Inhibition of EGF processing in responsive and nonresponsive human fibroblastsx
Identifieur interne : 003249 ( Main/Exploration ); précédent : 003248; suivant : 003250Inhibition of EGF processing in responsive and nonresponsive human fibroblastsx
Auteurs : R. Paul Schaudies ; H. Linton WraySource :
- Journal of Cellular Physiology [ 0021-9541 ] ; 1988-04.
Descripteurs français
- KwdFr :
- Animaux, Cellules cultivées, Chloroquine (pharmacologie), Cinétique, Facteur de croissance épidermique (génétique), Facteur de croissance épidermique (métabolisme), Humains, Leupeptines (pharmacologie), Maturation post-traductionnelle des protéines, Mâle, Peau (cytologie), Poumon (cytologie), Radio-isotopes de l'iode, Souris.
- MESH :
- cytologie : Peau, Poumon.
- génétique : Facteur de croissance épidermique.
- métabolisme : Facteur de croissance épidermique.
- pharmacologie : Chloroquine, Leupeptines.
- Animaux, Cellules cultivées, Cinétique, Humains, Maturation post-traductionnelle des protéines, Mâle, Radio-isotopes de l'iode, Souris.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Epidermal Growth Factor.
- chemical , metabolism : Epidermal Growth Factor.
- chemical , pharmacology : Chloroquine, Leupeptins.
- cytology : Lung, Skin.
- Teeft :
- Animals, Binding medium, Bovine serum albumin, Carboxy terminal, Carboxy terminus, Carboxyl terminus, Cell culture, Cell division, Cell line, Cell lines, Cell types, Cells, Cultured, Chloroquine, Clinical investigation, Complete degradation, Confluent cultures, Constant presence, Continual uptake, Control cultures, Culture dishes, Cytoplasmic domain, Degradation, Electrophoretic, Electrophoretic mobilities, Electrophoretic profiles, Epidermal, Epidermal growth factor, Fetal lung fibroblasts, Fibroblast, Final concentration, Growth factor, Growth induction, Growth response, Growth stimulation, High level, Hormonal processing, Hormone processing, Human fibroblasts, Human foreskin fibroblasts, Humans, Incubation, Incubation medium, Inhibitor, Intracellular, Intracellular processing, Iodine Radioisotopes, Kinase, Kinetics, Leupeptin, Lung fibroblasts, Male, Maximum level, Mice, Nondenaturing, Nondenaturing polyacrylamide, Nonresponsive, Nonresponsive cell lines, Nonresponsive cells, Nonresponsive cultures, Pglml leupeptin, Polyacrylamide, Protein Processing, Post-Translational, Proteolytic enzymes, Radioactivity, Radiolabel, Radiolabeled hormone, Receptor, Responsive, Responsive cells, Saturating levels, Schaudies, Specific events, Test tube, Time points, Walter reed army.
Abstract
We have examined the proteolytic processing of radiolabeled epidermal growth factor (EGF) in EGF growth‐responsive human foreskin fibroblasts (HFF) versus EGF nonresponsive human fetal lung fibroblasts (HFL). Previous studies (Schaudies et al., 1985) have shown that both cell lines demonstrate similar binding affinities and numbers of binding sites, as well as similar rates of internalization and degradation of the bound, radiolabeled hormone. We have used nondenaturing electrophoresis to compare how these two cell lines process EGF at its carboxy terminus. EGF lacking either one [des‐(53)‐EGF] or six [des (48–53)‐EGF] carboxy terminal amino acids could be distinguished by this method. Chloroquine or leupeptin were added to the incubatin system in an attempt to accentuate potential differences in hormonal processing between the responsive and nonresponsive cell lines. In the absence of inhibitors, the responsive and nonresponsive cells generated similar distributions of processed forms of EGF after 30‐minutes incubation. However after 4‐hours incubation in the constant presence of 125I‐EGF, the electrophoretic profiles of extracted hormone were substantially different. The radiolable within the responsive cells, as well as that released from them, migrated predominantly at the dye front, indicating complete degradation of EGF. In contrast, the majority of the radiolabel within the nonresponsive cells migrated as partially processed forms of hormone, while the released radiolabel migrated at the dye front. Addition of chloroquine to either cell line inhibited processing of EGF beyond removal of the carboxyl terminal arginine residue. Both intact 125I‐EGF, and 125I‐EGF lacking the carboxyl terminal arginine were released from chloroquine‐treated cells in a ratio equal to that present in the intact cells. Incubations in leupeptin, proteolysis of EGF beyond the des‐(48–53)‐EGF was blocked; however, no large‐molecular‐weight species were released from the cells under these conditions.
Url:
DOI: 10.1002/jcp.1041350111
Affiliations:
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Le document en format XML
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<term>Cells, Cultured</term>
<term>Chloroquine (pharmacology)</term>
<term>Epidermal Growth Factor (genetics)</term>
<term>Epidermal Growth Factor (metabolism)</term>
<term>Humans</term>
<term>Iodine Radioisotopes</term>
<term>Kinetics</term>
<term>Leupeptins (pharmacology)</term>
<term>Lung (cytology)</term>
<term>Male</term>
<term>Mice</term>
<term>Protein Processing, Post-Translational</term>
<term>Skin (cytology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Cellules cultivées</term>
<term>Chloroquine (pharmacologie)</term>
<term>Cinétique</term>
<term>Facteur de croissance épidermique (génétique)</term>
<term>Facteur de croissance épidermique (métabolisme)</term>
<term>Humains</term>
<term>Leupeptines (pharmacologie)</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Mâle</term>
<term>Peau (cytologie)</term>
<term>Poumon (cytologie)</term>
<term>Radio-isotopes de l'iode</term>
<term>Souris</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Epidermal Growth Factor</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Epidermal Growth Factor</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Chloroquine</term>
<term>Leupeptins</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Peau</term>
<term>Poumon</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Lung</term>
<term>Skin</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Facteur de croissance épidermique</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteur de croissance épidermique</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Chloroquine</term>
<term>Leupeptines</term>
</keywords>
<keywords scheme="Teeft" xml:lang="en"><term>Animals</term>
<term>Binding medium</term>
<term>Bovine serum albumin</term>
<term>Carboxy terminal</term>
<term>Carboxy terminus</term>
<term>Carboxyl terminus</term>
<term>Cell culture</term>
<term>Cell division</term>
<term>Cell line</term>
<term>Cell lines</term>
<term>Cell types</term>
<term>Cells, Cultured</term>
<term>Chloroquine</term>
<term>Clinical investigation</term>
<term>Complete degradation</term>
<term>Confluent cultures</term>
<term>Constant presence</term>
<term>Continual uptake</term>
<term>Control cultures</term>
<term>Culture dishes</term>
<term>Cytoplasmic domain</term>
<term>Degradation</term>
<term>Electrophoretic</term>
<term>Electrophoretic mobilities</term>
<term>Electrophoretic profiles</term>
<term>Epidermal</term>
<term>Epidermal growth factor</term>
<term>Fetal lung fibroblasts</term>
<term>Fibroblast</term>
<term>Final concentration</term>
<term>Growth factor</term>
<term>Growth induction</term>
<term>Growth response</term>
<term>Growth stimulation</term>
<term>High level</term>
<term>Hormonal processing</term>
<term>Hormone processing</term>
<term>Human fibroblasts</term>
<term>Human foreskin fibroblasts</term>
<term>Humans</term>
<term>Incubation</term>
<term>Incubation medium</term>
<term>Inhibitor</term>
<term>Intracellular</term>
<term>Intracellular processing</term>
<term>Iodine Radioisotopes</term>
<term>Kinase</term>
<term>Kinetics</term>
<term>Leupeptin</term>
<term>Lung fibroblasts</term>
<term>Male</term>
<term>Maximum level</term>
<term>Mice</term>
<term>Nondenaturing</term>
<term>Nondenaturing polyacrylamide</term>
<term>Nonresponsive</term>
<term>Nonresponsive cell lines</term>
<term>Nonresponsive cells</term>
<term>Nonresponsive cultures</term>
<term>Pglml leupeptin</term>
<term>Polyacrylamide</term>
<term>Protein Processing, Post-Translational</term>
<term>Proteolytic enzymes</term>
<term>Radioactivity</term>
<term>Radiolabel</term>
<term>Radiolabeled hormone</term>
<term>Receptor</term>
<term>Responsive</term>
<term>Responsive cells</term>
<term>Saturating levels</term>
<term>Schaudies</term>
<term>Specific events</term>
<term>Test tube</term>
<term>Time points</term>
<term>Walter reed army</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules cultivées</term>
<term>Cinétique</term>
<term>Humains</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Mâle</term>
<term>Radio-isotopes de l'iode</term>
<term>Souris</term>
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<front><div type="abstract" xml:lang="fr">We have examined the proteolytic processing of radiolabeled epidermal growth factor (EGF) in EGF growth‐responsive human foreskin fibroblasts (HFF) versus EGF nonresponsive human fetal lung fibroblasts (HFL). Previous studies (Schaudies et al., 1985) have shown that both cell lines demonstrate similar binding affinities and numbers of binding sites, as well as similar rates of internalization and degradation of the bound, radiolabeled hormone. We have used nondenaturing electrophoresis to compare how these two cell lines process EGF at its carboxy terminus. EGF lacking either one [des‐(53)‐EGF] or six [des (48–53)‐EGF] carboxy terminal amino acids could be distinguished by this method. Chloroquine or leupeptin were added to the incubatin system in an attempt to accentuate potential differences in hormonal processing between the responsive and nonresponsive cell lines. In the absence of inhibitors, the responsive and nonresponsive cells generated similar distributions of processed forms of EGF after 30‐minutes incubation. However after 4‐hours incubation in the constant presence of 125I‐EGF, the electrophoretic profiles of extracted hormone were substantially different. The radiolable within the responsive cells, as well as that released from them, migrated predominantly at the dye front, indicating complete degradation of EGF. In contrast, the majority of the radiolabel within the nonresponsive cells migrated as partially processed forms of hormone, while the released radiolabel migrated at the dye front. Addition of chloroquine to either cell line inhibited processing of EGF beyond removal of the carboxyl terminal arginine residue. Both intact 125I‐EGF, and 125I‐EGF lacking the carboxyl terminal arginine were released from chloroquine‐treated cells in a ratio equal to that present in the intact cells. Incubations in leupeptin, proteolysis of EGF beyond the des‐(48–53)‐EGF was blocked; however, no large‐molecular‐weight species were released from the cells under these conditions.</div>
</front>
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<tree><noCountry><name sortKey="Schaudies, R Paul" sort="Schaudies, R Paul" uniqKey="Schaudies R" first="R. Paul" last="Schaudies">R. Paul Schaudies</name>
<name sortKey="Wray, H Linton" sort="Wray, H Linton" uniqKey="Wray H" first="H. Linton" last="Wray">H. Linton Wray</name>
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