Chemical cross-linking alters high-density lipoprotein to be recognized by a scavenger receptor in rat peritoneal macrophages
Identifieur interne : 002F47 ( Main/Exploration ); précédent : 002F46; suivant : 002F48Chemical cross-linking alters high-density lipoprotein to be recognized by a scavenger receptor in rat peritoneal macrophages
Auteurs : Akira Miyazaki [Japon] ; Abu Torab M.A. Rahim [Japon] ; Shukuro Araki [Japon] ; Yoshimasa Morino [Japon] ; Seikoh Horiuchi [Japon]Source :
- Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism [ 0005-2760 ] ; 1991.
English descriptors
- Teeft :
- Biol, Bovine serum albumin, Cellular binding, Chem, Chemical modification, Cholesterol efflux, Cholesteryl, Cholesteryl esters, Dextran sulfate, Efflux, Endocytic uptake, Ester, Foam cells, Human fibroblasts, Ligand, Ligand activity, Ligand specificity, Lipid, Macrophage, Modification, Peritoneal, Peritoneal macrophages, Present study, Radioactivity, Receptor, Scavenger, Scavenger receptor, Scavenger receptors, Significant loss, Sinusoidal liver cells, Specific binding, Unlabeled, Unlabeled ligands.
Abstract
Abstract: Rat peritoneal macrophages possess a surface receptor for high-density lipoprotein (HDL). To obtain the functional aspect of the HDL receptor, the present study was undertaken to modify HDL with three different cross-linkers; dimethylsuberimidate, disuccinimidylsuberate and dithiobissuccinimidylpropionate (DSP) and determine their effect on the ligand activity for the HDL receptor. Upon modification at a low reagent concentration, DSP was found to be most effective in cross-linking of HDL apolipoproteins. The ligand activity of DSP-HDL for the HDL receptor was reduced by > 60%. Experiments with these macrophages at 37°C showed; (i) the amounts of the cell-associated [125I]DSP-HDL as 3.5-fold higher than [125I]HDL; (ii) the cell-association of [125I]DSP-HDL was effectively (> 70%) inhibited by unlabeled DSP-HDL, whereas HDL showed a partial inhibition (30%); (iii) [125I]DSP-HDL underwent chloroquine-sensitive intracellular degradation; and (iv) DSP-HDL induced a 3-fold increase in the incorporation of [14C]oleic acid into cholesteryl oleate when compared with unmodified HDL. Experiments at 0°C showed that the cellular binding of [125I]DSP-HDL was competed by acetylated low-density lipoprotein and dextran sulfate. These findings indicate that DSP-HDL is recognized as a ligand by a scavenger receptor of rat peritoneal macrophages, a notion consistent with HDL modified with tetranitromethane (Kleinherenbrink-Stins, M.F. et al. (1989) J. Lipid Res. 39, 511–520).
Url:
DOI: 10.1016/0005-2760(91)90188-N
Affiliations:
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Le document en format XML
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<term>Cholesterol efflux</term>
<term>Cholesteryl</term>
<term>Cholesteryl esters</term>
<term>Dextran sulfate</term>
<term>Efflux</term>
<term>Endocytic uptake</term>
<term>Ester</term>
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<term>Modification</term>
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<term>Radioactivity</term>
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<term>Scavenger receptors</term>
<term>Significant loss</term>
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<term>Specific binding</term>
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<front><div type="abstract" xml:lang="en">Abstract: Rat peritoneal macrophages possess a surface receptor for high-density lipoprotein (HDL). To obtain the functional aspect of the HDL receptor, the present study was undertaken to modify HDL with three different cross-linkers; dimethylsuberimidate, disuccinimidylsuberate and dithiobissuccinimidylpropionate (DSP) and determine their effect on the ligand activity for the HDL receptor. Upon modification at a low reagent concentration, DSP was found to be most effective in cross-linking of HDL apolipoproteins. The ligand activity of DSP-HDL for the HDL receptor was reduced by > 60%. Experiments with these macrophages at 37°C showed; (i) the amounts of the cell-associated [125I]DSP-HDL as 3.5-fold higher than [125I]HDL; (ii) the cell-association of [125I]DSP-HDL was effectively (> 70%) inhibited by unlabeled DSP-HDL, whereas HDL showed a partial inhibition (30%); (iii) [125I]DSP-HDL underwent chloroquine-sensitive intracellular degradation; and (iv) DSP-HDL induced a 3-fold increase in the incorporation of [14C]oleic acid into cholesteryl oleate when compared with unmodified HDL. Experiments at 0°C showed that the cellular binding of [125I]DSP-HDL was competed by acetylated low-density lipoprotein and dextran sulfate. These findings indicate that DSP-HDL is recognized as a ligand by a scavenger receptor of rat peritoneal macrophages, a notion consistent with HDL modified with tetranitromethane (Kleinherenbrink-Stins, M.F. et al. (1989) J. Lipid Res. 39, 511–520).</div>
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