ChloroquineV1, Main, Exploration, bibRecord, 002965

Inhibition of protein synthesis in small cell lung cancer cells induced by the diphtheria toxin-related fusion protein DAB389 GRP

Identifieur interne : 002965 ( Main/Exploration ); précédent : 002964; suivant : 002966

Inhibition of protein synthesis in small cell lung cancer cells induced by the diphtheria toxin-related fusion protein DAB389 GRP

Auteurs : J. C. Vanderspek [États-Unis] ; J. A. Sutherland [États-Unis] ; H. Zeng [États-Unis] ; J. F. Battey [États-Unis] ; R. T. Jensen [États-Unis] ; J. R. Murphy [États-Unis]

Source :

Cancer research : (Baltimore) [ 0008-5472 ] ; 1997.

RBID : Pascal:97-0163008

Descripteurs français

KwdFr :
- Animaux, Antienzymes (pharmacologie), Carcinome à petites cellules (enzymologie), Cellules 3T3, Cellules cancéreuses en culture, Données de séquences moléculaires, Humains, Peptides (génétique), Peptides (pharmacologie), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (pharmacologie), Rats, Souris, Séquence nucléotidique, Toxine diphtérique (génétique), Toxine diphtérique (pharmacologie), Tumeurs du poumon (enzymologie).
MESH :
- enzymologie : Carcinome à petites cellules, Tumeurs du poumon.
- génétique : Peptides, Protéines de fusion recombinantes, Toxine diphtérique.
- pharmacologie : Antienzymes, Peptides, Protéines de fusion recombinantes, Toxine diphtérique.
Pascal (Inist)
- Animaux, Cellules 3T3, Cellules cancéreuses en culture, Données de séquences moléculaires, Humains, Neuropeptide, Gastrine RH, Rats, Récepteur biologique, Protéine fusion, Souris, Séquence nucléotidique, Toxine, Diphtérie, Synthèse protéique, Lignée cellulaire établie, Carcinome petite cellule, Bronchopulmonaire, Cellule tumorale, In vitro, Cytotoxicité, Mécanisme action, Anticancéreux.

English descriptors

KwdEn :
- 3T3 Cells, Animals, Antineoplastic agent, Base Sequence, Biological receptor, Bronchopulmonary, Carcinoma, Small Cell (enzymology), Cytotoxicity, Diphtheria, Diphtheria Toxin (genetics), Diphtheria Toxin (pharmacology), Enzyme Inhibitors (pharmacology), Established cell line, Fusion protein, Gastrin releasing peptide, Humans, In vitro, Lung Neoplasms (enzymology), Mechanism of action, Mice, Molecular Sequence Data, Neuropeptide, Peptides (genetics), Peptides (pharmacology), Protein synthesis, Rats, Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (pharmacology), Small cell carcinoma, Toxin, Tumor Cells, Cultured, Tumor cell.
MESH :
- chemical , genetics : Diphtheria Toxin, Peptides, Recombinant Fusion Proteins.
- enzymology : Carcinoma, Small Cell, Lung Neoplasms.
- chemical , pharmacology : Diphtheria Toxin, Enzyme Inhibitors, Peptides, Recombinant Fusion Proteins.
- 3T3 Cells, Animals, Base Sequence, Humans, Mice, Molecular Sequence Data, Rats, Tumor Cells, Cultured.

Abstract

DAB₃₈₉, GRP is composed of the catalytic and transmembrane domains of diphtheria toxin fused to gastrin-releasing peptide (GRP). DAB₃₈₉ GRP is selectively targeted to, and inhibits protein synthesis in, cell lines expressing GRP receptors. Protein synthesis in 5'ET4 cells (BALB/3T3 fibroblasts transfected with the gene encoding the GRP receptor) was inhibited by 50% in the presence of 20 pM DAB₃₈₉ GRP (IC₅₀, 20 pM). DAB₃₈₉ GRP did not inhibit protein synthesis in untransfected BALB/3T3 cells. A second neuropeptide-conjugated toxin, DAB₃₈₉ SP, directed to cells expressing substance P receptors, was not cytotoxic to 5'ET4 cells, nor was DAB₃₈₉ GRP cytotoxic to substance P receptor-bearing cells. DAB₃₈₉GRP cytotoxic effects were receptor specific and were inhibited either by excess GRP or anti-GRP antibody. Cytotoxicity was mediated by passage through an acidic vesicle, because addition of 10 μM chloroquine to the reaction inhibited cytotoxicity. DAB₃₈₉ GRP and DAB₃₈₉ SP were tested on a number of tumor cell lines. DAB₃₈₉ GRP inhibited protein synthesis in AR42J rat pancreatic acinar cells and HuTu 80 human duodenal adenocarcinoma cells with IC₅₀s of 65 and 200 pM, respectively. DAB₃₈₉ SP had an IC₅₀of 9.5 pM for the AR42J cells and 12 nM for the HuTu 80 cell line. A number of small cell lung cancer cell (SCLC) lines were tested, and the IC₅₀ for DAB₃₈₉ GRP ranged from 1.1 to 85 nM. Sensitivity to DAB₃₈₉ GRP-appeared to be based on receptor number and receptor type (i.e., GRP or neuromedin B preferring). SCLC cells were also sensitive to DAB₃₈₉SP, with IC₅₀s ranging from 2.4 to 11.5 nM. These results suggest that a potential use exists for diphtheria-based fusion toxins as therapeutic agents for treatment of SCLC and other neuropeptide receptor-bearing cancers.

Affiliations:

États-Unis

Le document en format XML

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<series><title level="j" type="main">Cancer research : (Baltimore)</title>
<title level="j" type="abbreviated">Cancer res. : (Baltimore)</title>
<idno type="ISSN">0008-5472</idno>
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<seriesStmt><title level="j" type="main">Cancer research : (Baltimore)</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>3T3 Cells</term>
<term>Animals</term>
<term>Antineoplastic agent</term>
<term>Base Sequence</term>
<term>Biological receptor</term>
<term>Bronchopulmonary</term>
<term>Carcinoma, Small Cell (enzymology)</term>
<term>Cytotoxicity</term>
<term>Diphtheria</term>
<term>Diphtheria Toxin (genetics)</term>
<term>Diphtheria Toxin (pharmacology)</term>
<term>Enzyme Inhibitors (pharmacology)</term>
<term>Established cell line</term>
<term>Fusion protein</term>
<term>Gastrin releasing peptide</term>
<term>Humans</term>
<term>In vitro</term>
<term>Lung Neoplasms (enzymology)</term>
<term>Mechanism of action</term>
<term>Mice</term>
<term>Molecular Sequence Data</term>
<term>Neuropeptide</term>
<term>Peptides (genetics)</term>
<term>Peptides (pharmacology)</term>
<term>Protein synthesis</term>
<term>Rats</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (pharmacology)</term>
<term>Small cell carcinoma</term>
<term>Toxin</term>
<term>Tumor Cells, Cultured</term>
<term>Tumor cell</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Antienzymes (pharmacologie)</term>
<term>Carcinome à petites cellules (enzymologie)</term>
<term>Cellules 3T3</term>
<term>Cellules cancéreuses en culture</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Peptides (génétique)</term>
<term>Peptides (pharmacologie)</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (pharmacologie)</term>
<term>Rats</term>
<term>Souris</term>
<term>Séquence nucléotidique</term>
<term>Toxine diphtérique (génétique)</term>
<term>Toxine diphtérique (pharmacologie)</term>
<term>Tumeurs du poumon (enzymologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Diphtheria Toxin</term>
<term>Peptides</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Carcinome à petites cellules</term>
<term>Tumeurs du poumon</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Carcinoma, Small Cell</term>
<term>Lung Neoplasms</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peptides</term>
<term>Protéines de fusion recombinantes</term>
<term>Toxine diphtérique</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antienzymes</term>
<term>Peptides</term>
<term>Protéines de fusion recombinantes</term>
<term>Toxine diphtérique</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Diphtheria Toxin</term>
<term>Enzyme Inhibitors</term>
<term>Peptides</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>3T3 Cells</term>
<term>Animals</term>
<term>Base Sequence</term>
<term>Humans</term>
<term>Mice</term>
<term>Molecular Sequence Data</term>
<term>Rats</term>
<term>Tumor Cells, Cultured</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Animaux</term>
<term>Cellules 3T3</term>
<term>Cellules cancéreuses en culture</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Neuropeptide</term>
<term>Gastrine RH</term>
<term>Rats</term>
<term>Récepteur biologique</term>
<term>Protéine fusion</term>
<term>Souris</term>
<term>Séquence nucléotidique</term>
<term>Toxine</term>
<term>Diphtérie</term>
<term>Synthèse protéique</term>
<term>Lignée cellulaire établie</term>
<term>Carcinome petite cellule</term>
<term>Bronchopulmonaire</term>
<term>Cellule tumorale</term>
<term>In vitro</term>
<term>Cytotoxicité</term>
<term>Mécanisme action</term>
<term>Anticancéreux</term>
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<front><div type="abstract" xml:lang="en">DAB<sub>389</sub>
, GRP is composed of the catalytic and transmembrane domains of diphtheria toxin fused to gastrin-releasing peptide (GRP). DAB<sub>389</sub>
 GRP is selectively targeted to, and inhibits protein synthesis in, cell lines expressing GRP receptors. Protein synthesis in 5'ET4 cells (BALB/3T3 fibroblasts transfected with the gene encoding the GRP receptor) was inhibited by 50% in the presence of 20 pM DAB<sub>389</sub>
 GRP (IC<sub>50</sub>
, 20 pM). DAB<sub>389</sub>
 GRP did not inhibit protein synthesis in untransfected BALB/3T3 cells. A second neuropeptide-conjugated toxin, DAB<sub>389</sub>
 SP, directed to cells expressing substance P receptors, was not cytotoxic to 5'ET4 cells, nor was DAB<sub>389</sub>
 GRP cytotoxic to substance P receptor-bearing cells. DAB<sub>389</sub>
GRP cytotoxic effects were receptor specific and were inhibited either by excess GRP or anti-GRP antibody. Cytotoxicity was mediated by passage through an acidic vesicle, because addition of 10 μM chloroquine to the reaction inhibited cytotoxicity. DAB<sub>389</sub>
 GRP and DAB<sub>389</sub>
 SP were tested on a number of tumor cell lines. DAB<sub>389</sub>
 GRP inhibited protein synthesis in AR42J rat pancreatic acinar cells and HuTu 80 human duodenal adenocarcinoma cells with IC<sub>50</sub>
s of 65 and 200 pM, respectively. DAB<sub>389</sub>
 SP had an IC<sub>50</sub>
of 9.5 pM for the AR42J cells and 12 nM for the HuTu 80 cell line. A number of small cell lung cancer cell (SCLC) lines were tested, and the IC<sub>50</sub>
 for DAB<sub>389</sub>
 GRP ranged from 1.1 to 85 nM. Sensitivity to DAB<sub>389</sub>
 GRP-appeared to be based on receptor number and receptor type (i.e., GRP or neuromedin B preferring). SCLC cells were also sensitive to DAB<sub>389</sub>
SP, with IC<sub>50</sub>
s ranging from 2.4 to 11.5 nM. These results suggest that a potential use exists for diphtheria-based fusion toxins as therapeutic agents for treatment of SCLC and other neuropeptide receptor-bearing cancers.</div>
</front>
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<affiliations><list><country><li>États-Unis</li>
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<name sortKey="Murphy, J R" sort="Murphy, J R" uniqKey="Murphy J" first="J. R." last="Murphy">J. R. Murphy</name>
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Serveur d'exploration Chloroquine

Inhibition of protein synthesis in small cell lung cancer cells induced by the diphtheria toxin-related fusion protein DAB389 GRP

Inhibition of protein synthesis in small cell lung cancer cells induced by the diphtheria toxin-related fusion protein DAB389 GRP

Source :

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