Rapid mitogen-induced aminopeptidase N surface expression in human T cells is dominated by mechanisms independent of de novo protein biosynthesis
Identifieur interne : 001989 ( Main/Exploration ); précédent : 001988; suivant : 001990Rapid mitogen-induced aminopeptidase N surface expression in human T cells is dominated by mechanisms independent of de novo protein biosynthesis
Auteurs : Uwe Lendeckel [Allemagne] ; Thomas Wex [Allemagne] ; Annelore Ittenson [Allemagne] ; Marco Arndt [Allemagne] ; Karin Frank [Allemagne] ; Oleg Mayboroda [Allemagne] ; Walter Schubert [Allemagne] ; Siegfried Ansorge [Allemagne]Source :
- 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
Affiliations:
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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><affiliations><list><country><li>Allemagne</li></country><region><li>Saxe-Anhalt</li></region><settlement><li>Magdebourg</li></settlement></list><tree><country name="Allemagne"><region name="Saxe-Anhalt"><name sortKey="Lendeckel, Uwe" sort="Lendeckel, Uwe" uniqKey="Lendeckel U" first="Uwe" last="Lendeckel">Uwe Lendeckel</name></region><name sortKey="Ansorge, Siegfried" sort="Ansorge, Siegfried" uniqKey="Ansorge S" first="Siegfried" last="Ansorge">Siegfried Ansorge</name><name sortKey="Arndt, Marco" sort="Arndt, Marco" uniqKey="Arndt M" first="Marco" last="Arndt">Marco Arndt</name><name sortKey="Frank, Karin" sort="Frank, Karin" uniqKey="Frank K" first="Karin" last="Frank">Karin Frank</name><name sortKey="Ittenson, Annelore" sort="Ittenson, Annelore" uniqKey="Ittenson A" first="Annelore" last="Ittenson">Annelore Ittenson</name><name sortKey="Lendeckel, Uwe" sort="Lendeckel, Uwe" uniqKey="Lendeckel U" first="Uwe" last="Lendeckel">Uwe Lendeckel</name><name sortKey="Mayboroda, Oleg" sort="Mayboroda, Oleg" uniqKey="Mayboroda O" first="Oleg" last="Mayboroda">Oleg Mayboroda</name><name sortKey="Schubert, Walter" sort="Schubert, Walter" uniqKey="Schubert W" first="Walter" last="Schubert">Walter Schubert</name><name sortKey="Wex, Thomas" sort="Wex, Thomas" uniqKey="Wex T" first="Thomas" last="Wex">Thomas Wex</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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