High-density lipoprotein subpopulations as substrates for the transfer of cholesteryl esters to very-low-density lipoproteins

Lasunción, Miguel A.; Iglesias, Angel; Škottová, Nina; Orozco, Esther; Herrera, Emílio

doi:10.1042/bj2700441

Cited by 18 publications

(10 citation statements)

References 34 publications

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“…The consequences of this interaction on CETP activity are not well understood since it has been reported that these two HDL fractions support equivalent CETP activity when added to assays on a CE basis (54). However, here we observed that not only are HDL 2 and HDL 3 unique in their response to LTIP, these lipoproteins, when compared on an equivalent phospholipid bases, also supported very different CETP activities.…”

Section: Ltip Binding To Ldl Hdlcontrasting

confidence: 47%

Lipid Transfer Inhibitor Protein Defines the Participation of High Density Lipoprotein Subfractions in Lipid Transfer Reactions Mediated by Cholesterol Ester Transfer Protein (CETP)

Paromov

Morton

2003

Journal of Biological Chemistry

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Cholesterol ester transfer protein (CETP) moves triglyceride (TG) and cholesteryl ester (CE) between lipoproteins. CETP has no apparent preference for high (HDL) or low (LDL) density lipoprotein as lipid donor to very low density lipoprotein (VLDL), and the preference for HDL observed in plasma is due to suppression of LDL transfers by lipid transfer inhibitor protein (LTIP).Given the heterogeneity of HDL, and a demonstrated ability of HDL subfractions to bind LTIP, we examined whether LTIP might also control CETP-facilitated lipid flux among HDL subfractions. CETP-mediated CE transfers from [ 3 H]CE VLDL to various lipoproteins, combined on an equal phospholipid basis, ranged 2-fold and followed the order: HDL 3 > LDL > HDL 2 . LTIP inhibited VLDL to HDL 2 transfer at one-half the rate of VLDL to LDL. In contrast, VLDL to HDL 3 transfer was stimulated, resulting in a CETP preference for HDL 3 that was 3-fold greater than that for LDL or HDL 2 . Long-term mass transfer experiments confirmed these findings and further established that the previously observed stimulation of CETP activity on HDL by LTIP is due solely to its stimulation of transfer activity on HDL 3 . TG enrichment of HDL 2 , which occurs during the HDL cycle, inhibited CETP activity by ϳ2-fold and LTIP activity was blocked almost completely. This suggests that LTIP keeps lipid transfer activity on HDL 2 low and constant regardless of its TG enrichment status. Overall, these results show that LTIP tailors CETP-mediated remodeling of HDL 3 and HDL 2 particles in subclass-specific ways, strongly implicating LTIP as a regulator of HDL metabolism.Cholesteryl ester transfer protein (CETP) 1 promotes the net transfer of lipids among lipoproteins (1, 2). Because of its unique capacity to mediate net exchange of triglyceride (TG) and cholesteryl ester (CE) between TG-rich VLDL and CE-rich lipoproteins, such as LDL and HDL, CETP plays an essential role in regulating plasma cholesterol levels. By altering lipoprotein core lipid composition, CETP participates in the catabolism of VLDL to LDL (1, 3, 4) and affects the level of LDL subfractions (5-7). Additionally, CETP facilitates HDL metabolism by promoting the formation of larger TG-rich HDL 2 from smaller HDL 3 subspecies (8, 9), stimulating LCAT activity (10, 11), and enhancing the formation of pre␤-HDL (12). These processes influence the reverse transport of peripheral tissue cholesterol to the liver (2,13,14).In a previous study (15), we demonstrated that CETP possesses no functional preference for HDL over LDL. Consequently, in the absence of other factors, LDL is the most active donor of CE to VLDL due to the relative abundance of CE in this lipoprotein in normal plasma. However, CETP activity is controlled by several apolipoproteins including lipid transfer inhibitor protein (LTIP) (15-19). LTIP has been purified and characterized as an acidic glycoprotein with a molecular mass of 33 kDa (17,20). Molecular cloning of LTIP had determined its identity with apolipoprotein F (20). LTIP prevents CETP activi...

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Section: Ltip Binding To Ldl Hdlcontrasting

confidence: 47%

Lipid Transfer Inhibitor Protein Defines the Participation of High Density Lipoprotein Subfractions in Lipid Transfer Reactions Mediated by Cholesterol Ester Transfer Protein (CETP)

Paromov

Morton

2003

Journal of Biological Chemistry

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“…OxLDL was prepared by incubating 3 mg of LDLprotein/ml in 20 m CuSO 4 during 20 h at room temperature. All lipoproteins were filtered through 0.4-m filters and stored in 0.15 m NaCl, 0.01% Na 2 EDTA, pH 7.4, at 4 Њ C. HDL was subfractionated in apoE ϩ and apoE Ϫ fractions by heparin-Sepharose affinity chromatography as described (42).…”

Section: Isolation Modification and Labeling Of Lipoproteinsmentioning

confidence: 99%

Human CD36 is a high affinity receptor for the native lipoproteins HDL, LDL, and VLDL

Calvo

Gómez-Coronado

Suárez

et al. 1998

Journal of Lipid Research

330

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Mouse and hamster SR-BI glycoproteins and their putative human counterpart CLA-I are so far the only scavenger receptors known to bind both native and modified lipoproteins. CD36, a multigland glycoprotein structurally related to SR-BI and CLA-1, has been reported to bind oxidized low density lipoprotein (OxLDL) and acetylated LDL (AcLDL). In this report, we have studied the ability of CD36 to bind native lipoproteins. By transient expression of human CD36 in mammalian and insect cells, we demonstrate that CD36 is a high affinity receptor for the native lipoproteins HDL, LDL, VLDL, and, as previously reported, for OxLDL and AcLDL. The specificity of these interactions is supported by the dosedependent inhibitory effect of a monoclonal antibody against CD36. Furthermore, at least for HDL, binding to CD36 does not require the presence of apoE. These findings, together with preferential expression of CD36 in tissues performing very active fatty acid metabolism (skeletal muscle, heart, mammary epithelium, and adipose tissue) and its involvement in foam cell formation (macrophages), suggest that binding of lipoproteins to CD36 might contribute to the regulation of lipid metabolism, and to the pathogenesis of atherosclerosis. -

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“…1 As high LDL cholesterol (LDL-C) concentrations and low HDL cholesterol human plasma, a number of factors can potentially influence the cholesteryl ester transfer activity, including the concentration, structure, and composition of donor 6 as well as acceptor 78 lipoprotein substrates. In consequence, CETP mass may not exactly reflect the cholesteryl ester transfer activity in total plasma.…”

mentioning

confidence: 99%

Influence of plasma cholesteryl ester transfer activity on the LDL and HDL distribution profiles in normolipidemic subjects.

Lagrost¹,

Gandjini²,

Athias³

et al. 1993

Arterioscler Thromb

115

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The relations of cholesteryl ester transfer protein (CETP) activity to the distribution of low density lipoproteins (LDLs) and high density lipoproteins (HDLs) were investigated in fasting plasma samples from 27 normolipidemic subjects. LDL and HDL subtractions were separated by electrophoresis on 20-160 g/L and 40-300 g/L polyacrylamide gradient gels, respectively. Subjects were subdivided into two groups according to their LDL pattern. Monodisperse patterns were characterized by the presence of a single LDL band, whereas polydisperse patterns were characterized by the presence of several LDL bands of different sizes. To investigate the influence of lipid transfers on LDL patterns, total plasma was incubated at 37°C in the absence of lecithin: cholesterol acyltransferase (LCAT) activity. The incubation induced a progressive transformation of polydisperse patterns into monodisperse patterns. Under the same conditions, initially monodisperse patterns remained unchanged. Measurements of the rate of radiolabeled cholesteryl esters transferred from HDL 3 s to very low density lipoproteins (VLDLs) and LDLs revealed that subjects with a monodisperse LDL pattern presented a significantly higher plasma CETP activity than subjects with a polydisperse LDL pattern (301±85%/hr per milliliter versus 216±47%/hr per milliliter, respectively; p<0.02). In addition, when total plasma was incubated for 24 hours at 37°C in the absence of LCAT activity, the relative mass of cholesteryl esters transferred from

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High-density lipoprotein subpopulations as substrates for the transfer of cholesteryl esters to very-low-density lipoproteins

Cited by 18 publications

References 34 publications

Lipid Transfer Inhibitor Protein Defines the Participation of High Density Lipoprotein Subfractions in Lipid Transfer Reactions Mediated by Cholesterol Ester Transfer Protein (CETP)

Lipid Transfer Inhibitor Protein Defines the Participation of High Density Lipoprotein Subfractions in Lipid Transfer Reactions Mediated by Cholesterol Ester Transfer Protein (CETP)

Human CD36 is a high affinity receptor for the native lipoproteins HDL, LDL, and VLDL

Influence of plasma cholesteryl ester transfer activity on the LDL and HDL distribution profiles in normolipidemic subjects.

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