Effect of brefeldin A and lysosomotropic reagents on intracellular trafficking of epidermal growth factor and transferrin in Madin-Darby canine kidney epithelial cells
Identifieur interne : 002762 ( Main/Exploration ); précédent : 002761; suivant : 002763Effect of brefeldin A and lysosomotropic reagents on intracellular trafficking of epidermal growth factor and transferrin in Madin-Darby canine kidney epithelial cells
Auteurs : Yoshihisa Shitara [Japon] ; Yukio Kato [Japon] ; Yuichi Sugiyama [Japon]Source :
- Journal of Controlled Release [ 0168-3659 ] ; 1998.
English descriptors
- Teeft :
- Ammonium, Ammonium chloride, Amount transcytosed, Apical, Apical medium, Apical side, Basal, Basal side, Biol, Brefeldin, Canine kidney, Cell monolayer, Cell monolayers, Chem, Chloroquine, Degradation, Different cell preparations, Epidermal, Epidermal growth factor, Epithelial, Epithelial cells, Error bars, Excess conditions, Golgi apparatus, Initial ligand concentration, Internalization, Intracellular, Kinetic analysis, Ligand, Lysosomal degradation, Lysosomotropic, Lysosomotropic reagents, Mdck, Mdck cell monolayers, Mdck cells, Molecular weight, Molecular weights, Monensin, Monolayers, Nonsp, Other hand, Paracellular penetration, Peptide, Rate constants, Reagent, Receptor, Shitara, Tracer conditions, Trans, Transcellular, Transcellular transport, Transcytosed, Transcytosis, Transferrin, Transport buffer.
Abstract
Abstract: To regulate intracellular sorting of epidermal growth factor (EGF) or transferrin (Tf), the effect of brefeldin A (BFA) or lysosomotropic reagents was investigated. To examine the effect of them on the net transcellular transport of 125I-EGF or 125I-Tf, their transcytosis was investigated in the presence or absence of reagents. For the investigation of their fate after internalization, radiolabeled ligands were internalized at 37°C, followed by extensive washing and subsequent incubation at 37°C in the ligand-free medium (pulse-chase study). BFA enhanced transcytosis of 125I-Tf, but had no effect on 125I-EGF. Kinetic analysis in the pulse-chase study showed that BFA does not affect cell-surface binding or intracellular sorting of EGF, while it only increases the transcytosis rate constant of Tf. From the lysosomotropic reagents study, both ammonium chloride and monensin suppressed transcytosis and recycling as well as the degradation of EGF, while both chloroquine and bafilomycin A selectively suppressed the degradation process with only a minimal effect on transcytosis, resulting in an increase in the amount transcytosed. It is concluded the that enhancement effect of BFA on transcytosis depends upon the type of receptor targeted. Lysosomotropic reagents can be divided into two types as far as the specificity of the effect on the net amount of EGF transcytosed in Madin-Darby canine kidney (MDCK) cells is concerned.
Url:
DOI: 10.1016/S0168-3659(98)00025-X
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 000C62
- to stream Istex, to step Curation: 000C62
- to stream Istex, to step Checkpoint: 001566
- to stream Main, to step Merge: 002804
- to stream Main, to step Curation: 002762
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Effect of brefeldin A and lysosomotropic reagents on intracellular trafficking of epidermal growth factor and transferrin in Madin-Darby canine kidney epithelial cells</title><author><name sortKey="Shitara, Yoshihisa" sort="Shitara, Yoshihisa" uniqKey="Shitara Y" first="Yoshihisa" last="Shitara">Yoshihisa Shitara</name></author><author><name sortKey="Kato, Yukio" sort="Kato, Yukio" uniqKey="Kato Y" first="Yukio" last="Kato">Yukio Kato</name></author><author><name sortKey="Sugiyama, Yuichi" sort="Sugiyama, Yuichi" uniqKey="Sugiyama Y" first="Yuichi" last="Sugiyama">Yuichi Sugiyama</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:61EB33E2568872787686D24944FC5177F771C261</idno><date when="1998" year="1998">1998</date><idno type="doi">10.1016/S0168-3659(98)00025-X</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-LWMCRNR3-6/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000C62</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000C62</idno><idno type="wicri:Area/Istex/Curation">000C62</idno><idno type="wicri:Area/Istex/Checkpoint">001566</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001566</idno><idno type="wicri:doubleKey">0168-3659:1998:Shitara Y:effect:of:brefeldin</idno><idno type="wicri:Area/Main/Merge">002804</idno><idno type="wicri:Area/Main/Curation">002762</idno><idno type="wicri:Area/Main/Exploration">002762</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Effect of brefeldin A and lysosomotropic reagents on intracellular trafficking of epidermal growth factor and transferrin in Madin-Darby canine kidney epithelial cells</title><author><name sortKey="Shitara, Yoshihisa" sort="Shitara, Yoshihisa" uniqKey="Shitara Y" first="Yoshihisa" last="Shitara">Yoshihisa Shitara</name><affiliation wicri:level="4"><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName><orgName type="university">Université de Tokyo</orgName><placeName><settlement type="city">Tokyo</settlement><region type="province">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Kato, Yukio" sort="Kato, Yukio" uniqKey="Kato Y" first="Yukio" last="Kato">Yukio Kato</name><affiliation wicri:level="4"><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName><orgName type="university">Université de Tokyo</orgName><placeName><settlement type="city">Tokyo</settlement><region type="province">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Sugiyama, Yuichi" sort="Sugiyama, Yuichi" uniqKey="Sugiyama Y" first="Yuichi" last="Sugiyama">Yuichi Sugiyama</name><affiliation wicri:level="4"><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName><orgName type="university">Université de Tokyo</orgName><placeName><settlement type="city">Tokyo</settlement><region type="province">Région de Kantō</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Controlled Release</title><title level="j" type="abbrev">COREL</title><idno type="ISSN">0168-3659</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">55</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="35">35</biblScope><biblScope unit="page" to="43">43</biblScope></imprint><idno type="ISSN">0168-3659</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0168-3659</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Ammonium</term><term>Ammonium chloride</term><term>Amount transcytosed</term><term>Apical</term><term>Apical medium</term><term>Apical side</term><term>Basal</term><term>Basal side</term><term>Biol</term><term>Brefeldin</term><term>Canine kidney</term><term>Cell monolayer</term><term>Cell monolayers</term><term>Chem</term><term>Chloroquine</term><term>Degradation</term><term>Different cell preparations</term><term>Epidermal</term><term>Epidermal growth factor</term><term>Epithelial</term><term>Epithelial cells</term><term>Error bars</term><term>Excess conditions</term><term>Golgi apparatus</term><term>Initial ligand concentration</term><term>Internalization</term><term>Intracellular</term><term>Kinetic analysis</term><term>Ligand</term><term>Lysosomal degradation</term><term>Lysosomotropic</term><term>Lysosomotropic reagents</term><term>Mdck</term><term>Mdck cell monolayers</term><term>Mdck cells</term><term>Molecular weight</term><term>Molecular weights</term><term>Monensin</term><term>Monolayers</term><term>Nonsp</term><term>Other hand</term><term>Paracellular penetration</term><term>Peptide</term><term>Rate constants</term><term>Reagent</term><term>Receptor</term><term>Shitara</term><term>Tracer conditions</term><term>Trans</term><term>Transcellular</term><term>Transcellular transport</term><term>Transcytosed</term><term>Transcytosis</term><term>Transferrin</term><term>Transport buffer</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: To regulate intracellular sorting of epidermal growth factor (EGF) or transferrin (Tf), the effect of brefeldin A (BFA) or lysosomotropic reagents was investigated. To examine the effect of them on the net transcellular transport of 125I-EGF or 125I-Tf, their transcytosis was investigated in the presence or absence of reagents. For the investigation of their fate after internalization, radiolabeled ligands were internalized at 37°C, followed by extensive washing and subsequent incubation at 37°C in the ligand-free medium (pulse-chase study). BFA enhanced transcytosis of 125I-Tf, but had no effect on 125I-EGF. Kinetic analysis in the pulse-chase study showed that BFA does not affect cell-surface binding or intracellular sorting of EGF, while it only increases the transcytosis rate constant of Tf. From the lysosomotropic reagents study, both ammonium chloride and monensin suppressed transcytosis and recycling as well as the degradation of EGF, while both chloroquine and bafilomycin A selectively suppressed the degradation process with only a minimal effect on transcytosis, resulting in an increase in the amount transcytosed. It is concluded the that enhancement effect of BFA on transcytosis depends upon the type of receptor targeted. Lysosomotropic reagents can be divided into two types as far as the specificity of the effect on the net amount of EGF transcytosed in Madin-Darby canine kidney (MDCK) cells is concerned.</div></front></TEI><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><country name="Japon"><region name="Région de Kantō"><name sortKey="Shitara, Yoshihisa" sort="Shitara, Yoshihisa" uniqKey="Shitara Y" first="Yoshihisa" last="Shitara">Yoshihisa Shitara</name></region><name sortKey="Kato, Yukio" sort="Kato, Yukio" uniqKey="Kato Y" first="Yukio" last="Kato">Yukio Kato</name><name sortKey="Sugiyama, Yuichi" sort="Sugiyama, Yuichi" uniqKey="Sugiyama Y" first="Yuichi" last="Sugiyama">Yuichi Sugiyama</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/ChloroquineV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002762 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002762 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= ChloroquineV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= ISTEX:61EB33E2568872787686D24944FC5177F771C261
|texte= Effect of brefeldin A and lysosomotropic reagents on intracellular trafficking of epidermal growth factor and transferrin in Madin-Darby canine kidney epithelial cells
}}
| This area was generated with Dilib version V0.6.33. |  |