Rapid reduction and removal of HDL- but not LDL-associated cholesteryl ester hydroperoxides by rat liver perfused <i>in situ</i>

Christison, J.; Karjalainen, Ari; Brauman, J; Bygrave, Fyfe L.; Stocker, Roland

doi:10.1042/bj3140739

Cited by 78 publications

(43 citation statements)

References 29 publications

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“…Thus, the accumulation of oxidised lipids in HDL most probably results not only from their transfer from LDL but also from remnant triglyceride-rich lipoproteins and/or arterial wall cells, mediated in part by lipid transfer proteins (Christison et al 1995). Subsequently, LOOHs and their corresponding hydroxides can be rapidly removed from HDL via scavenger receptor class B-I (SR-BI)-mediated selective uptake by the liver (Christison et al 1996). This pathway may significantly contribute to the removal of toxic, oxidised lipids from the body.…”

Section: Mechanisms Of Protectionmentioning

confidence: 99%

Functionality of HDL: Antioxidation and Detoxifying Effects

Karlsson

Kontush

James

2014

Handbook of Experimental Pharmacology

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Section: Mechanisms Of Protectionmentioning

confidence: 99%

Functionality of HDL: Antioxidation and Detoxifying Effects

Karlsson

Kontush

James

2014

Handbook of Experimental Pharmacology

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“…Thus, cholesteryl ester transfer protein (CETP) transfers oxidized lipids from low density lipoproteins (LDL) to HDL (7), and HDL carries the majority of cholesteryl ester hydroperoxides (CE-OOH, the first and major products formed during lipoprotein oxidation) in human plasma (5). In addition, CE-OOH and cholesteryl ester hydroxides (CE-OH) in HDL, but not LDL, are removed rapidly via selective uptake by liver parenchymal cells in vitro (6) and by perfused liver in situ (8). This uptake is associated with cellular detoxification of CE-OOH (6) and is more rapid than that of the corresponding nonoxidized cholesteryl esters (CE) (6,8).…”

Section: High Density Lipoproteins (Hdl)mentioning

confidence: 99%

“…In addition, CE-OOH and cholesteryl ester hydroxides (CE-OH) in HDL, but not LDL, are removed rapidly via selective uptake by liver parenchymal cells in vitro (6) and by perfused liver in situ (8). This uptake is associated with cellular detoxification of CE-OOH (6) and is more rapid than that of the corresponding nonoxidized cholesteryl esters (CE) (6,8). Furthermore, CE-OH are also rapidly removed from HDL via hepatic clearance in vivo (9), and this is associated with biliary secretion of the CE-OH-derived cholesterol (9), indicating that oxidation of the fatty acid moiety of CE may aid the elimination of cholesterol from the body.…”

Section: High Density Lipoproteins (Hdl)mentioning

confidence: 99%

Oxidation of Methionine Residues to Methionine Sulfoxides Does Not Decrease Potential Antiatherogenic Properties of Apolipoprotein A-I

Panzenboeck¹,

Kritharides²,

Raftery³

et al. 2000

Journal of Biological Chemistry

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The initial stage of oxidation of high density lipoproteins (HDL) is accompanied by the lipid hydroperoxidedependent, selective oxidation of two of the three Met residues of apolipoprotein A-I (apoA-I) to Met sulfoxides (Met(O)). Formation of such selectively oxidized apoA-I (i.e. apoA-I ؉32 ) may affect the antiatherogenic properties of HDL, because it has been suggested that Met 86 and Met 112 are important for cholesterol efflux and Met 148 is involved in the activation of lecithin:cholesterol acyl transferase (LCAT). We therefore determined which Met residues were oxidized in apoA-I ؉32 and how such oxidation of apoA-I affects its secondary structure, the affinity for lipids, and its ability to remove lipids from human macrophages. We also assessed the capacity of discoidal reconstituted HDL containing apoA-I ؉32 to act as substrate for LCAT, and the dissociation of apoA-I and apoA-I ؉32 from reconstituted HDL. Met 86 and Met 112 were present as Met(O), as determined by amino acid sequencing and mass spectrometry of isolated peptides derived from apoA-I ؉32 . Selective oxidation did not alter the ␣-helicity of lipid-free and lipid-associated apoA-I as assessed by circular dichroism, and the affinity for LCAT was comparable for reconstituted HDL containing apoA-I or apoA-I ؉32 . Cholesteryl ester transfer protein mediated the dissociation of apoA-I more readily from reconstituted HDL containing apoA-I ؉32 than unoxidized apoA-I. Also, compared with native apoA-I, apoA-I ؉32 had a 2-to 3-fold greater affinity for lipid (as determined by the rate of clearance of multilamellar phospholipid vesicles) and its ability to cause efflux of [ 3 H]cholesterol, [ 3 H]phospholipid, and [ 14 C]␣-tocopherol from lipid-laden human monocyte-derived macrophages was significantly enhanced. By contrast, no difference was observed for cholesterol and ␣-tocopherol efflux to lipid-associated apolipoproteins. Together, these results suggest that selective oxidation of Met residues enhances rather than diminishes known antiatherogenic activities of apoA-I, consistent with the overall hypothesis that detoxification of lipid hydroperoxides by HDL is potentially antiatherogenic.

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“…HDL has a protective role against atherosclerosis: it removes lipid peroxides (LPOs) and cholesterol from oxidized LDL (9,10) and from cell membranes through the reverse cholesterol transport pathway (11,12). Once LPOs are absorbed by HDL, they are either transported to the liver, where they are detoxified and excreted into the bile (13)(14)(15), or they are reduced directly by HDL to hydroxylipids (16,17). At least two HDL-bound proteins are involved with LPO detoxification, paraoxonase (PON-1) (18,19) and apolipoprotein A-I (apoA-I) (20).…”

mentioning

confidence: 99%

Increased methionine sulfoxide content of apoA-I in type 1 diabetes

Brock

Jenkins

Lyons

et al. 2008

Journal of Lipid Research

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Cardiovascular disease is a major cause of morbidity and premature mortality in diabetes. HDL plays an important role in limiting vascular damage by removing cholesterol and cholesteryl ester hydroperoxides from oxidized low density lipoprotein and foam cells. Methionine (Met) residues in apolipoprotein A-I (apoA-I), the major apolipoprotein of HDL, reduce peroxides in HDL lipids, forming methionine sulfoxide [Met(O)]. We examined the extent and sites of Met(O) formation in apoA-I of HDL isolated from plasma of healthy control and type 1 diabetic subjects to assess apoA-I exposure to lipid peroxides and the status of oxidative stress in the vascular compartment in diabetes. Three tryptic peptides of apoA-I contain Met residues: Q 84 -M 86 -K 88 , W 108 -M 112 -R 116 , and L 144 -M 148 -R 149 . These peptides and their Met(O) analogs were identified and quantified by mass spectrometry. Relative to controls, Met(O) formation was significantly increased at all three locations (Met 86 , Met 112 , and Met 148 ) in diabetic patients. The increase in Met(O) in the diabetic group did not correlate with other biomarkers of oxidative stress, such as N : -malondialdehyde-lysine or N : -(carboxymethyl)lysine, in plasma or lipoproteins. The higher Met(O) content in apoA-I from diabetic patients is consistent with increased levels of lipid peroxidation products in plasma in diabetes. Using the methods developed here, future studies can address the relationship between Met(O) in apoA-I and the risk, development, or progression of the vascular complications of diabetes.-Brock, J.

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Rapid reduction and removal of HDL- but not LDL-associated cholesteryl ester hydroperoxides by rat liver perfused in situ

Cited by 78 publications

References 29 publications

Functionality of HDL: Antioxidation and Detoxifying Effects

Functionality of HDL: Antioxidation and Detoxifying Effects

Oxidation of Methionine Residues to Methionine Sulfoxides Does Not Decrease Potential Antiatherogenic Properties of Apolipoprotein A-I

Increased methionine sulfoxide content of apoA-I in type 1 diabetes

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