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24 sentences in this article containing lipoprotein Abstract
LPC is also a major phospholipid component of oxidized low-density lipoproteins (Ox-LDL) and is implicated as a critical factor in the atherogenic activity of Ox-LDL.
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LPC is derived from polar surface phosphatidylcholine (PC) of lipoproteins or from cell membrane-derived PC as a result of phospholipase A2 (PLA2) [8,9].
In plasma most of the circulating LPC is likely bound to albumin, representing 5–20% of total phospholipids [26], but some is associated with lipoprotein particles, where it comprises 1–5% of the total PC content of LDL particles [34].
The cell specific effects are summarized in Table 4 . 5 Atherogenic disease association of LPC and pharmacological aspects In vivo, LPC is claimed to be an important component of Ox-LDL [55,56] which is increased 5-fold in Ox-LDL compared to normal LDL and 7-fold in oxidized lipoprotein (a) (Lp(a)) compared to normal Lp(a).
Ox-LDL and oxidized Lp(a) induce apoptosis via oxidative stress which promotes atherogenesis [57].
Among the sPLA2 enzymes groups IIa, V and X are highly expressed in human atherosclerotic lesions where the various groups have overlapping and dissimilar potential roles in atherosclerosis and lipoprotein metabolism [61].
Concerning the role of lipoproteins as physiologic substrates of these three enzymes, sPLA2-V and X are considerably more active than sPLA2-IIA, an acute phase protein [65], to hydrolyze PC in HDL with no oxidation or modification of apolipoprotein A–I [66].
Furthermore, the interaction of apolipoprotein B containing lipoproteins with arterial proteoglycans in the intima is believed to be an important component of their atherogenicity [67].
In the extracellular intima sPLA2-V and X in contrast to sPLA2-IIa can be better suited for acting on apoliporotein B lipoproteins entrapped in this space [62] and LDL modified by sPLA2-V and X induce both foam cell formation [68]. sPLA2-IIa and V activity lead to fusion and enhanced binding of modified lipoproteins to extracellular proteoglycans that increase extracellular deposition of cholesterol-rich modified lipoproteins [69].
All these characteristics lead to the fact that sPLA2 enzymes have become a promising therapeutic target. 5.2 Lipoprotein-associated phospholipase A2 (Lp-PLA2) Lp-PLA2, also known as platelet activating factor acetylhydrolase or type VIIA PLA2, is a calcium-independent phospholipase predominantly synthesized by macrophages.
The biology of Lp-PLA2 is discussed in detail in a review article by Stafforini et al. [70].
In plasma Lp-PLA2 is bound to LDL and HDL lipoproteins with a greater affinity for the polar surface of LDL particles, particularly electronegative small LDL particles that have been minimally oxidatively modified [61].
Through hydrolysis of Ox-LDL particles, Lp-PLA2 generates two proinflammatory mediators, LPC and oxidized fatty acids, which activate redox-sensitive inflammatory pathways [71].
The products of Lp-PLA2 activity have been identified in human atherosclerotic vessel wall [72].
An overview of more than 25 published prospective epidemiologic studies showing an association of elevated Lp-PLA2 and higher cardiovascular risk is presented by recent reviews [64,73,74].
Lp-PLA2 appears to be highly specific for vascular inflammation such that it appears to be unaffected by common infections or arthritis, and it has low biologic variability, similar to lipids [74].
The level of Lp-PLA2 is independent of traditional risk factors, BMI and insulin resistance because Lp-PLA2 is produced by macrophages and foam cells in atherosclerotic plaques unlike systemic inflammatory markers, which may be produced by the liver in response to cytokines produced in mesenteric adipose tissue [74].
Lp-PLA2 is also incremental to high sensitivity C-reactive protein in risk assessment [73].
However, Lp-PLA2, unlike C-reactive protein and other biomarkers, is not recommended for general population screening.
But, once a patient is determined to be at intermediate or high cardiovascular risk, elevated Lp-PLA2 might be used to move the patient to the next higher risk category, and low Lp-PLA2 might increase confidence that the patient is optimally treated or at lower risk [73].
Further selective PLA2 inhibitors have to be analyzed in randomized clinical trials and currently two specific inhibitors for Lp-PLA2 and sPLA2 are under evaluation [61].
Recently a review about PLA2 inhibitors was published by Rosenson et al. [61] showing that sPLA2 inhibition reduces LDL cholesterol levels, and both Lp-PLA2 and sPLA2 inhibitors mitigate inflammatory processes.
An emerging field of LPC based drug target development in atherosclerosis will certainly be inhibitors of the phospholipase A2 superfamily which serve as potential targets of therapy to reduce cardiovascular events as they are involved in lipoprotein modification, retention and oxidation; and activation of vascular and systemic inflammatory responses [61].
Together with Lp-PLA2 as a biomarker the final aim of preventive therapies might be fulfilled to match the intensity of treatment to individual patient risk.
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