The epidermal growth factor receptor antibody cetuximab induces autophagy in cancer cells by downregulating HIF-1alpha and Bcl-2 and activating the beclin 1/hVps34 complex.
Identifieur interne : 000138 ( Ncbi/Merge ); précédent : 000137; suivant : 000139The epidermal growth factor receptor antibody cetuximab induces autophagy in cancer cells by downregulating HIF-1alpha and Bcl-2 and activating the beclin 1/hVps34 complex.
Auteurs : Xinqun Li [États-Unis] ; Zhen FanSource :
- Cancer research [ 1538-7445 ] ; 2010.
Descripteurs français
- KwdFr :
- Adénocarcinome (anatomopathologie), Adénocarcinome (traitement médicamenteux), Anticorps monoclonaux (pharmacologie), Anticorps monoclonaux humanisés, Autophagie (), Bécline-1, Carcinome pulmonaire non à petites cellules (anatomopathologie), Carcinome pulmonaire non à petites cellules (traitement médicamenteux), Carcinome épidermoïde (anatomopathologie), Carcinome épidermoïde (traitement médicamenteux), Cétuximab, Femelle, Humains, MAP Kinase Kinase Kinases (antagonistes et inhibiteurs), MAP Kinase Kinase Kinases (métabolisme), Phosphatidylinositol 3-kinases (métabolisme), Protein-Serine-Threonine Kinases (métabolisme), Protéines du transport vésiculaire (métabolisme), Protéines et peptides de signalisation intracellulaire (métabolisme), Protéines membranaires (métabolisme), Protéines proto-oncogènes c-akt (antagonistes et inhibiteurs), Protéines proto-oncogènes c-akt (métabolisme), Protéines proto-oncogènes c-bcl-2 (biosynthèse), Protéines proto-oncogènes c-bcl-2 (génétique), Protéines régulatrices de l'apoptose (métabolisme), Récepteurs ErbB (antagonistes et inhibiteurs), Régulation négative (), Sous-unité alpha du facteur-1 induit par l'hypoxie (biosynthèse), Sous-unité alpha du facteur-1 induit par l'hypoxie (génétique), Sérine-thréonine kinases TOR, Tumeurs (anatomopathologie), Tumeurs (métabolisme), Tumeurs (traitement médicamenteux), Tumeurs colorectales (anatomopathologie), Tumeurs colorectales (traitement médicamenteux), Tumeurs de la vulve (anatomopathologie), Tumeurs de la vulve (traitement médicamenteux), Tumeurs du poumon (anatomopathologie), Tumeurs du poumon (traitement médicamenteux).
- MESH :
- anatomopathologie : Adénocarcinome, Carcinome pulmonaire non à petites cellules, Carcinome épidermoïde, Tumeurs, Tumeurs colorectales, Tumeurs de la vulve, Tumeurs du poumon.
- antagonistes et inhibiteurs : MAP Kinase Kinase Kinases, Protéines proto-oncogènes c-akt, Récepteurs ErbB.
- biosynthèse : Protéines proto-oncogènes c-bcl-2, Sous-unité alpha du facteur-1 induit par l'hypoxie.
- génétique : Protéines proto-oncogènes c-bcl-2, Sous-unité alpha du facteur-1 induit par l'hypoxie.
- métabolisme : MAP Kinase Kinase Kinases, Phosphatidylinositol 3-kinases, Protein-Serine-Threonine Kinases, Protéines du transport vésiculaire, Protéines et peptides de signalisation intracellulaire, Protéines membranaires, Protéines proto-oncogènes c-akt, Protéines régulatrices de l'apoptose, Tumeurs.
- pharmacologie : Anticorps monoclonaux.
- traitement médicamenteux : Adénocarcinome, Carcinome pulmonaire non à petites cellules, Carcinome épidermoïde, Tumeurs, Tumeurs colorectales, Tumeurs de la vulve, Tumeurs du poumon.
- Anticorps monoclonaux humanisés, Autophagie, Bécline-1, Cétuximab, Femelle, Humains, Régulation négative, Sérine-thréonine kinases TOR.
English descriptors
- KwdEn :
- Adenocarcinoma (drug therapy), Adenocarcinoma (pathology), Antibodies, Monoclonal (pharmacology), Antibodies, Monoclonal, Humanized, Apoptosis Regulatory Proteins (metabolism), Autophagy (drug effects), Beclin-1, Carcinoma, Non-Small-Cell Lung (drug therapy), Carcinoma, Non-Small-Cell Lung (pathology), Carcinoma, Squamous Cell (drug therapy), Carcinoma, Squamous Cell (pathology), Cetuximab, Colorectal Neoplasms (drug therapy), Colorectal Neoplasms (pathology), Down-Regulation (drug effects), ErbB Receptors (antagonists & inhibitors), Female, Humans, Hypoxia-Inducible Factor 1, alpha Subunit (biosynthesis), Hypoxia-Inducible Factor 1, alpha Subunit (genetics), Intracellular Signaling Peptides and Proteins (metabolism), Lung Neoplasms (drug therapy), Lung Neoplasms (pathology), MAP Kinase Kinase Kinases (antagonists & inhibitors), MAP Kinase Kinase Kinases (metabolism), Membrane Proteins (metabolism), Neoplasms (drug therapy), Neoplasms (metabolism), Neoplasms (pathology), Phosphatidylinositol 3-Kinases (metabolism), Phosphoinositide-3 Kinase Inhibitors, Protein-Serine-Threonine Kinases (metabolism), Proto-Oncogene Proteins c-akt (antagonists & inhibitors), Proto-Oncogene Proteins c-akt (metabolism), Proto-Oncogene Proteins c-bcl-2 (biosynthesis), Proto-Oncogene Proteins c-bcl-2 (genetics), TOR Serine-Threonine Kinases, Vesicular Transport Proteins (metabolism), Vulvar Neoplasms (drug therapy), Vulvar Neoplasms (pathology).
- MESH :
- chemical , antagonists & inhibitors : ErbB Receptors, MAP Kinase Kinase Kinases, Proto-Oncogene Proteins c-akt.
- chemical , biosynthesis : Hypoxia-Inducible Factor 1, alpha Subunit, Proto-Oncogene Proteins c-bcl-2.
- chemical , genetics : Hypoxia-Inducible Factor 1, alpha Subunit, Proto-Oncogene Proteins c-bcl-2.
- chemical , metabolism : Apoptosis Regulatory Proteins, Intracellular Signaling Peptides and Proteins, MAP Kinase Kinase Kinases, Membrane Proteins, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins c-akt, Vesicular Transport Proteins.
- chemical , pharmacology : Antibodies, Monoclonal.
- drug effects : Autophagy, Down-Regulation.
- drug therapy : Adenocarcinoma, Carcinoma, Non-Small-Cell Lung, Carcinoma, Squamous Cell, Colorectal Neoplasms, Lung Neoplasms, Neoplasms, Vulvar Neoplasms.
- metabolism : Neoplasms, Phosphatidylinositol 3-Kinases.
- pathology : Adenocarcinoma, Carcinoma, Non-Small-Cell Lung, Carcinoma, Squamous Cell, Colorectal Neoplasms, Lung Neoplasms, Neoplasms, Vulvar Neoplasms.
- chemical : Antibodies, Monoclonal, Humanized, Beclin-1, Cetuximab, Female, Humans, Phosphoinositide-3 Kinase Inhibitors, TOR Serine-Threonine Kinases.
Abstract
Autophagy is a regulated catabolic process triggered in cells deprived of nutrients or growth factors that govern nutrient uptake. Here, we report that autophagy is induced by cetuximab, a therapeutic antibody that blocks epidermal growth factor receptor function. Cancer cell treatment with cetuximab triggered autophagosome formation, conversion of microtubule-associated protein 1 light chain 3 from its cytoplasmic to membrane-associated form, and increased acidic vesicular organelle formation. Autophagy occurred when cetuximab inhibited the class I phosphoinositide 3-kinase (PI3K)/Akt/mammalian target of rapamycin pathway, but not when it inhibited only the mitogen-activated protein/extracellular signal-regulated kinase kinase/Erk pathway, and it was accompanied by decreased levels of hypoxia inducible factor-1 alpha (HIF-1alpha) and Bcl-2. Stable overexpression of a HIF-1alpha mutant prevented cetuximab-induced autophagy and decrease in Bcl-2 levels. Knockdown of autophagy regulator beclin 1 or cell treatment with autophagy inhibitor 3-methyladenine, a class III PI3K (hVps34) inhibitor, also inhibited cetuximab-induced autophagy. Furthermore, knockdown of beclin 1 or Atg7 or treatment with the lysosome inhibitor chloroquine sensitized cancer cells to cetuximab-induced apoptosis. Mechanistic analysis argued that cetuximab acted by promoting an association between beclin 1 and hVps34, which was inhibited by overexpression of Bcl-2. Our findings suggest that the autophagy protects cancer cells from the proapoptotic effects of cetuximab.
DOI: 10.1158/0008-5472.CAN-10-0157
PubMed: 20634405
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 000395
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- to stream PubMed, to step Checkpoint: 000381
Links to Exploration step
pubmed:20634405Le document en format XML
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<term>Adenocarcinoma (pathology)</term>
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<term>Antibodies, Monoclonal, Humanized</term>
<term>Apoptosis Regulatory Proteins (metabolism)</term>
<term>Autophagy (drug effects)</term>
<term>Beclin-1</term>
<term>Carcinoma, Non-Small-Cell Lung (drug therapy)</term>
<term>Carcinoma, Non-Small-Cell Lung (pathology)</term>
<term>Carcinoma, Squamous Cell (drug therapy)</term>
<term>Carcinoma, Squamous Cell (pathology)</term>
<term>Cetuximab</term>
<term>Colorectal Neoplasms (drug therapy)</term>
<term>Colorectal Neoplasms (pathology)</term>
<term>Down-Regulation (drug effects)</term>
<term>ErbB Receptors (antagonists & inhibitors)</term>
<term>Female</term>
<term>Humans</term>
<term>Hypoxia-Inducible Factor 1, alpha Subunit (biosynthesis)</term>
<term>Hypoxia-Inducible Factor 1, alpha Subunit (genetics)</term>
<term>Intracellular Signaling Peptides and Proteins (metabolism)</term>
<term>Lung Neoplasms (drug therapy)</term>
<term>Lung Neoplasms (pathology)</term>
<term>MAP Kinase Kinase Kinases (antagonists & inhibitors)</term>
<term>MAP Kinase Kinase Kinases (metabolism)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Neoplasms (drug therapy)</term>
<term>Neoplasms (metabolism)</term>
<term>Neoplasms (pathology)</term>
<term>Phosphatidylinositol 3-Kinases (metabolism)</term>
<term>Phosphoinositide-3 Kinase Inhibitors</term>
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<term>TOR Serine-Threonine Kinases</term>
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<term>Proto-Oncogene Proteins c-akt</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Hypoxia-Inducible Factor 1, alpha Subunit</term>
<term>Proto-Oncogene Proteins c-bcl-2</term>
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<term>Intracellular Signaling Peptides and Proteins</term>
<term>MAP Kinase Kinase Kinases</term>
<term>Membrane Proteins</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Proto-Oncogene Proteins c-akt</term>
<term>Vesicular Transport Proteins</term>
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<term>Carcinome épidermoïde</term>
<term>Tumeurs</term>
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<term>Tumeurs de la vulve</term>
<term>Tumeurs du poumon</term>
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<term>Récepteurs ErbB</term>
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<term>Carcinoma, Non-Small-Cell Lung</term>
<term>Carcinoma, Squamous Cell</term>
<term>Colorectal Neoplasms</term>
<term>Lung Neoplasms</term>
<term>Neoplasms</term>
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<term>Phosphatidylinositol 3-Kinases</term>
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<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines du transport vésiculaire</term>
<term>Protéines et peptides de signalisation intracellulaire</term>
<term>Protéines membranaires</term>
<term>Protéines proto-oncogènes c-akt</term>
<term>Protéines régulatrices de l'apoptose</term>
<term>Tumeurs</term>
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<term>Carcinoma, Non-Small-Cell Lung</term>
<term>Carcinoma, Squamous Cell</term>
<term>Colorectal Neoplasms</term>
<term>Lung Neoplasms</term>
<term>Neoplasms</term>
<term>Vulvar Neoplasms</term>
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</keywords>
<keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Adénocarcinome</term>
<term>Carcinome pulmonaire non à petites cellules</term>
<term>Carcinome épidermoïde</term>
<term>Tumeurs</term>
<term>Tumeurs colorectales</term>
<term>Tumeurs de la vulve</term>
<term>Tumeurs du poumon</term>
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<term>Beclin-1</term>
<term>Cetuximab</term>
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<term>Autophagie</term>
<term>Bécline-1</term>
<term>Cétuximab</term>
<term>Femelle</term>
<term>Humains</term>
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<front><div type="abstract" xml:lang="en">Autophagy is a regulated catabolic process triggered in cells deprived of nutrients or growth factors that govern nutrient uptake. Here, we report that autophagy is induced by cetuximab, a therapeutic antibody that blocks epidermal growth factor receptor function. Cancer cell treatment with cetuximab triggered autophagosome formation, conversion of microtubule-associated protein 1 light chain 3 from its cytoplasmic to membrane-associated form, and increased acidic vesicular organelle formation. Autophagy occurred when cetuximab inhibited the class I phosphoinositide 3-kinase (PI3K)/Akt/mammalian target of rapamycin pathway, but not when it inhibited only the mitogen-activated protein/extracellular signal-regulated kinase kinase/Erk pathway, and it was accompanied by decreased levels of hypoxia inducible factor-1 alpha (HIF-1alpha) and Bcl-2. Stable overexpression of a HIF-1alpha mutant prevented cetuximab-induced autophagy and decrease in Bcl-2 levels. Knockdown of autophagy regulator beclin 1 or cell treatment with autophagy inhibitor 3-methyladenine, a class III PI3K (hVps34) inhibitor, also inhibited cetuximab-induced autophagy. Furthermore, knockdown of beclin 1 or Atg7 or treatment with the lysosome inhibitor chloroquine sensitized cancer cells to cetuximab-induced apoptosis. Mechanistic analysis argued that cetuximab acted by promoting an association between beclin 1 and hVps34, which was inhibited by overexpression of Bcl-2. Our findings suggest that the autophagy protects cancer cells from the proapoptotic effects of cetuximab.</div>
</front>
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<DateCompleted><Year>2010</Year>
<Month>08</Month>
<Day>24</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>12</Month>
<Day>10</Day>
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<Issue>14</Issue>
<PubDate><Year>2010</Year>
<Month>Jul</Month>
<Day>15</Day>
</PubDate>
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<Title>Cancer research</Title>
<ISOAbbreviation>Cancer Res.</ISOAbbreviation>
</Journal>
<ArticleTitle>The epidermal growth factor receptor antibody cetuximab induces autophagy in cancer cells by downregulating HIF-1alpha and Bcl-2 and activating the beclin 1/hVps34 complex.</ArticleTitle>
<Pagination><MedlinePgn>5942-52</MedlinePgn>
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<Abstract><AbstractText>Autophagy is a regulated catabolic process triggered in cells deprived of nutrients or growth factors that govern nutrient uptake. Here, we report that autophagy is induced by cetuximab, a therapeutic antibody that blocks epidermal growth factor receptor function. Cancer cell treatment with cetuximab triggered autophagosome formation, conversion of microtubule-associated protein 1 light chain 3 from its cytoplasmic to membrane-associated form, and increased acidic vesicular organelle formation. Autophagy occurred when cetuximab inhibited the class I phosphoinositide 3-kinase (PI3K)/Akt/mammalian target of rapamycin pathway, but not when it inhibited only the mitogen-activated protein/extracellular signal-regulated kinase kinase/Erk pathway, and it was accompanied by decreased levels of hypoxia inducible factor-1 alpha (HIF-1alpha) and Bcl-2. Stable overexpression of a HIF-1alpha mutant prevented cetuximab-induced autophagy and decrease in Bcl-2 levels. Knockdown of autophagy regulator beclin 1 or cell treatment with autophagy inhibitor 3-methyladenine, a class III PI3K (hVps34) inhibitor, also inhibited cetuximab-induced autophagy. Furthermore, knockdown of beclin 1 or Atg7 or treatment with the lysosome inhibitor chloroquine sensitized cancer cells to cetuximab-induced apoptosis. Mechanistic analysis argued that cetuximab acted by promoting an association between beclin 1 and hVps34, which was inhibited by overexpression of Bcl-2. Our findings suggest that the autophagy protects cancer cells from the proapoptotic effects of cetuximab.</AbstractText>
<CopyrightInformation>(c)2010 AACR.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Xinqun</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Department of Experimental Therapeutics, The University of Texas MD Anderson Cancer Center, Houston, Texas 77030, USA.</Affiliation>
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<ForeName>Zhen</ForeName>
<Initials>Z</Initials>
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<Language>eng</Language>
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