Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro
Identifieur interne : 003847 ( Main/Exploration ); précédent : 003846; suivant : 003848Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro
Auteurs : Leiv Ose [Norvège] ; Turid Ose [Norvège] ; Kaare R. Norum [Norvège] ; Trond Berg [Norvège]Source :
- Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism [ 0005-2760 ] ; 1979.
English descriptors
- Teeft :
- Acid phosphatase, Acta, Adsorptive endocytosis, Aliquot, Berg, Binding sites, Biochim, Biol, Biophys, Cell suspension, Centrifugation, Chloroquine, Cholesteryl, Cholesteryl ester hydrolysis, Cholesteryl ester moiety, Collagenase, Collagenase perfusion, Degradation, Degraded, Differential centrifugation, Endocytosis, Ester, Extracellular, Fluid endocytosis, Hepatocytes, High density lipoproteins, Ilabelled, Incubation, Incubation medium, Intracellular, Intravenous injection, Isopycnic centrifugation, Leupeptin, Lipid, Lipoprotein, Lipoprotein degradation, Lipoprotein metabolism, Liver cells, Lysosomal, Lysosome, Nonparenchymal cells, Perfusion, Phosphatase, Plasma membrane, Polyvinylpyrrolidone, Preincubated, Pronase, Pronase treatment, Radioactivity, Specific activity, Speed centrifugation, Supernatant, Time points, Trichloroacetic acid, Uptake, Various organs.
Abstract
Abstract: 1. 1. The uptake of 125I-labelled high density lipoproteins (HDL) in various organs of the rat was determined after an intravenous injection. The uptake of 125I-labelled polyvinylpyrrolidone in the same organs was determined in order to assess uptake by fluid endocytosis. The uptake/organ was highest for the liver. The adrenals showed the highest uptake/unit weight of the organs studied. The liver, the kidneys and the spleen showed comparable values for uptake/g of tissue. The uptake of 125I-labelled HDL exceeded by far that of 125I-labelled polyvinylpyrrolidone in the liver, the kidneys, the spleen and the adrenals, indicating that the uptake of 125I-labelled HDL was mediated by adsorptive endocytosis. 2. 2. The in vivo uptake of 125I-labelled HDL was determined in purified hepatocytes and non-parenchymal cells prepared by collagenase perfusion of livers from animals after intravenous injections of 125I-labelled HDL. When expressed per cell, the hepatocytes and the non-parenchymal liver cells took up about the same amount of 125I-labelled HDL. 3. 3. The in vitro uptake and degradation of 125I-labelled HDL in isolated rat hepatocytes was studied. The uptake at increasing concentrations of 125I-labelled HDL was saturable indicating uptake mediated through binding sites. 125I-labelled HDL were easily degraded by contaminating proteases from the perfusate. 4. 4. Subcellular fractionation by isopycnic centrifugation indicated that the accumulation of 125I-labelled HDL did not take place in the lysosomes, but rather on the plasma membrane and possibly in the endosomes (phagosomes). 5. 5. 125I-labelled HDL were internalized into the cells and degraded in the lysosomes. Leupeptin and chloroquine, inhibitors of the lysosomal function effectively inhibited the formation of 125I-labelled acid-soluble radioactivity by the cells. Chloroquine, but not the protease inhibitor leupeptin, reduced the hydrolysis of the cholesteryl ester moiety of HDL.
Url:
DOI: 10.1016/0005-2760(79)90248-0
Affiliations:
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Le document en format XML
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<term>Aliquot</term>
<term>Berg</term>
<term>Binding sites</term>
<term>Biochim</term>
<term>Biol</term>
<term>Biophys</term>
<term>Cell suspension</term>
<term>Centrifugation</term>
<term>Chloroquine</term>
<term>Cholesteryl</term>
<term>Cholesteryl ester hydrolysis</term>
<term>Cholesteryl ester moiety</term>
<term>Collagenase</term>
<term>Collagenase perfusion</term>
<term>Degradation</term>
<term>Degraded</term>
<term>Differential centrifugation</term>
<term>Endocytosis</term>
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<term>Extracellular</term>
<term>Fluid endocytosis</term>
<term>Hepatocytes</term>
<term>High density lipoproteins</term>
<term>Ilabelled</term>
<term>Incubation</term>
<term>Incubation medium</term>
<term>Intracellular</term>
<term>Intravenous injection</term>
<term>Isopycnic centrifugation</term>
<term>Leupeptin</term>
<term>Lipid</term>
<term>Lipoprotein</term>
<term>Lipoprotein degradation</term>
<term>Lipoprotein metabolism</term>
<term>Liver cells</term>
<term>Lysosomal</term>
<term>Lysosome</term>
<term>Nonparenchymal cells</term>
<term>Perfusion</term>
<term>Phosphatase</term>
<term>Plasma membrane</term>
<term>Polyvinylpyrrolidone</term>
<term>Preincubated</term>
<term>Pronase</term>
<term>Pronase treatment</term>
<term>Radioactivity</term>
<term>Specific activity</term>
<term>Speed centrifugation</term>
<term>Supernatant</term>
<term>Time points</term>
<term>Trichloroacetic acid</term>
<term>Uptake</term>
<term>Various organs</term>
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<front><div type="abstract" xml:lang="en">Abstract: 1. 1. The uptake of 125I-labelled high density lipoproteins (HDL) in various organs of the rat was determined after an intravenous injection. The uptake of 125I-labelled polyvinylpyrrolidone in the same organs was determined in order to assess uptake by fluid endocytosis. The uptake/organ was highest for the liver. The adrenals showed the highest uptake/unit weight of the organs studied. The liver, the kidneys and the spleen showed comparable values for uptake/g of tissue. The uptake of 125I-labelled HDL exceeded by far that of 125I-labelled polyvinylpyrrolidone in the liver, the kidneys, the spleen and the adrenals, indicating that the uptake of 125I-labelled HDL was mediated by adsorptive endocytosis. 2. 2. The in vivo uptake of 125I-labelled HDL was determined in purified hepatocytes and non-parenchymal cells prepared by collagenase perfusion of livers from animals after intravenous injections of 125I-labelled HDL. When expressed per cell, the hepatocytes and the non-parenchymal liver cells took up about the same amount of 125I-labelled HDL. 3. 3. The in vitro uptake and degradation of 125I-labelled HDL in isolated rat hepatocytes was studied. The uptake at increasing concentrations of 125I-labelled HDL was saturable indicating uptake mediated through binding sites. 125I-labelled HDL were easily degraded by contaminating proteases from the perfusate. 4. 4. Subcellular fractionation by isopycnic centrifugation indicated that the accumulation of 125I-labelled HDL did not take place in the lysosomes, but rather on the plasma membrane and possibly in the endosomes (phagosomes). 5. 5. 125I-labelled HDL were internalized into the cells and degraded in the lysosomes. Leupeptin and chloroquine, inhibitors of the lysosomal function effectively inhibited the formation of 125I-labelled acid-soluble radioactivity by the cells. Chloroquine, but not the protease inhibitor leupeptin, reduced the hydrolysis of the cholesteryl ester moiety of HDL.</div>
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