Serveur d'exploration Chloroquine

Attention, ce site est en cours de développement !
Attention, site généré par des moyens informatiques à partir de corpus bruts.
Les informations ne sont donc pas validées.

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 : 003848

Uptake 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 :

RBID : ISTEX:FDE907CA05675D68E34DDAD529E5B25D871FB804

English descriptors

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:


Links toward previous steps (curation, corpus...)


Le document en format XML

<record>
<TEI wicri:istexFullTextTei="biblStruct">
<teiHeader>
<fileDesc>
<titleStmt>
<title>Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro</title>
<author>
<name sortKey="Ose, Leiv" sort="Ose, Leiv" uniqKey="Ose L" first="Leiv" last="Ose">Leiv Ose</name>
</author>
<author>
<name sortKey="Ose, Turid" sort="Ose, Turid" uniqKey="Ose T" first="Turid" last="Ose">Turid Ose</name>
</author>
<author>
<name sortKey="Norum, Kaare R" sort="Norum, Kaare R" uniqKey="Norum K" first="Kaare R." last="Norum">Kaare R. Norum</name>
</author>
<author>
<name sortKey="Berg, Trond" sort="Berg, Trond" uniqKey="Berg T" first="Trond" last="Berg">Trond Berg</name>
</author>
</titleStmt>
<publicationStmt>
<idno type="wicri:source">ISTEX</idno>
<idno type="RBID">ISTEX:FDE907CA05675D68E34DDAD529E5B25D871FB804</idno>
<date when="1979" year="1979">1979</date>
<idno type="doi">10.1016/0005-2760(79)90248-0</idno>
<idno type="url">https://api.istex.fr/ark:/67375/6H6-L16444XM-9/fulltext.pdf</idno>
<idno type="wicri:Area/Istex/Corpus">000D44</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000D44</idno>
<idno type="wicri:Area/Istex/Curation">000D44</idno>
<idno type="wicri:Area/Istex/Checkpoint">002602</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">002602</idno>
<idno type="wicri:doubleKey">0005-2760:1979:Ose L:uptake:and:degradation</idno>
<idno type="wicri:Area/Main/Merge">003926</idno>
<idno type="wicri:Area/Main/Curation">003847</idno>
<idno type="wicri:Area/Main/Exploration">003847</idno>
</publicationStmt>
<sourceDesc>
<biblStruct>
<analytic>
<title level="a">Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro</title>
<author>
<name sortKey="Ose, Leiv" sort="Ose, Leiv" uniqKey="Ose L" first="Leiv" last="Ose">Leiv Ose</name>
<affiliation wicri:level="3">
<country xml:lang="fr">Norvège</country>
<wicri:regionArea>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo</wicri:regionArea>
<placeName>
<settlement type="city">Oslo</settlement>
<region nuts="2">Østlandet</region>
</placeName>
</affiliation>
</author>
<author>
<name sortKey="Ose, Turid" sort="Ose, Turid" uniqKey="Ose T" first="Turid" last="Ose">Turid Ose</name>
<affiliation wicri:level="3">
<country xml:lang="fr">Norvège</country>
<wicri:regionArea>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo</wicri:regionArea>
<placeName>
<settlement type="city">Oslo</settlement>
<region nuts="2">Østlandet</region>
</placeName>
</affiliation>
</author>
<author>
<name sortKey="Norum, Kaare R" sort="Norum, Kaare R" uniqKey="Norum K" first="Kaare R." last="Norum">Kaare R. Norum</name>
<affiliation wicri:level="3">
<country xml:lang="fr">Norvège</country>
<wicri:regionArea>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo</wicri:regionArea>
<placeName>
<settlement type="city">Oslo</settlement>
<region nuts="2">Østlandet</region>
</placeName>
</affiliation>
</author>
<author>
<name sortKey="Berg, Trond" sort="Berg, Trond" uniqKey="Berg T" first="Trond" last="Berg">Trond Berg</name>
<affiliation wicri:level="3">
<country xml:lang="fr">Norvège</country>
<wicri:regionArea>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo</wicri:regionArea>
<placeName>
<settlement type="city">Oslo</settlement>
<region nuts="2">Østlandet</region>
</placeName>
</affiliation>
</author>
</analytic>
<monogr></monogr>
<series>
<title level="j">Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism</title>
<title level="j" type="abbrev">BBALIP</title>
<idno type="ISSN">0005-2760</idno>
<imprint>
<publisher>ELSEVIER</publisher>
<date type="published" when="1979">1979</date>
<biblScope unit="volume">574</biblScope>
<biblScope unit="issue">3</biblScope>
<biblScope unit="page" from="521">521</biblScope>
<biblScope unit="page" to="536">536</biblScope>
</imprint>
<idno type="ISSN">0005-2760</idno>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt>
<idno type="ISSN">0005-2760</idno>
</seriesStmt>
</fileDesc>
<profileDesc>
<textClass>
<keywords scheme="Teeft" xml:lang="en">
<term>Acid phosphatase</term>
<term>Acta</term>
<term>Adsorptive endocytosis</term>
<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>
<term>Ester</term>
<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>
</keywords>
</textClass>
<langUsage>
<language ident="en">en</language>
</langUsage>
</profileDesc>
</teiHeader>
<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>
</front>
</TEI>
<affiliations>
<list>
<country>
<li>Norvège</li>
</country>
<region>
<li>Østlandet</li>
</region>
<settlement>
<li>Oslo</li>
</settlement>
</list>
<tree>
<country name="Norvège">
<region name="Østlandet">
<name sortKey="Ose, Leiv" sort="Ose, Leiv" uniqKey="Ose L" first="Leiv" last="Ose">Leiv Ose</name>
</region>
<name sortKey="Berg, Trond" sort="Berg, Trond" uniqKey="Berg T" first="Trond" last="Berg">Trond Berg</name>
<name sortKey="Norum, Kaare R" sort="Norum, Kaare R" uniqKey="Norum K" first="Kaare R." last="Norum">Kaare R. Norum</name>
<name sortKey="Ose, Turid" sort="Ose, Turid" uniqKey="Ose T" first="Turid" last="Ose">Turid Ose</name>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/ChloroquineV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003847 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 003847 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    ChloroquineV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     ISTEX:FDE907CA05675D68E34DDAD529E5B25D871FB804
   |texte=   Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro
}}

Wicri

This area was generated with Dilib version V0.6.33.
Data generation: Wed Mar 25 22:43:59 2020. Site generation: Sun Jan 31 12:44:45 2021