Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro
Identifieur interne : 001F04 ( Istex/Corpus ); précédent : 001F03; suivant : 001F05Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro
Auteurs : Leiv Ose ; Turid Ose ; Kaare R. Norum ; Trond BergSource :
- Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism [ 0005-2760 ] ; 1979.
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.
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DOI: 10.1016/0005-2760(79)90248-0
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<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><affiliation><mods:affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</mods:affiliation></affiliation></author><author><name sortKey="Ose, Turid" sort="Ose, Turid" uniqKey="Ose T" first="Turid" last="Ose">Turid Ose</name><affiliation><mods:affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</mods:affiliation></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><mods:affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</mods:affiliation></affiliation></author><author><name sortKey="Berg, Trond" sort="Berg, Trond" uniqKey="Berg T" first="Trond" last="Berg">Trond Berg</name><affiliation><mods:affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</mods:affiliation></affiliation></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/document/FDE907CA05675D68E34DDAD529E5B25D871FB804/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001F04</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><mods:affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</mods:affiliation></affiliation></author><author><name sortKey="Ose, Turid" sort="Ose, Turid" uniqKey="Ose T" first="Turid" last="Ose">Turid Ose</name><affiliation><mods:affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</mods:affiliation></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><mods:affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</mods:affiliation></affiliation></author><author><name sortKey="Berg, Trond" sort="Berg, Trond" uniqKey="Berg T" first="Trond" last="Berg">Trond Berg</name><affiliation><mods:affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</mods:affiliation></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><idno type="istex">FDE907CA05675D68E34DDAD529E5B25D871FB804</idno><idno type="DOI">10.1016/0005-2760(79)90248-0</idno><idno type="PII">0005-2760(79)90248-0</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0005-2760</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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><istex><corpusName>elsevier</corpusName><author><json:item><name>Leiv Ose</name><affiliations><json:string>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</json:string></affiliations></json:item><json:item><name>Turid Ose</name><affiliations><json:string>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</json:string></affiliations></json:item><json:item><name>Kaare R. Norum</name><affiliations><json:string>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</json:string></affiliations></json:item><json:item><name>Trond Berg</name><affiliations><json:string>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>HDL</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Endocytosis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Lipoprotein metabolism</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Lysosome</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>(Rat liver</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Kupffer cell)</value></json:item></subject><language><json:string>eng</json:string></language><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.</abstract><qualityIndicators><score>8</score><pdfVersion>1.2</pdfVersion><pdfPageSize>468 x 684 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>6</keywordCount><abstractCharCount>1967</abstractCharCount><pdfWordCount>5305</pdfWordCount><pdfCharCount>36948</pdfCharCount><pdfPageCount>16</pdfPageCount><abstractWordCount>285</abstractWordCount></qualityIndicators><title>Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro</title><pii><json:string>0005-2760(79)90248-0</json:string></pii><genre><json:string>research-article</json:string></genre><host><volume>574</volume><pii><json:string>S0005-2760(00)X0303-7</json:string></pii><pages><last>536</last><first>521</first></pages><issn><json:string>0005-2760</json:string></issn><issue>3</issue><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><title>Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism</title><publicationDate>1979</publicationDate></host><categories><wos><json:string>BIOCHEMISTRY & MOLECULAR BIOLOGY</json:string><json:string>BIOPHYSICS</json:string></wos></categories><publicationDate>1979</publicationDate><copyrightDate>1979</copyrightDate><doi><json:string>10.1016/0005-2760(79)90248-0</json:string></doi><id>FDE907CA05675D68E34DDAD529E5B25D871FB804</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/FDE907CA05675D68E34DDAD529E5B25D871FB804/fulltext/pdf</uri></json:item><json:item><original>true</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/FDE907CA05675D68E34DDAD529E5B25D871FB804/fulltext/txt</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/FDE907CA05675D68E34DDAD529E5B25D871FB804/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/FDE907CA05675D68E34DDAD529E5B25D871FB804/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1979</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro</title><author><persName><forename type="first">Leiv</forename><surname>Ose</surname></persName><affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</affiliation></author><author><persName><forename type="first">Turid</forename><surname>Ose</surname></persName><affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</affiliation></author><author><persName><forename type="first">Kaare R.</forename><surname>Norum</surname></persName><affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</affiliation></author><author><persName><forename type="first">Trond</forename><surname>Berg</surname></persName><affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo, Norway</affiliation></author></analytic><monogr><title level="j">Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism</title><title level="j" type="abbrev">BBALIP</title><idno type="pISSN">0005-2760</idno><idno type="PII">S0005-2760(00)X0303-7</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="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></monogr><idno type="istex">FDE907CA05675D68E34DDAD529E5B25D871FB804</idno><idno type="DOI">10.1016/0005-2760(79)90248-0</idno><idno type="PII">0005-2760(79)90248-0</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1979</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>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.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>HDL</term></item><item><term>Endocytosis</term></item><item><term>Lipoprotein metabolism</term></item><item><term>Lysosome</term></item><item><term>(Rat liver</term></item><item><term>Kupffer cell)</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1979-03-15">Received</change><change when="1979">Published</change></revisionDesc></teiHeader></istex:fulltextTEI></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>BBALIP</jid><aid>79902480</aid><ce:pii>0005-2760(79)90248-0</ce:pii><ce:doi>10.1016/0005-2760(79)90248-0</ce:doi><ce:copyright type="unknown" year="1979"></ce:copyright></item-info><head><ce:title>Uptake and degradation of <ce:sup loc="pre">125</ce:sup>I-labelled high density lipoproteins in rat liver cells in vivo and in vitro</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, Oslo, Norway</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="15" month="3" year="1979"></ce:date-received><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para><ce:list><ce:list-item><ce:label>1.</ce:label><ce:para>1. The uptake of <ce:sup loc="pre">125</ce:sup>I-labelled high density lipoproteins (HDL) in various organs of the rat was determined after an intravenous injection. The uptake of <ce:sup>125</ce:sup>I-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 <ce:sup loc="pre">125</ce:sup>I-labelled HDL exceeded by far that of <ce:sup loc="pre">125</ce:sup>I-labelled polyvinylpyrrolidone in the liver, the kidneys, the spleen and the adrenals, indicating that the uptake of <ce:sup loc="pre">125</ce:sup>I-labelled HDL was mediated by adsorptive endocytosis.</ce:para></ce:list-item><ce:list-item><ce:label>2.</ce:label><ce:para>2. The in vivo uptake of <ce:sup loc="pre">125</ce:sup>I-labelled HDL was determined in purified hepatocytes and non-parenchymal cells prepared by collagenase perfusion of livers from animals after intravenous injections of <ce:sup loc="pre">125</ce:sup>I-labelled HDL. When expressed per cell, the hepatocytes and the non-parenchymal liver cells took up about the same amount of <ce:sup loc="pre">125</ce:sup>I-labelled HDL.</ce:para></ce:list-item><ce:list-item><ce:label>3.</ce:label><ce:para>3. The in vitro uptake and degradation of <ce:sup loc="pre">125</ce:sup>I-labelled HDL in isolated rat hepatocytes was studied. The uptake at increasing concentrations of <ce:sup loc="pre">125</ce:sup>I-labelled HDL was saturable indicating uptake mediated through binding sites. <ce:sup>125</ce:sup>I-labelled HDL were easily degraded by contaminating proteases from the perfusate.</ce:para></ce:list-item><ce:list-item><ce:label>4.</ce:label><ce:para>4. Subcellular fractionation by isopycnic centrifugation indicated that the accumulation of <ce:sup loc="pre">125</ce:sup>I-labelled HDL did not take place in the lysosomes, but rather on the plasma membrane and possibly in the endosomes (phagosomes).</ce:para></ce:list-item><ce:list-item><ce:label>5.</ce:label><ce:para>5. <ce:sup loc="pre">125</ce:sup>I-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 <ce:sup loc="pre">125</ce:sup>I-labelled acid-soluble radioactivity by the cells. Chloroquine, but not the protease inhibitor leupeptin, reduced the hydrolysis of the cholesteryl ester moiety of HDL.</ce:para></ce:list-item></ce:list></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 liver</ce:text></ce:keyword><ce:keyword><ce:text>Kupffer cell)</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Uptake and degradation of 125I-labelled high density lipoproteins in rat liver cells in vivo and in vitro</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Uptake and degradation of</title></titleInfo><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, Oslo, Norway</affiliation><role><roleTerm type="text">author</roleTerm></role></name><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, Oslo, Norway</affiliation><role><roleTerm type="text">author</roleTerm></role></name><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, Oslo, 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, Oslo, Norway</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1979</dateIssued><dateCaptured encoding="w3cdtf">1979-03-15</dateCaptured><copyrightDate encoding="w3cdtf">1979</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">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.</abstract><subject><genre>Keywords</genre><topic>HDL</topic><topic>Endocytosis</topic><topic>Lipoprotein metabolism</topic><topic>Lysosome</topic><topic>(Rat liver</topic><topic>Kupffer cell)</topic></subject><relatedItem type="host"><titleInfo><title>Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism</title></titleInfo><titleInfo type="abbreviated"><title>BBALIP</title></titleInfo><genre type="Journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19790928</dateIssued></originInfo><identifier type="ISSN">0005-2760</identifier><identifier type="PII">S0005-2760(00)X0303-7</identifier><part><date>19790928</date><detail type="volume"><number>574</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue pages"><start>369</start><end>552</end></extent><extent unit="pages"><start>521</start><end>536</end></extent></part></relatedItem><identifier type="istex">FDE907CA05675D68E34DDAD529E5B25D871FB804</identifier><identifier type="DOI">10.1016/0005-2760(79)90248-0</identifier><identifier type="PII">0005-2760(79)90248-0</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/FDE907CA05675D68E34DDAD529E5B25D871FB804/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">BIOCHEMISTRY & MOLECULAR BIOLOGY</classCode><classCode scheme="WOS">BIOPHYSICS</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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