Rapid mitogen-induced aminopeptidase N surface expression in human T cells is dominated by mechanisms independent of de novo protein biosynthesis
Identifieur interne : 000662 ( Istex/Corpus ); précédent : 000661; suivant : 000663Rapid mitogen-induced aminopeptidase N surface expression in human T cells is dominated by mechanisms independent of de novo protein biosynthesis
Auteurs : Uwe Lendeckel ; Thomas Wex ; Annelore Ittenson ; Marco Arndt ; Karin Frank ; Oleg Mayboroda ; Walter Schubert ; Siegfried AnsorgeSource :
- Immunobiology [ 0171-2985 ] ; 1997.
English descriptors
- KwdEn :
- Teeft :
- Aminopeptidase, Ansorge, Biosynthesis, Boehringer mannheim, Cell activation, Cell lines, Cell surface, Cycloheximide, Dipeptidyl peptidase, Enzymatic activity, Febs lett, Gene expression, Glycosylation, Human aminopeptidase, Hydrolysing activity, Immunofluorescence microscopy, Induction, Inhibitor, Internal medicine, Intestinal brush border enzymes, Intestinal microvillar proteins, Lendeckel, Lymphoblastic leukemia, Membrane expression, Mitogenic, Mitogenic activation, Mitogenic stimulation, Myeloid, Natural killer cells, Peripheral blood, Positive cells, Primary antibody, Protein biosynthesis, Puromycin, Rapid degradation, Rapid induction, Rapid surface expression, Room temperature, Slight increase, Surface expression, Synovial fluid, Tumor invasion, Tunicamycin.
Abstract
Abstract: The membrane bound metalloprotease aminopeptidase N (APN, CD13, EC 3.4.11.2) is a well established marker of normal and malignant cells of the myelo-monocytic lineage. It is also expressed by leukaemic blasts of a small group of patients suffering from acute or chronic lymphoid leukaemia. Recently, the expression of the APN gene in T cell lines as well as the induction of APN gene and surface expression in human peripheral T cells by mitogenic activation have been demonstrated. Here, by means of cytofluorimetric analysis evidence is provided, that the induction of APN surface expression is partially resistent to the action of the inhibitors of protein biosynthesis, puromycin and cycloheximide, and is not prevented by tunicamycin, an inhibitor of glycosylation.These data suggest that the rapid mitogen-induced surface expression of APN, detectable 20 hours after stimulation is dominated by mechanisms not dependent on de novo protein biosynthesis or glycosylation. As shown by simultaneous analyses, the inhibitors used did also differently modify the induction of surface expression of other inducible glycosylated leukocyte surface antigens, namely CD25, CD69 and CD95.
Url:
DOI: 10.1016/S0171-2985(97)80057-5
Links to Exploration step
ISTEX:23E6E8EAF317FDFDF3BBB786FD3F671D657CE7E3Le document en format XML
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Germany</mods:affiliation></affiliation></author><author><name sortKey="Frank, Karin" sort="Frank, Karin" uniqKey="Frank K" first="Karin" last="Frank">Karin Frank</name><affiliation><mods:affiliation>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</mods:affiliation></affiliation></author><author><name sortKey="Mayboroda, Oleg" sort="Mayboroda, Oleg" uniqKey="Mayboroda O" first="Oleg" last="Mayboroda">Oleg Mayboroda</name><affiliation><mods:affiliation>Institute of Medical Neurobiology, Otto von Guericke University Magdeburg, Magdeburg, Germany</mods:affiliation></affiliation></author><author><name sortKey="Schubert, Walter" sort="Schubert, Walter" uniqKey="Schubert W" first="Walter" last="Schubert">Walter Schubert</name><affiliation><mods:affiliation>Institute of Medical Neurobiology, Otto von Guericke University Magdeburg, Magdeburg, Germany</mods:affiliation></affiliation></author><author><name sortKey="Ansorge, Siegfried" sort="Ansorge, Siegfried" uniqKey="Ansorge S" first="Siegfried" last="Ansorge">Siegfried Ansorge</name><affiliation><mods:affiliation>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Immunobiology</title><title level="j" type="abbrev">IMBIO</title><idno type="ISSN">0171-2985</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997">1997</date><biblScope unit="volume">197</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="55">55</biblScope><biblScope unit="page" to="69">69</biblScope></imprint><idno type="ISSN">0171-2985</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0171-2985</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>APN</term><term>CD</term><term>CHX</term><term>PBS</term><term>PHA</term><term>PMA</term><term>PP</term><term>mAb</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Aminopeptidase</term><term>Ansorge</term><term>Biosynthesis</term><term>Boehringer mannheim</term><term>Cell activation</term><term>Cell lines</term><term>Cell surface</term><term>Cycloheximide</term><term>Dipeptidyl peptidase</term><term>Enzymatic activity</term><term>Febs lett</term><term>Gene expression</term><term>Glycosylation</term><term>Human aminopeptidase</term><term>Hydrolysing activity</term><term>Immunofluorescence microscopy</term><term>Induction</term><term>Inhibitor</term><term>Internal medicine</term><term>Intestinal brush border enzymes</term><term>Intestinal microvillar proteins</term><term>Lendeckel</term><term>Lymphoblastic leukemia</term><term>Membrane expression</term><term>Mitogenic</term><term>Mitogenic activation</term><term>Mitogenic stimulation</term><term>Myeloid</term><term>Natural killer cells</term><term>Peripheral blood</term><term>Positive cells</term><term>Primary antibody</term><term>Protein biosynthesis</term><term>Puromycin</term><term>Rapid degradation</term><term>Rapid induction</term><term>Rapid surface expression</term><term>Room temperature</term><term>Slight increase</term><term>Surface expression</term><term>Synovial fluid</term><term>Tumor invasion</term><term>Tunicamycin</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The membrane bound metalloprotease aminopeptidase N (APN, CD13, EC 3.4.11.2) is a well established marker of normal and malignant cells of the myelo-monocytic lineage. It is also expressed by leukaemic blasts of a small group of patients suffering from acute or chronic lymphoid leukaemia. Recently, the expression of the APN gene in T cell lines as well as the induction of APN gene and surface expression in human peripheral T cells by mitogenic activation have been demonstrated. Here, by means of cytofluorimetric analysis evidence is provided, that the induction of APN surface expression is partially resistent to the action of the inhibitors of protein biosynthesis, puromycin and cycloheximide, and is not prevented by tunicamycin, an inhibitor of glycosylation.These data suggest that the rapid mitogen-induced surface expression of APN, detectable 20 hours after stimulation is dominated by mechanisms not dependent on de novo protein biosynthesis or glycosylation. As shown by simultaneous analyses, the inhibitors used did also differently modify the induction of surface expression of other inducible glycosylated leukocyte surface antigens, namely CD25, CD69 and CD95.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>aminopeptidase</json:string><json:string>surface expression</json:string><json:string>tunicamycin</json:string><json:string>biosynthesis</json:string><json:string>protein biosynthesis</json:string><json:string>cycloheximide</json:string><json:string>puromycin</json:string><json:string>glycosylation</json:string><json:string>mitogenic</json:string><json:string>lendeckel</json:string><json:string>ansorge</json:string><json:string>mitogenic activation</json:string><json:string>inhibitor</json:string><json:string>cell lines</json:string><json:string>cell activation</json:string><json:string>positive cells</json:string><json:string>mitogenic stimulation</json:string><json:string>myeloid</json:string><json:string>cell surface</json:string><json:string>synovial fluid</json:string><json:string>immunofluorescence microscopy</json:string><json:string>rapid induction</json:string><json:string>lymphoblastic leukemia</json:string><json:string>induction</json:string><json:string>primary antibody</json:string><json:string>tumor invasion</json:string><json:string>peripheral blood</json:string><json:string>natural killer cells</json:string><json:string>enzymatic activity</json:string><json:string>slight increase</json:string><json:string>rapid surface expression</json:string><json:string>hydrolysing activity</json:string><json:string>internal medicine</json:string><json:string>rapid degradation</json:string><json:string>membrane expression</json:string><json:string>gene expression</json:string><json:string>human aminopeptidase</json:string><json:string>dipeptidyl peptidase</json:string><json:string>febs lett</json:string><json:string>boehringer mannheim</json:string><json:string>room temperature</json:string><json:string>intestinal microvillar proteins</json:string><json:string>intestinal brush border enzymes</json:string></teeft></keywords><author><json:item><name>Uwe Lendeckel</name><affiliations><json:string>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</json:string><json:string>3Uwe Lendeckel, University of Magdeburg, Center of Internal Medicine, Institute of Experimental Internal Medicine, Leipziger Str. 44, D-39120 Magdeburg, Germany</json:string></affiliations></json:item><json:item><name>Thomas Wex</name><affiliations><json:string>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</json:string></affiliations></json:item><json:item><name>Annelore Ittenson</name><affiliations><json:string>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</json:string></affiliations></json:item><json:item><name>Marco Arndt</name><affiliations><json:string>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</json:string></affiliations></json:item><json:item><name>Karin Frank</name><affiliations><json:string>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</json:string></affiliations></json:item><json:item><name>Oleg Mayboroda</name><affiliations><json:string>Institute of Medical Neurobiology, Otto von Guericke University Magdeburg, Magdeburg, Germany</json:string></affiliations></json:item><json:item><name>Walter Schubert</name><affiliations><json:string>Institute of Medical Neurobiology, Otto von Guericke University Magdeburg, Magdeburg, Germany</json:string></affiliations></json:item><json:item><name>Siegfried Ansorge</name><affiliations><json:string>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>APN : aminopeptidase N</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CD : cluster of differentiation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CHX : cycloheximide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>mAb : monoclonal antibody</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PBS : phosphate buffered saline</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PHA : phytohemagglutinine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PMA : phorbol 12-myristate 13-acetate 4-O-methyl ether</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PP : PHA/PMA</value></json:item></subject><articleId><json:string>80057</json:string></articleId><arkIstex>ark:/67375/6H6-05B7238K-H</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The membrane bound metalloprotease aminopeptidase N (APN, CD13, EC 3.4.11.2) is a well established marker of normal and malignant cells of the myelo-monocytic lineage. It is also expressed by leukaemic blasts of a small group of patients suffering from acute or chronic lymphoid leukaemia. Recently, the expression of the APN gene in T cell lines as well as the induction of APN gene and surface expression in human peripheral T cells by mitogenic activation have been demonstrated. Here, by means of cytofluorimetric analysis evidence is provided, that the induction of APN surface expression is partially resistent to the action of the inhibitors of protein biosynthesis, puromycin and cycloheximide, and is not prevented by tunicamycin, an inhibitor of glycosylation.These data suggest that the rapid mitogen-induced surface expression of APN, detectable 20 hours after stimulation is dominated by mechanisms not dependent on de novo protein biosynthesis or glycosylation. As shown by simultaneous analyses, the inhibitors used did also differently modify the induction of surface expression of other inducible glycosylated leukocyte surface antigens, namely CD25, CD69 and CD95.</abstract><qualityIndicators><score>8.686</score><pdfWordCount>4574</pdfWordCount><pdfCharCount>27493</pdfCharCount><pdfVersion>1.7</pdfVersion><pdfPageCount>15</pdfPageCount><pdfPageSize>439.2 x 712.8 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>176</abstractWordCount><abstractCharCount>1192</abstractCharCount><keywordCount>8</keywordCount></qualityIndicators><title>Rapid mitogen-induced aminopeptidase N surface expression in human T cells is dominated by mechanisms independent of de novo protein 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scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>©1997 Gustav Fischer Verlag</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</p></availability><date>1997</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></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Rapid mitogen-induced aminopeptidase N surface expression in human T cells is dominated by mechanisms independent of de novo protein biosynthesis</title><author xml:id="author-0000"><persName><forename type="first">Uwe</forename><surname>Lendeckel</surname></persName><affiliation>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</affiliation><affiliation>3Uwe Lendeckel, University of Magdeburg, Center of Internal Medicine, Institute of Experimental Internal Medicine, Leipziger Str. 44, D-39120 Magdeburg, Germany</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Thomas</forename><surname>Wex</surname></persName><affiliation>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Annelore</forename><surname>Ittenson</surname></persName><affiliation>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Marco</forename><surname>Arndt</surname></persName><affiliation>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Karin</forename><surname>Frank</surname></persName><affiliation>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</affiliation></author><author xml:id="author-0005"><persName><forename type="first">Oleg</forename><surname>Mayboroda</surname></persName><affiliation>Institute of Medical Neurobiology, Otto von Guericke University Magdeburg, Magdeburg, Germany</affiliation></author><author xml:id="author-0006"><persName><forename type="first">Walter</forename><surname>Schubert</surname></persName><affiliation>Institute of Medical Neurobiology, Otto von Guericke University Magdeburg, Magdeburg, Germany</affiliation></author><author xml:id="author-0007"><persName><forename type="first">Siegfried</forename><surname>Ansorge</surname></persName><affiliation>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</affiliation></author><idno type="istex">23E6E8EAF317FDFDF3BBB786FD3F671D657CE7E3</idno><idno type="ark">ark:/67375/6H6-05B7238K-H</idno><idno type="DOI">10.1016/S0171-2985(97)80057-5</idno><idno type="PII">S0171-2985(97)80057-5</idno><idno type="article-id">80057</idno></analytic><monogr><title level="j">Immunobiology</title><title level="j" type="abbrev">IMBIO</title><idno type="pISSN">0171-2985</idno><idno type="PII">S0171-2985(97)X8052-0</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997"></date><biblScope unit="volume">197</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="55">55</biblScope><biblScope unit="page" to="69">69</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1997</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The membrane bound metalloprotease aminopeptidase N (APN, CD13, EC 3.4.11.2) is a well established marker of normal and malignant cells of the myelo-monocytic lineage. It is also expressed by leukaemic blasts of a small group of patients suffering from acute or chronic lymphoid leukaemia. Recently, the expression of the APN gene in T cell lines as well as the induction of APN gene and surface expression in human peripheral T cells by mitogenic activation have been demonstrated. Here, by means of cytofluorimetric analysis evidence is provided, that the induction of APN surface expression is partially resistent to the action of the inhibitors of protein biosynthesis, puromycin and cycloheximide, and is not prevented by tunicamycin, an inhibitor of glycosylation.These data suggest that the rapid mitogen-induced surface expression of APN, detectable 20 hours after stimulation is dominated by mechanisms not dependent on de novo protein biosynthesis or glycosylation. As shown by simultaneous analyses, the inhibitors used did also differently modify the induction of surface expression of other inducible glycosylated leukocyte surface antigens, namely CD25, CD69 and CD95.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>APN</term><term>aminopeptidase N</term></item><item><term>CD</term><term>cluster of differentiation</term></item><item><term>CHX</term><term>cycloheximide</term></item><item><term>mAb</term><term>monoclonal antibody</term></item><item><term>PBS</term><term>phosphate buffered saline</term></item><item><term>PHA</term><term>phytohemagglutinine</term></item><item><term>PMA</term><term>phorbol 12-myristate 13-acetate 4-O-methyl ether</term></item><item><term>PP</term><term>PHA/PMA</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1997">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-05B7238K-H/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier doc found" wicri:toSee="Elsevier, no converted or simple article"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" </istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 5.1.0//EN//XML" URI="art510.dtd" name="istex:docType"></istex:docType><istex:document><article version="5.1" xml:lang="en" docsubtype="fla"><item-info><jid>IMBIO</jid><aid>80057</aid><ce:pii>S0171-2985(97)80057-5</ce:pii><ce:doi>10.1016/S0171-2985(97)80057-5</ce:doi><ce:copyright type="other" year="1997">Gustav Fischer Verlag</ce:copyright></item-info><head><ce:title>Rapid mitogen-induced aminopeptidase N surface expression in human T cells is dominated by mechanisms independent of <ce:italic>de novo</ce:italic> protein biosynthesis</ce:title><ce:author-group><ce:author><ce:given-name>Uwe</ce:given-name><ce:surname>Lendeckel</ce:surname><ce:cross-ref refid="aff1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="fn3"><ce:sup>3</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Thomas</ce:given-name><ce:surname>Wex</ce:surname><ce:cross-ref refid="aff1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Annelore</ce:given-name><ce:surname>Ittenson</ce:surname><ce:cross-ref refid="aff1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Marco</ce:given-name><ce:surname>Arndt</ce:surname><ce:cross-ref refid="aff1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Karin</ce:given-name><ce:surname>Frank</ce:surname><ce:cross-ref refid="aff1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Oleg</ce:given-name><ce:surname>Mayboroda</ce:surname><ce:cross-ref refid="aff2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Walter</ce:given-name><ce:surname>Schubert</ce:surname><ce:cross-ref refid="aff2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Siegfried</ce:given-name><ce:surname>Ansorge</ce:surname><ce:cross-ref refid="aff1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="aff1"><ce:label>1</ce:label><ce:textfn>Institute of Experimental Internal Medicine, Center of Internal Medicine, Magdeburg, Germany</ce:textfn></ce:affiliation><ce:affiliation id="aff2"><ce:label>2</ce:label><ce:textfn>Institute of Medical Neurobiology, Otto von Guericke University Magdeburg, Magdeburg, Germany</ce:textfn></ce:affiliation><ce:footnote id="fn3"><ce:label>3</ce:label><ce:note-para>Uwe Lendeckel, University of Magdeburg, Center of Internal Medicine, Institute of Experimental Internal Medicine, Leipziger Str. 44, D-39120 Magdeburg, Germany</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="16" month="7" year="1996"></ce:date-received><ce:date-accepted day="17" month="2" year="1997"></ce:date-accepted><ce:abstract id="ab1"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para id="SP0005">The membrane bound metalloprotease aminopeptidase N (APN, CD13, EC 3.4.11.2) is a well established marker of normal and malignant cells of the myelo-monocytic lineage. It is also expressed by leukaemic blasts of a small group of patients suffering from acute or chronic lymphoid leukaemia. Recently, the expression of the APN gene in T cell lines as well as the induction of APN gene and surface expression in human peripheral T cells by mitogenic activation have been demonstrated. Here, by means of cytofluorimetric analysis evidence is provided, that the induction of APN surface expression is partially resistent to the action of the inhibitors of protein biosynthesis, puromycin and cycloheximide, and is not prevented by tunicamycin, an inhibitor of glycosylation.</ce:simple-para><ce:simple-para id="SP0010">These data suggest that the rapid mitogen-induced surface expression of APN, detectable 20 hours after stimulation is dominated by mechanisms not dependent on <ce:italic>de novo</ce:italic> protein biosynthesis or glycosylation. As shown by simultaneous analyses, the inhibitors used did also differently modify the induction of surface expression of other inducible glycosylated leukocyte surface antigens, namely CD25, CD69 and CD95.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>APN</ce:text><ce:keyword><ce:text>aminopeptidase N</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>CD</ce:text><ce:keyword><ce:text>cluster of differentiation</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>CHX</ce:text><ce:keyword><ce:text>cycloheximide</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>mAb</ce:text><ce:keyword><ce:text>monoclonal antibody</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>PBS</ce:text><ce:keyword><ce:text>phosphate buffered saline</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>PHA</ce:text><ce:keyword><ce:text>phytohemagglutinine</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>PMA</ce:text><ce:keyword><ce:text>phorbol 12-myristate 13-acetate 4-O-methyl ether</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>PP</ce:text><ce:keyword><ce:text>PHA/PMA</ce:text></ce:keyword></ce:keyword></ce:keywords></head><tail><ce:bibliography id="R0005"><ce:section-title>References</ce:section-title><ce:bibliography-sec id="RS0005"><ce:bib-reference id="bib1"><ce:label>1.</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>V.M.</ce:given-name><ce:surname>Watt</ce:surname></sb:author><sb:author><ce:given-name>H.F.</ce:given-name><ce:surname>Willard</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>The human aminopeptidase N gene: isolation, chromosome localization, and DNA polymorphism analysis</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Hum. 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It is also expressed by leukaemic blasts of a small group of patients suffering from acute or chronic lymphoid leukaemia. Recently, the expression of the APN gene in T cell lines as well as the induction of APN gene and surface expression in human peripheral T cells by mitogenic activation have been demonstrated. Here, by means of cytofluorimetric analysis evidence is provided, that the induction of APN surface expression is partially resistent to the action of the inhibitors of protein biosynthesis, puromycin and cycloheximide, and is not prevented by tunicamycin, an inhibitor of glycosylation.These data suggest that the rapid mitogen-induced surface expression of APN, detectable 20 hours after stimulation is dominated by mechanisms not dependent on de novo protein biosynthesis or glycosylation. As shown by simultaneous analyses, the inhibitors used did also differently modify the induction of surface expression of other inducible glycosylated leukocyte surface antigens, namely CD25, CD69 and CD95.</abstract><subject lang="en"><genre>Abbreviations</genre><topic>APN : aminopeptidase N</topic><topic>CD : cluster of differentiation</topic><topic>CHX : cycloheximide</topic><topic>mAb : monoclonal antibody</topic><topic>PBS : phosphate buffered saline</topic><topic>PHA : phytohemagglutinine</topic><topic>PMA : phorbol 12-myristate 13-acetate 4-O-methyl ether</topic><topic>PP : PHA/PMA</topic></subject><relatedItem type="host"><titleInfo><title>Immunobiology</title></titleInfo><titleInfo type="abbreviated"><title>IMBIO</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">1997</dateIssued></originInfo><identifier type="ISSN">0171-2985</identifier><identifier type="PII">S0171-2985(97)X8052-0</identifier><part><date>1997</date><detail type="volume"><number>197</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>132</end></extent><extent unit="pages"><start>55</start><end>69</end></extent></part></relatedItem><identifier type="istex">23E6E8EAF317FDFDF3BBB786FD3F671D657CE7E3</identifier><identifier type="ark">ark:/67375/6H6-05B7238K-H</identifier><identifier type="DOI">10.1016/S0171-2985(97)80057-5</identifier><identifier type="PII">S0171-2985(97)80057-5</identifier><identifier type="ArticleID">80057</identifier><accessCondition type="use and reproduction" contentType="copyright">©1997 Gustav Fischer Verlag</accessCondition><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><recordOrigin>Gustav Fischer Verlag, ©1997</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-05B7238K-H/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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