Lp(a) that degrades oxidized phospholipids (OxPLs), substrates containing oxidatively fragmented residues linked to vascular inflammation and atherosclerosis. Plasma OxPL levels on apolipoprotein B-100 correlate with coronary, carotid and peripheral arterial disease, and are strongly correlated with and preferentially sequestered on Lp(a), making them potentially subject to degradation by Lp(a)-associated phospholipase A2. The review focuses on this Lp(a)-bound enzyme characteristics and discusses its possible role in light of emerging evidence that OxPLs are preferentially carried by Lp(a), potentially contributing to its heightened atherogenicity.
Original abstract
Lipoprotein(a) [Lp(a)] plays an important role in atherosclerosis. The biological effects of Lp(a) have been attributed either to apolipoprotein(a) or to its low-density lipoprotein-like particle. Lp(a) contains platelet-activating factor acetylhydrolase, an enzyme that exhibits a Ca2+-independent phospholipase A2 activity and is complexed to lipoproteins in plasma; thus, it is also referred to as lipoprotein-associated phospholipase A2. Substrates for lipoprotein-associated phospholipase A2 include phospholipids containing oxidatively fragmented residues at the sn-2 position (oxidized phospholipids; OxPLs). OxPLs may play important roles in vascular inflammation and atherosclerosis. Plasma levels of OxPLs present on apolipoprotein B-100 particles (OxPL/apolipoprotein B) are correlated with coronary artery, carotid, and peripheral arterial disease. Furthermore, OxPL/apolipoprotein B levels in plasma are strongly correlated with Lp(a) levels, are preferentially sequestered on Lp(a), and thus are potentially subjected to degradation by the Lp(a)-associated lipoprotein-associated phospholipase A2. The present review article focuses specifically on the characteristics of the lipoprotein-associated phospholipase A2 associated with Lp(a) and discusses the possible role of this enzyme in view of emerging data showing that OxPLs in plasma are preferentially sequestered on Lp(a) and may significantly contribute to the increased atherogenicity of this lipoprotein.
Summary written by lp-a.org from the published abstract; figures as published. Page updated 18 August 2026. Methods.