The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes
Identifieur interne : 000952 ( Istex/Corpus ); précédent : 000951; suivant : 000953The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes
Auteurs : Leiv Ose ; Ingeborg R Ken ; Kaare R. Norum ; Trond BergSource :
- 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
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ISTEX:E44F954904C2488575A980B5FBD4270EC46FB1D9Le document en format XML
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Norum</name><affiliation><mods:affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo 3, 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 3, Norway</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:E44F954904C2488575A980B5FBD4270EC46FB1D9</idno><date when="1980" year="1980">1980</date><idno type="doi">10.1016/0014-4827(80)90049-X</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-TD358NFB-8/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000952</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000952</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes</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 3, Norway</mods:affiliation></affiliation></author><author><name sortKey="R Ken, Ingeborg" sort="R Ken, Ingeborg" uniqKey="R Ken I" first="Ingeborg" last="R Ken">Ingeborg R Ken</name><affiliation><mods:affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo 3, 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 3, 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 3, Norway</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Experimental Cell Research</title><title level="j" type="abbrev">YEXCR</title><idno type="ISSN">0014-4827</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1980">1980</date><biblScope unit="volume">130</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="127">127</biblScope><biblScope unit="page" to="135">135</biblScope></imprint><idno type="ISSN">0014-4827</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0014-4827</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acid phosphatase</term><term>Acta</term><term>Adsorptive endocytosis</term><term>Ammonia</term><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><term>Control cells</term><term>Control values</term><term>Cpmlng protein</term><term>Degradation</term><term>Hepatocytes</term><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><term>Vivo</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><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></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>hepatocytes</json:string><json:string>leupeptin</json:string><json:string>colchicine</json:string><json:string>chloroquine</json:string><json:string>ammonia</json:string><json:string>degradation</json:string><json:string>lipoprotein</json:string><json:string>subcellular</json:string><json:string>biochem</json:string><json:string>lysosome</json:string><json:string>microtubuli</json:string><json:string>intracellular</json:string><json:string>lysosomal</json:string><json:string>biol</json:string><json:string>acta</json:string><json:string>sucrose</json:string><json:string>microfilaments</json:string><json:string>incubation medium</json:string><json:string>biochim biophys acta</json:string><json:string>acid phosphatase</json:string><json:string>cell suspension</json:string><json:string>tail vein</json:string><json:string>vivo</json:string><json:string>berg</json:string><json:string>centrifugation</json:string><json:string>inhibitor</json:string><json:string>radioactivity</json:string><json:string>bovine serum albumin</json:string><json:string>high density lipoproteins</json:string><json:string>cellular degradation</json:string><json:string>cpmlng protein</json:string><json:string>control values</json:string><json:string>adsorptive endocytosis</json:string><json:string>control cells</json:string><json:string>lysosomal function</json:string><json:string>isopycnic centrifugation</json:string></teeft></keywords><author><json:item><name>Leiv Ose</name><affiliations><json:string>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo 3, Norway</json:string></affiliations></json:item><json:item><name>Ingeborg Røken</name><affiliations><json:string>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo 3, 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 3, 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 3, Norway</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-TD358NFB-8</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><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.</abstract><qualityIndicators><refBibsNative>true</refBibsNative><abstractWordCount>226</abstractWordCount><abstractCharCount>1526</abstractCharCount><keywordCount>0</keywordCount><score>9.184</score><pdfWordCount>4472</pdfWordCount><pdfCharCount>26802</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>9</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize></qualityIndicators><title>The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes</title><pmid><json:string>7192635</json:string></pmid><pii><json:string>0014-4827(80)90049-X</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Experimental Cell Research</title><language><json:string>unknown</json:string></language><publicationDate>1980</publicationDate><issn><json:string>0014-4827</json:string></issn><pii><json:string>S0014-4827(00)X0505-8</json:string></pii><volume>130</volume><issue>1</issue><pages><first>127</first><last>135</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>12s</json:string><json:string>1980</json:string></date><geogName></geogName><orgName><json:string>Sigma Chemical Co</json:string><json:string>Koch-Light Laboratories</json:string><json:string>Norwegian Research Council for Science</json:string><json:string>Norway SUMMARY Degradation</json:string><json:string>Landsforeningen for Hjerte</json:string><json:string>Hjelpestikkenes Medisinske Forskningsfond</json:string><json:string>Anders Jahres Foundation</json:string><json:string>Norwegian Council on Cardiovascular Disease</json:string><json:string>Langfeldts Fond</json:string></orgName><orgName_funder><json:string>Landsforeningen for Hjerte</json:string><json:string>Hjelpestikkenes Medisinske Forskningsfond</json:string><json:string>Anders Jahres Foundation</json:string><json:string>Norwegian Council on Cardiovascular Disease</json:string><json:string>Langfeldts Fond</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Turid Ose</json:string></persName><placeName><json:string>Norway</json:string><json:string>Copenhagen</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>[45]</json:string><json:string>Ose et al.</json:string><json:string>Bilheimer et al. 1221</json:string><json:string>[29]</json:string><json:string>[3,4,5,6]</json:string><json:string>[44]</json:string><json:string>[ 1251]</json:string><json:string>[8]</json:string><json:string>[43]</json:string><json:string>[16]</json:string><json:string>[39,42]</json:string><json:string>[31]</json:string><json:string>[5]</json:string><json:string>[37]</json:string><json:string>[30]</json:string><json:string>Lowry et al. [35]</json:string><json:string>[7]</json:string><json:string>[ 1,2]</json:string><json:string>[36]</json:string><json:string>[9]</json:string><json:string>[40]</json:string><json:string>[13]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-TD358NFB-8</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - oncology</json:string><json:string>2 - cell biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Cell Biology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences medicales</json:string></inist></categories><publicationDate>1980</publicationDate><copyrightDate>1980</copyrightDate><doi><json:string>10.1016/0014-4827(80)90049-X</json:string></doi><id>E44F954904C2488575A980B5FBD4270EC46FB1D9</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-TD358NFB-8/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-TD358NFB-8/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-TD358NFB-8/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1980</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note>The project was also supported by grants from the Anders Jahres Foundation, Hjelpestikkenes Medisinske Forskningsfond, Langfeldts Fond, the Norwegian Council on Cardiovascular Disease, and Landsforeningen for Hjerte- og Lungesyke.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes</title><author xml:id="author-0000"><persName><forename type="first">Leiv</forename><surname>Ose</surname></persName><note type="biography">One of the authors (L. O.) is a Fellow of the Norwegian Research Council for Science and the Humanities.</note><affiliation>One of the authors (L. O.) is a Fellow of the Norwegian Research Council for Science and the Humanities.</affiliation><affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo 3, Norway</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Ingeborg</forename><surname>Røken</surname></persName><affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo 3, Norway</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Kaare R.</forename><surname>Norum</surname></persName><affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo 3, Norway</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Trond</forename><surname>Berg</surname></persName><affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo 3, Norway</affiliation></author><idno type="istex">E44F954904C2488575A980B5FBD4270EC46FB1D9</idno><idno type="ark">ark:/67375/6H6-TD358NFB-8</idno><idno type="DOI">10.1016/0014-4827(80)90049-X</idno><idno type="PII">0014-4827(80)90049-X</idno></analytic><monogr><title level="j">Experimental Cell Research</title><title level="j" type="abbrev">YEXCR</title><idno type="pISSN">0014-4827</idno><idno type="PII">S0014-4827(00)X0505-8</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1980"></date><biblScope unit="volume">130</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="127">127</biblScope><biblScope unit="page" to="135">135</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1980</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>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.</p></abstract></profileDesc><revisionDesc><change when="1980-05-21">Modified</change><change when="1980">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-TD358NFB-8/fulltext.txt</uri></json:item></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>YEXCR</jid><aid>8090049X</aid><ce:pii>0014-4827(80)90049-X</ce:pii><ce:doi>10.1016/0014-4827(80)90049-X</ce:doi><ce:copyright type="unknown" year="1980"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>The project was also supported by grants from the Anders Jahres Foundation, Hjelpestikkenes Medisinske Forskningsfond, Langfeldts Fond, the Norwegian Council on Cardiovascular Disease, and Landsforeningen for Hjerte- og Lungesyke.</ce:note-para></ce:article-footnote><ce:title>The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes</ce:title><ce:author-group><ce:author><ce:given-name>Leiv</ce:given-name><ce:surname>Ose</ce:surname><ce:cross-ref refid="FN1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Ingeborg</ce:given-name><ce:surname>Røken</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 3, Norway</ce:textfn></ce:affiliation><ce:footnote id="FN1"><ce:label>1</ce:label><ce:note-para>One of the authors (L. O.) is a Fellow of the Norwegian Research Council for Science and the Humanities.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="4" month="3" year="1980"></ce:date-received><ce:date-revised day="21" month="5" year="1980"></ce:date-revised><ce:date-accepted day="23" month="5" year="1980"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Degradation of <ce:sup loc="pre">125</ce:sup>I-labelled HDL ([<ce:sup loc="pre">125</ce:sup>I]HDL) was measured in isolated rat hepatocytes that had been preincubated with [<ce:sup loc="pre">125</ce:sup>I]HDL and then reincubated in fresh medium without [<ce:sup loc="pre">125</ce:sup>I]HDL. About 5 % of the [<ce:sup loc="pre">125</ce:sup>I]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 [<ce:sup loc="pre">125</ce:sup>I]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 [<ce:sup loc="pre">125</ce:sup>I]HDL associated with cells in vivo after intravenous injection was also studied in isolated cells. About 8.5% of the [<ce:sup loc="pre">125</ce:sup>I]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 [<ce:sup loc="pre">125</ce:sup>I]HDL taken up in vivo and in vitro. Subcellular fractionation by centrifugation in sucrose gradients indicated that [<ce:sup loc="pre">125</ce:sup>I]HDL associated with hepatocytes in vivo are primarily accumulated in lysosomes. [<ce:sup loc="pre">125</ce:sup>I]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 [<ce:sup loc="pre">125</ce:sup>I]HDL in rat hepatocytes is relatively slow. The intracellular degradation of the apoproteins of HDL is at least partly lysosomal.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>The effect of ammonia, chloroquine, leupeptin, colchicine and cytochalasin B on degradation of high density lipoproteins in isolated rat hepatocytes</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 3, Norway</affiliation><description>One of the authors (L. O.) is a Fellow of the Norwegian Research Council for Science and the Humanities.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ingeborg</namePart><namePart type="family">Røken</namePart><affiliation>Institute for Nutrition Research, School of Medicine, University of Oslo, Blindern, Oslo 3, 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 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, Oslo 3, Norway</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1980</dateIssued><dateModified encoding="w3cdtf">1980-05-21</dateModified><copyrightDate encoding="w3cdtf">1980</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract 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.</abstract><note>The project was also supported by grants from the Anders Jahres Foundation, Hjelpestikkenes Medisinske Forskningsfond, Langfeldts Fond, the Norwegian Council on Cardiovascular Disease, and Landsforeningen for Hjerte- og Lungesyke.</note><relatedItem type="host"><titleInfo><title>Experimental Cell Research</title></titleInfo><titleInfo type="abbreviated"><title>YEXCR</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1980</dateIssued></originInfo><identifier type="ISSN">0014-4827</identifier><identifier type="PII">S0014-4827(00)X0505-8</identifier><part><date>1980</date><detail type="volume"><number>130</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>250</end></extent><extent unit="pages"><start>127</start><end>135</end></extent></part></relatedItem><identifier type="istex">E44F954904C2488575A980B5FBD4270EC46FB1D9</identifier><identifier type="ark">ark:/67375/6H6-TD358NFB-8</identifier><identifier type="DOI">10.1016/0014-4827(80)90049-X</identifier><identifier type="PII">0014-4827(80)90049-X</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-TD358NFB-8/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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