Cholesteryl ester transfer protein promotes the association of HDL apolipoproteins A-I and A-II with LDL: potentiation by oleic acid
Identifieur interne : 001475 ( Istex/Curation ); précédent : 001474; suivant : 001476Cholesteryl ester transfer protein promotes the association of HDL apolipoproteins A-I and A-II with LDL: potentiation by oleic acid
Auteurs : Laurent Lagrost [France] ; Philip J. Barter [Australie]Source :
- Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism [ 0005-2760 ] ; 1992.
Descripteurs français
- Wicri :
- topic : Troc.
English descriptors
- KwdEn :
- Apo, Apolipoprotein, Apolipoproteins, Barter, Biol, CETP, Cetp, Cetp concentration, Chem, Cholesteryl, Cholesteryl ester transfer protein, Cholesteryl esters, Coprecipitated, Ester, Fatty acids, Final protein concentration, Final volume, HDL, HDL3, Human plasma, Immunoprecipitated, Immunoprecipitated samples, Immunoprecipitation, Immunoprecipitation procedure, Incubation, Incubation mixture, Incubation mixtures, Incubation times, LDL, Lipid, Lipoprotein, Lipoprotein particles, Monoclonal, Monoclonal antibodies, Non-esterified fatty acid, Oleic, Oleic acid, Particle size redistribution, Present experiments, Present study, Protein concentration, Significant proportion, Single determination, Supernatant, TBS, Total plasma, VLDL.
- Teeft :
- Apolipoproteins, Barter, Biol, Cetp, Cetp concentration, Chem, Cholesteryl, Cholesteryl ester transfer protein, Cholesteryl esters, Coprecipitated, Ester, Fatty acids, Final protein concentration, Final volume, Human plasma, Immunoprecipitated, Immunoprecipitated samples, Immunoprecipitation, Immunoprecipitation procedure, Incubation, Incubation mixture, Incubation mixtures, Incubation times, Lipid, Lipoprotein, Lipoprotein particles, Monoclonal, Monoclonal antibodies, Oleic, Oleic acid, Particle size redistribution, Present experiments, Present study, Protein concentration, Significant proportion, Single determination, Supernatant, Total plasma.
Abstract
Abstract: The association of apolipoprotein (apo) A-I and apo A-II with apo-B-containing particles was measured after incubation at 37°C of either total plasma or low-density lipoproteins (LDL) and high-density lipoproteins-3 (HDL3) in the presence of partially purified cholesteryl ester transfer protein (CETP). At the end of the incubation, apo-B-containing lipoproteins were separated by immunoprecipitation with an anti-apo B γ-globulin fraction. In mixtures containing LDL and HDL3, either maintained at 4°C or incubated at 37°C, optimal concentrations of anti-apo B antibodies induced the precipitation of more than 95% of apo B without precipitation of apo A-I and apo A-II. When total plasma was incubated at 37°C for 24 h, a significant proportion of apo A-I and apo A-II became associated with apo-B-containing lipoproteins. The fraction of HDL apoproteins associated with apo-B-containing lipoproteins was significantly reduced when plasma was supplemented with TP2 anti-CETP monoclonal antibodies, which are known to inhibit CETP activity. Incubation of LDL and HDL3 for 24 h at 37°C in the presence of purified CETP also induced the association of a significant proportion of apo A-I and apo A-II with apo-B-containing particles. This effect was dependent on CETP concentration in the incubation mixtures and could be suppressed by the addition of anti-CETP monoclonal antibodies. While oleic acid alone, at a final concentration of 0.2 mmol/l, did not promote any association of HDL-apolipoproteins with LDL, it was able, at this concentration, to greatly enhance the CETP-mediated association of apo A-I and apo A-II with apo-B-containing particles. In the presence of both CETP and oleic acid, the association of apo A-I and apo A-II with apo-B-containing particles was apparent within 3 h of commencing the incubation. Approximately 3 mol of apo A-I and 1 mol of apo A-II co-precipitated with each mol of apo B after a 24 h incubation of LDL, HDL3 and CETP. When oleic acid was added to the incubation mixture in addition to CETP, up to 5.5 mol of apo A-I and 2.3 mol of apo A-II were associated with each mol of apo B. The present study has demonstrated that CETP can promote the association of apo A-I and apo A-II with apo-B-containing particles and that this process is enhanced by oleic acid.
Url:
DOI: 10.1016/0005-2760(92)90229-O
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<term>Apolipoprotein</term>
<term>Apolipoproteins</term>
<term>Barter</term>
<term>Biol</term>
<term>CETP</term>
<term>Cetp</term>
<term>Cetp concentration</term>
<term>Chem</term>
<term>Cholesteryl</term>
<term>Cholesteryl ester transfer protein</term>
<term>Cholesteryl esters</term>
<term>Coprecipitated</term>
<term>Ester</term>
<term>Fatty acids</term>
<term>Final protein concentration</term>
<term>Final volume</term>
<term>HDL</term>
<term>HDL3</term>
<term>Human plasma</term>
<term>Immunoprecipitated</term>
<term>Immunoprecipitated samples</term>
<term>Immunoprecipitation</term>
<term>Immunoprecipitation procedure</term>
<term>Incubation</term>
<term>Incubation mixture</term>
<term>Incubation mixtures</term>
<term>Incubation times</term>
<term>LDL</term>
<term>Lipid</term>
<term>Lipoprotein</term>
<term>Lipoprotein particles</term>
<term>Monoclonal</term>
<term>Monoclonal antibodies</term>
<term>Non-esterified fatty acid</term>
<term>Oleic</term>
<term>Oleic acid</term>
<term>Particle size redistribution</term>
<term>Present experiments</term>
<term>Present study</term>
<term>Protein concentration</term>
<term>Significant proportion</term>
<term>Single determination</term>
<term>Supernatant</term>
<term>TBS</term>
<term>Total plasma</term>
<term>VLDL</term>
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<keywords scheme="Teeft" xml:lang="en"><term>Apolipoproteins</term>
<term>Barter</term>
<term>Biol</term>
<term>Cetp</term>
<term>Cetp concentration</term>
<term>Chem</term>
<term>Cholesteryl</term>
<term>Cholesteryl ester transfer protein</term>
<term>Cholesteryl esters</term>
<term>Coprecipitated</term>
<term>Ester</term>
<term>Fatty acids</term>
<term>Final protein concentration</term>
<term>Final volume</term>
<term>Human plasma</term>
<term>Immunoprecipitated</term>
<term>Immunoprecipitated samples</term>
<term>Immunoprecipitation</term>
<term>Immunoprecipitation procedure</term>
<term>Incubation</term>
<term>Incubation mixture</term>
<term>Incubation mixtures</term>
<term>Incubation times</term>
<term>Lipid</term>
<term>Lipoprotein</term>
<term>Lipoprotein particles</term>
<term>Monoclonal</term>
<term>Monoclonal antibodies</term>
<term>Oleic</term>
<term>Oleic acid</term>
<term>Particle size redistribution</term>
<term>Present experiments</term>
<term>Present study</term>
<term>Protein concentration</term>
<term>Significant proportion</term>
<term>Single determination</term>
<term>Supernatant</term>
<term>Total plasma</term>
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<keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Troc</term>
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<front><div type="abstract" xml:lang="en">Abstract: The association of apolipoprotein (apo) A-I and apo A-II with apo-B-containing particles was measured after incubation at 37°C of either total plasma or low-density lipoproteins (LDL) and high-density lipoproteins-3 (HDL3) in the presence of partially purified cholesteryl ester transfer protein (CETP). At the end of the incubation, apo-B-containing lipoproteins were separated by immunoprecipitation with an anti-apo B γ-globulin fraction. In mixtures containing LDL and HDL3, either maintained at 4°C or incubated at 37°C, optimal concentrations of anti-apo B antibodies induced the precipitation of more than 95% of apo B without precipitation of apo A-I and apo A-II. When total plasma was incubated at 37°C for 24 h, a significant proportion of apo A-I and apo A-II became associated with apo-B-containing lipoproteins. The fraction of HDL apoproteins associated with apo-B-containing lipoproteins was significantly reduced when plasma was supplemented with TP2 anti-CETP monoclonal antibodies, which are known to inhibit CETP activity. Incubation of LDL and HDL3 for 24 h at 37°C in the presence of purified CETP also induced the association of a significant proportion of apo A-I and apo A-II with apo-B-containing particles. This effect was dependent on CETP concentration in the incubation mixtures and could be suppressed by the addition of anti-CETP monoclonal antibodies. While oleic acid alone, at a final concentration of 0.2 mmol/l, did not promote any association of HDL-apolipoproteins with LDL, it was able, at this concentration, to greatly enhance the CETP-mediated association of apo A-I and apo A-II with apo-B-containing particles. In the presence of both CETP and oleic acid, the association of apo A-I and apo A-II with apo-B-containing particles was apparent within 3 h of commencing the incubation. Approximately 3 mol of apo A-I and 1 mol of apo A-II co-precipitated with each mol of apo B after a 24 h incubation of LDL, HDL3 and CETP. When oleic acid was added to the incubation mixture in addition to CETP, up to 5.5 mol of apo A-I and 2.3 mol of apo A-II were associated with each mol of apo B. The present study has demonstrated that CETP can promote the association of apo A-I and apo A-II with apo-B-containing particles and that this process is enhanced by oleic acid.</div>
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