Cholesterol-induced alteration of apolipoprotein A-I conformation in reassembled high density lipoprotein

Talussot, Corinne; Ponsin, Gabriel

doi:10.1016/0300-9084(91)90001-h

Cited by 4 publications

(2 citation statements)

References 18 publications

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“…Although the secondary structure of apoA-I appears similar in all HDL subclasses, several reports show that the microconformation of apoA-I may vary from one particle to another. The differences in apoA-I microconformation may depend on various parameters, including the particle size (60), the number of apoA-I molecules per particle, the number of helical segments in contact with lipid (61,62), and the content of free cholesterol in HDL (63). These different conformations of apoA-I are probably critically important for the physiological functions of HDL.…”

Section: Discussionmentioning

confidence: 99%

Binding of phospholipid transfer protein (PLTP) to apolipoproteins A-I and A-II: location of a PLTP binding domain in the amino terminal region of apoA-I

Pussinen

Jauhiainen

Metso

et al. 1998

Journal of Lipid Research

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The interaction of plasma phospholipid transfer protein (PLTP) with HDL has not been characterized in detail, although we have reported that the apoA-I/apoA-II molar ratio in the HDL particle influences PLTP-mediated HDL conversion, but not phospholipid transfer. The aim of this study was to examine whether PLTP binds apoA-I or apoA-II, and if this occurs, then determine the PLTP-binding domain of the apoA-I molecule. To study the PLTP/apolipoprotein interaction we used a solid phase ligand binding assay, the ELISA technique, and apoA-I and apoA-II affinity chromatography. PLTP bound to both apoA-I and apoA-II affinity columns, a finding subsequently utilized in the purification of PLTP. PLTP also bound to both apoA-I and apoA-II on ELISA plates in a concentration-dependent manner, and the binding could be displaced by preincubating the PLTP sample with purified apolipoproteins. To determine which portion of apoA-I is recognized by PLTP, we coated ELISA plates with either recombinant full-length apoA-I or three shortened apoA-I forms sequentially truncated from the C-terminus. To characterize the PLTP binding ability of the C-terminal region of apoA-I, we used both C-terminal CNBr-fragment and a synthetic C-terminal peptide of apoA-I. To further confirm the identity of the binding region, we probed the interaction with a polyclonal and several monoclonal anti-apoA-I antibodies. The antibodies that inhibited the interaction between PLTP and apoA-I were directed towards apoA-I epitopes localized between amino acids 27-141. The polyclonal antibody, R33, and the monoclonal antibody A-I-1 (epitope between amino acids 27-48) were most effective and reduced PLTP binding by 70%. These results show that PLTP binds to both apoA-I and apoA-II, and that the PLTP binding domain of apoA-I resides in the amino terminal region.

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Section: Discussionmentioning

confidence: 99%

Binding of phospholipid transfer protein (PLTP) to apolipoproteins A-I and A-II: location of a PLTP binding domain in the amino terminal region of apoA-I

Pussinen

Jauhiainen

Metso

et al. 1998

Journal of Lipid Research

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“…The dynamics of HDL surface was monitored by measuring the fluorescence anisotropy of 1-(4-trimethylammonium phenyl)-6-phenyl-1,3,5-hexatriene (TMA-DPH) using an SLM-Aminico SPF-500c spectrofluorometer equipped with an externally controlled temperature regulator [36]. After precipitation of apo B-containing lipoproteins by the phosphotungstate-magnesium chloride procedure HDL was isolated by ultracentrifugation at a density of 1 .…”

Section: Fluorescence Polarization Measurementsmentioning

confidence: 99%

Multiple abnormalities in the transfer of phospholipids from VLDL and LDL to HDL in non‐insulin‐dependent diabetes

Elchebly

Pulcini

Porokhov

et al. 1996

Eur J Clin Investigation

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Transfers or exchanges of cholesterol esters and triglycerides between lipoproteins are mediated by a specialized protein referred to as cholesteryl ester transfer protein (CETP), whereas those of phospholipids (PLs) are facilitated by both CETP and a specific phospholipid transfer protein (PLTP). In the present study, the authors compared phospholipid transfer (PLT) in normal subjects and in patients with non-insulin-dependent diabetes (NIDD), which is associated with an increased risk of atherosclerosis. PLT was measured in different recombination experiments using an isotopic assay in which the transfer of labelled PLs from very low-density lipoprotein (VLDLs) and low-density lipoproteins (LDLs) to high-density lipoproteins (HDLs) was determined. This allowed discrimination between the roles of VLDLs + LDLs, HDLs, and plasma PLT activity (PLTA). VLDL + LDL-dependent PLT, HDL-dependent PLT and PLTA were decreased in NIDD. VLDL + LDL-dependent PLT was found to be negatively correlated with the PL/apolipoprotein B ratio, whereas HDL-dependent PLT was positively correlated with the HDL2/HDL3 and PL/apolipoprotein A-I ratios and negatively correlated with the flow activation energy at the HDL surface. The HDL2/HDL3 ratio was positively correlated with PLTA but not with CETP, which confirms previous reports suggesting that PLTP might act as an HDL conversion factor. These data show that several abnormalities in PLT occur in NIDD and raise the question as to whether a lowered PLT might be a new characteristic of dis factors associated with an increased risk of atherosclerosis.

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Decreased capacity to inhibit platelet hyperactivity and to stabilize prostacyclin of high-density lipoproteins in experimental diabetes

et al. 1995

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Twenty-eight male Sprague Dawley rats were divided into two groups: a control group (C) of 15 animals and a streptozotocin-induced diabetes group mildly balanced by insulin (D) of 13 animals. After 15 weeks, plasma and high-density lipoprotein (HDL) lipids were determined in each group. Apoprotein A-I concentration was evaluated in HDL fractions. The capacity of the HDL fraction to inhibit thrombin and ADP-induced aggregation of normal platelets was determined for each rat, and in an additional experiment the relation dose-effect of HDL was established. The effect of HDL of the two groups on the stabilization of prostacyclin was compared by aggregation bioassay. After 15 weeks, HDL cholesterol (free + esterified). After 15 weeks, HDL cholesterol (free + esterified) tended to increase in group D compared with group C (P < 0.08). By contrast, apoprotein A-I was very significantly decreased in HDL-D compared with HDL-C (P < 0.001). These alterations were accompanied by a significantly decreased capacity of HDL (60 micrograms/ml platelet suspension) to inhibit ADP-induced aggregation (P< 0.0001) in group D compared with group C. Furthermore, HDL-D incubated 45 or 90 min with prostacyclin showed a significantly decreased capacity to stabilize prostacyclin compared with HDL-C (P<0.04; P <0.03, respectively). These alterations in HDL could be involved in thrombosis and atheromatous complications associated with this disease.

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Cholesterol-induced alteration of apolipoprotein A-I conformation in reassembled high density lipoprotein

Cited by 4 publications

References 18 publications

Binding of phospholipid transfer protein (PLTP) to apolipoproteins A-I and A-II: location of a PLTP binding domain in the amino terminal region of apoA-I

Binding of phospholipid transfer protein (PLTP) to apolipoproteins A-I and A-II: location of a PLTP binding domain in the amino terminal region of apoA-I

Multiple abnormalities in the transfer of phospholipids from VLDL and LDL to HDL in non‐insulin‐dependent diabetes

Decreased capacity to inhibit platelet hyperactivity and to stabilize prostacyclin of high-density lipoproteins in experimental diabetes

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