The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes
Identifieur interne : 003808 ( Main/Exploration ); précédent : 003807; suivant : 003809The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes
Auteurs : Leiv Ose [Norvège] ; Ingeborg R Ken [Norvège] ; Kaare R. Norum [Norvège] ; Trond Berg [Norvège]Source :
- Experimental Cell Research [ 0014-4827 ] ; 1980.
English descriptors
- Teeft :
- Acid phosphatase, Acta, Adsorptive endocytosis, Ammonia, Berg, Biochem, Biochim biophys acta, Biol, Bovine serum albumin, Cell suspension, Cellular degradation, Centrifugation, Chloroquine, Colchicine, Control cells, Control values, Cpmlng protein, Degradation, Hepatocytes, High density lipoproteins, Incubation medium, Inhibitor, Intracellular, Isopycnic centrifugation, Leupeptin, Lipoprotein, Lysosomal, Lysosomal function, Lysosome, Microfilaments, Microtubuli, Radioactivity, Subcellular, Sucrose, Tail vein, Vivo.
Abstract
Abstract: Degradation of 125I-labelled HDL ([125I]HDL) was measured in isolated rat hepatocytes that had been preincubated with [125I]HDL and then reincubated in fresh medium without [125I]HDL. About 5 % of the [125I]HDL associated with the cells in advance were degraded per hour at 37 °C. This in vitro degradation was inhibited about 50% by lysosomal inhibitors such as chloroquine, ammonia and leupeptin. Depolymerization of microtubuli by colchicine inhibited the degradation of [125I]HDL to about 65–75 % of the control cells. Cytochalasin B (CB), a destabilizer of microfilaments, had a less marked effect on the degradation in vitro. Degradation of [125I]HDL associated with cells in vivo after intravenous injection was also studied in isolated cells. About 8.5% of the [125I]HDL associated with the cells in vivo were degraded per hour in the isolated cells. The effects of ammonia, chloroquine, leupeptin and colchicine on HDL degradation were similar for [125I]HDL taken up in vivo and in vitro. Subcellular fractionation by centrifugation in sucrose gradients indicated that [125I]HDL associated with hepatocytes in vivo are primarily accumulated in lysosomes. [125I]HDL associated with the cells in vitro are located in organelles whose distribution coincides with that of 5′-nucleotidase. These organelles may be endocytic vesicles. It is concluded that the internalization of [125I]HDL in rat hepatocytes is relatively slow. The intracellular degradation of the apoproteins of HDL is at least partly lysosomal.
Url:
DOI: 10.1016/0014-4827(80)90049-X
Affiliations:
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Le document en format XML
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<term>Berg</term>
<term>Biochem</term>
<term>Biochim biophys acta</term>
<term>Biol</term>
<term>Bovine serum albumin</term>
<term>Cell suspension</term>
<term>Cellular degradation</term>
<term>Centrifugation</term>
<term>Chloroquine</term>
<term>Colchicine</term>
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<term>Control values</term>
<term>Cpmlng protein</term>
<term>Degradation</term>
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<term>High density lipoproteins</term>
<term>Incubation medium</term>
<term>Inhibitor</term>
<term>Intracellular</term>
<term>Isopycnic centrifugation</term>
<term>Leupeptin</term>
<term>Lipoprotein</term>
<term>Lysosomal</term>
<term>Lysosomal function</term>
<term>Lysosome</term>
<term>Microfilaments</term>
<term>Microtubuli</term>
<term>Radioactivity</term>
<term>Subcellular</term>
<term>Sucrose</term>
<term>Tail vein</term>
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<front><div type="abstract" xml:lang="en">Abstract: Degradation of 125I-labelled HDL ([125I]HDL) was measured in isolated rat hepatocytes that had been preincubated with [125I]HDL and then reincubated in fresh medium without [125I]HDL. About 5 % of the [125I]HDL associated with the cells in advance were degraded per hour at 37 °C. This in vitro degradation was inhibited about 50% by lysosomal inhibitors such as chloroquine, ammonia and leupeptin. Depolymerization of microtubuli by colchicine inhibited the degradation of [125I]HDL to about 65–75 % of the control cells. Cytochalasin B (CB), a destabilizer of microfilaments, had a less marked effect on the degradation in vitro. Degradation of [125I]HDL associated with cells in vivo after intravenous injection was also studied in isolated cells. About 8.5% of the [125I]HDL associated with the cells in vivo were degraded per hour in the isolated cells. The effects of ammonia, chloroquine, leupeptin and colchicine on HDL degradation were similar for [125I]HDL taken up in vivo and in vitro. Subcellular fractionation by centrifugation in sucrose gradients indicated that [125I]HDL associated with hepatocytes in vivo are primarily accumulated in lysosomes. [125I]HDL associated with the cells in vitro are located in organelles whose distribution coincides with that of 5′-nucleotidase. These organelles may be endocytic vesicles. It is concluded that the internalization of [125I]HDL in rat hepatocytes is relatively slow. The intracellular degradation of the apoproteins of HDL is at least partly lysosomal.</div>
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