The intracellular distribution of high density lipoproteins taken up by isolated rat hepatocytes
Identifieur interne : 000C17 ( Istex/Corpus ); précédent : 000C16; suivant : 000C18The intracellular distribution of high density lipoproteins taken up by isolated rat hepatocytes
Auteurs : Leiv Ose ; Turid Ose ; Kaare R. Norum ; Trond BergSource :
- Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism [ 0005-2760 ] ; 1980.
English descriptors
- Teeft :
- Acid phosphatase, Acta, Apolipoprotein, Beckman ultracentrifuge, Berg, Biol, Biophys, Bovine serum albumin, Centrifugation, Centrifuge tube, Chloroquine, Differential centrifugation, Enzyme activities, Hepatocytes, High density lipoproteins, Homogenate, Incubation, Incubation medium, Intracellular, Isopycnic, Isopycnic centrifugation, Light mitochondrial, Linear sucrose gradients, Lipoprotein, Lysosome, Major part, Marker enzymes, Mitochondrial, Phosphatase, Plasma cell membrane, Postnuclear fractions, Radioactivity, Speed centrifugation, Subcellular, Subcellular distribution, Subcellular fractions, Sucrose, Sucrose gradients, Sucrose solution, Unlabelled, Vivo.
Abstract
Abstract: The subcellular distribution of 125I-labelled HDL taken up by rat hepatocytes in vivo and in vitro has been studied with subcellular fractionation techniques: differential centrifugation and isopycnic centrifugation in sucrose gradients. 125I-labelled HDL bind to plasma membranes both in vivo and in vitro and part of the membrane-bound 125I-labelled HDL can be dissociated by the addition of unlabelled HDL. The hepatocytes also internalize 125I-labelled HDL. The 125I-labelled HDL accumulate, however, at different intracellular sites in the in vivo and in vitro situation. The subcellular distribution pattern of 125I-labelled HDL taken up by the cells in vivo is similar to that of the lysosomal marker enzyme acid phosphatase. Peak activity was found at a density of 1.20 g/ml. In vitro 125I-labelled HDL accumulate in an organelle with a medium density of about 1.13 g/ml. This distribution was similar to that of the plasma membrane marker 5'-nucleotidase. The subcellular distribution of radioactivity taken up in vivo was changed to lower density by incubating the cells with chloroquine, a drug known to render the lysosomes more boyant. Chloroquine had no effect on the distribution of 125I-labelled HDL taken up by hepatocytes in vitro.
Url:
DOI: 10.1016/0005-2760(80)90191-5
Links to Exploration step
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<front><div type="abstract" xml:lang="en">Abstract: The subcellular distribution of 125I-labelled HDL taken up by rat hepatocytes in vivo and in vitro has been studied with subcellular fractionation techniques: differential centrifugation and isopycnic centrifugation in sucrose gradients. 125I-labelled HDL bind to plasma membranes both in vivo and in vitro and part of the membrane-bound 125I-labelled HDL can be dissociated by the addition of unlabelled HDL. The hepatocytes also internalize 125I-labelled HDL. The 125I-labelled HDL accumulate, however, at different intracellular sites in the in vivo and in vitro situation. The subcellular distribution pattern of 125I-labelled HDL taken up by the cells in vivo is similar to that of the lysosomal marker enzyme acid phosphatase. Peak activity was found at a density of 1.20 g/ml. In vitro 125I-labelled HDL accumulate in an organelle with a medium density of about 1.13 g/ml. This distribution was similar to that of the plasma membrane marker 5'-nucleotidase. The subcellular distribution of radioactivity taken up in vivo was changed to lower density by incubating the cells with chloroquine, a drug known to render the lysosomes more boyant. Chloroquine had no effect on the distribution of 125I-labelled HDL taken up by hepatocytes in vitro.</div>
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<abstract>Abstract: The subcellular distribution of 125I-labelled HDL taken up by rat hepatocytes in vivo and in vitro has been studied with subcellular fractionation techniques: differential centrifugation and isopycnic centrifugation in sucrose gradients. 125I-labelled HDL bind to plasma membranes both in vivo and in vitro and part of the membrane-bound 125I-labelled HDL can be dissociated by the addition of unlabelled HDL. The hepatocytes also internalize 125I-labelled HDL. The 125I-labelled HDL accumulate, however, at different intracellular sites in the in vivo and in vitro situation. The subcellular distribution pattern of 125I-labelled HDL taken up by the cells in vivo is similar to that of the lysosomal marker enzyme acid phosphatase. Peak activity was found at a density of 1.20 g/ml. In vitro 125I-labelled HDL accumulate in an organelle with a medium density of about 1.13 g/ml. This distribution was similar to that of the plasma membrane marker 5'-nucleotidase. The subcellular distribution of radioactivity taken up in vivo was changed to lower density by incubating the cells with chloroquine, a drug known to render the lysosomes more boyant. Chloroquine had no effect on the distribution of 125I-labelled HDL taken up by hepatocytes in vitro.</abstract>
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<abstract xml:lang="en"><p>Abstract: The subcellular distribution of 125I-labelled HDL taken up by rat hepatocytes in vivo and in vitro has been studied with subcellular fractionation techniques: differential centrifugation and isopycnic centrifugation in sucrose gradients. 125I-labelled HDL bind to plasma membranes both in vivo and in vitro and part of the membrane-bound 125I-labelled HDL can be dissociated by the addition of unlabelled HDL. The hepatocytes also internalize 125I-labelled HDL. The 125I-labelled HDL accumulate, however, at different intracellular sites in the in vivo and in vitro situation. The subcellular distribution pattern of 125I-labelled HDL taken up by the cells in vivo is similar to that of the lysosomal marker enzyme acid phosphatase. Peak activity was found at a density of 1.20 g/ml. In vitro 125I-labelled HDL accumulate in an organelle with a medium density of about 1.13 g/ml. This distribution was similar to that of the plasma membrane marker 5'-nucleotidase. The subcellular distribution of radioactivity taken up in vivo was changed to lower density by incubating the cells with chloroquine, a drug known to render the lysosomes more boyant. Chloroquine had no effect on the distribution of 125I-labelled HDL taken up by hepatocytes in vitro.</p>
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<head><ce:title>The intracellular distribution of high density lipoproteins taken up by isolated rat hepatocytes</ce:title>
<ce:author-group><ce:author><ce:given-name>Leiv</ce:given-name>
<ce:surname>Ose</ce:surname>
</ce:author>
<ce:author><ce:given-name>Turid</ce:given-name>
<ce:surname>Ose</ce:surname>
</ce:author>
<ce:author><ce:given-name>Kaare R.</ce:given-name>
<ce:surname>Norum</ce:surname>
</ce:author>
<ce:author><ce:given-name>Trond</ce:given-name>
<ce:surname>Berg</ce:surname>
</ce:author>
<ce:affiliation><ce:textfn>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, P.O. Box 1046, Oslo 3, Norway</ce:textfn>
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<ce:date-received day="29" month="2" year="1980"></ce:date-received>
<ce:abstract><ce:section-title>Abstract</ce:section-title>
<ce:abstract-sec><ce:simple-para>The subcellular distribution of <ce:sup loc="pre">125</ce:sup>
I-labelled HDL taken up by rat hepatocytes in vivo and in vitro has been studied with subcellular fractionation techniques: differential centrifugation and isopycnic centrifugation in sucrose gradients. <ce:sup>125</ce:sup>
I-labelled HDL bind to plasma membranes both in vivo and in vitro and part of the membrane-bound <ce:sup loc="pre">125</ce:sup>
I-labelled HDL can be dissociated by the addition of unlabelled HDL. The hepatocytes also internalize <ce:sup loc="pre">125</ce:sup>
I-labelled HDL. The <ce:sup loc="pre">125</ce:sup>
I-labelled HDL accumulate, however, at different intracellular sites in the in vivo and in vitro situation. The subcellular distribution pattern of <ce:sup loc="pre">125</ce:sup>
I-labelled HDL taken up by the cells in vivo is similar to that of the lysosomal marker enzyme acid phosphatase. Peak activity was found at a density of 1.20 g/ml. In vitro <ce:sup>125</ce:sup>
I-labelled HDL accumulate in an organelle with a medium density of about 1.13 g/ml. This distribution was similar to that of the plasma membrane marker 5'-nucleotidase. The subcellular distribution of radioactivity taken up in vivo was changed to lower density by incubating the cells with chloroquine, a drug known to render the lysosomes more boyant. Chloroquine had no effect on the distribution of <ce:sup loc="pre">125</ce:sup>
I-labelled HDL taken up by hepatocytes in vitro.</ce:simple-para>
</ce:abstract-sec>
</ce:abstract>
<ce:keywords><ce:section-title>Keywords</ce:section-title>
<ce:keyword><ce:text>HDL</ce:text>
</ce:keyword>
<ce:keyword><ce:text>Endocytosis</ce:text>
</ce:keyword>
<ce:keyword><ce:text>Lipoprotein metabolism</ce:text>
</ce:keyword>
<ce:keyword><ce:text>Lysosome</ce:text>
</ce:keyword>
<ce:keyword><ce:text>(Rat hepatocyte)</ce:text>
</ce:keyword>
</ce:keywords>
<ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title>
<ce:keyword><ce:text>VLDL</ce:text>
</ce:keyword>
<ce:keyword><ce:text>very low density lipoproteins (<ce:italic>d</ce:italic>
< 1.006 <ce:italic>g</ce:italic>
/<ce:italic>ml</ce:italic>
) HDL</ce:text>
</ce:keyword>
<ce:keyword><ce:text>high density lipoproteins (<ce:italic>d</ce:italic>
= 1.075–1.21 <ce:italic>g</ce:italic>
/<ce:italic>ml</ce:italic>
)</ce:text>
</ce:keyword>
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<name type="personal"><namePart type="given">Leiv</namePart>
<namePart type="family">Ose</namePart>
<affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, P.O. Box 1046, Oslo 3, Norway</affiliation>
<role><roleTerm type="text">author</roleTerm>
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<name type="personal"><namePart type="given">Turid</namePart>
<namePart type="family">Ose</namePart>
<affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, P.O. Box 1046, Oslo 3, Norway</affiliation>
<role><roleTerm type="text">author</roleTerm>
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<name type="personal"><namePart type="given">Kaare R.</namePart>
<namePart type="family">Norum</namePart>
<affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, P.O. Box 1046, Oslo 3, Norway</affiliation>
<role><roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal"><namePart type="given">Trond</namePart>
<namePart type="family">Berg</namePart>
<affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, P.O. Box 1046, Oslo 3, Norway</affiliation>
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<abstract lang="en">Abstract: The subcellular distribution of 125I-labelled HDL taken up by rat hepatocytes in vivo and in vitro has been studied with subcellular fractionation techniques: differential centrifugation and isopycnic centrifugation in sucrose gradients. 125I-labelled HDL bind to plasma membranes both in vivo and in vitro and part of the membrane-bound 125I-labelled HDL can be dissociated by the addition of unlabelled HDL. The hepatocytes also internalize 125I-labelled HDL. The 125I-labelled HDL accumulate, however, at different intracellular sites in the in vivo and in vitro situation. The subcellular distribution pattern of 125I-labelled HDL taken up by the cells in vivo is similar to that of the lysosomal marker enzyme acid phosphatase. Peak activity was found at a density of 1.20 g/ml. In vitro 125I-labelled HDL accumulate in an organelle with a medium density of about 1.13 g/ml. This distribution was similar to that of the plasma membrane marker 5'-nucleotidase. The subcellular distribution of radioactivity taken up in vivo was changed to lower density by incubating the cells with chloroquine, a drug known to render the lysosomes more boyant. Chloroquine had no effect on the distribution of 125I-labelled HDL taken up by hepatocytes in vitro.</abstract>
<subject><genre>Keywords</genre>
<topic>HDL</topic>
<topic>Endocytosis</topic>
<topic>Lipoprotein metabolism</topic>
<topic>Lysosome</topic>
<topic>(Rat hepatocyte)</topic>
</subject>
<subject><genre>Abbreviations</genre>
<topic>VLDL</topic>
<topic>very low density lipoproteins (d < 1.006 g/ml) HDL</topic>
<topic>high density lipoproteins (d = 1.075–1.21 g/ml)</topic>
</subject>
<relatedItem type="host"><titleInfo><title>Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism</title>
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<dateIssued encoding="w3cdtf">1980</dateIssued>
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<identifier type="ISSN">0005-2760</identifier>
<identifier type="PII">S0005-2760(00)X0296-2</identifier>
<part><date>1980</date>
<detail type="volume"><number>620</number>
<caption>vol.</caption>
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<extent unit="issue-pages"><start>1</start>
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