Methylation of death-associated protein kinase is associated with cetuximab and erlotinib resistance
Anti-EGFR therapy is among the most promising molecular targeted therapies against cancer developed in the past decade. However, drug resistance eventually arises in most, if not all, treated patients. Emerging evidence has linked epigenetic changes, such as DNA methylation at CpG islands, to the de...
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creator | Ogawa, Takenori Liggett, Thomas E. Melnikov, Anatoliy A. Monitto, Constance L. Kusuke, Daniela Shiga, Kiyoto Kobayashi, Toshimitsu Horii, Akira Chatterjee, Aditi Levenson, Victor V. Koch, Wayne M. Sidransky, David Chang, Xiaofei |
description | Anti-EGFR therapy is among the most promising molecular targeted therapies against cancer developed in the past decade. However, drug resistance eventually arises in most, if not all, treated patients. Emerging evidence has linked epigenetic changes, such as DNA methylation at CpG islands, to the development of resistance to multiple anticancer drugs. In addition, genes that are differentially methylated have increasingly been appreciated as a source of clinically relevant biomarker candidates. To identify genes that are specifically methylated during the evolution of resistance to anti-EGFR therapeutic agents, we performed a methylation-specific array containing a panel of 56 genes that are commonly known to be regulated through promoter methylation in two parental non-small cell lung cancer (NSCLC) and head and neck squamous cell carcinoma (HNSCC) cell lines and their resistant derivatives to either erlotinib or cetuximab. We found that death-associated protein kinase (DAPK) was hypermethylated in drug-resistant derivatives generated from both parental cell lines. Restoration of DAPK into the resistant NSCLC cells by stable transfection re-sensitized the cells to both erlotinib and cetuximab. Conversely, siRNA-mediated knockdown of DAPK induced resistance in the parental sensitive cells. These results demonstrate that DAPK plays important roles in both cetuximab and erlotinib resistance, and that gene silencing through promoter methylation is one of the key mechanisms of developed resistance to anti-EGFR therapeutic agents. In conclusion, DAPK could be a novel target to overcome resistance to anti-EGFR agents to improve the therapeutic benefit, and further evaluation of DAPK methylation as a potential biomarker of drug response is needed. |
doi_str_mv | 10.4161/cc.20120 |
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However, drug resistance eventually arises in most, if not all, treated patients. Emerging evidence has linked epigenetic changes, such as DNA methylation at CpG islands, to the development of resistance to multiple anticancer drugs. In addition, genes that are differentially methylated have increasingly been appreciated as a source of clinically relevant biomarker candidates. To identify genes that are specifically methylated during the evolution of resistance to anti-EGFR therapeutic agents, we performed a methylation-specific array containing a panel of 56 genes that are commonly known to be regulated through promoter methylation in two parental non-small cell lung cancer (NSCLC) and head and neck squamous cell carcinoma (HNSCC) cell lines and their resistant derivatives to either erlotinib or cetuximab. We found that death-associated protein kinase (DAPK) was hypermethylated in drug-resistant derivatives generated from both parental cell lines. Restoration of DAPK into the resistant NSCLC cells by stable transfection re-sensitized the cells to both erlotinib and cetuximab. Conversely, siRNA-mediated knockdown of DAPK induced resistance in the parental sensitive cells. These results demonstrate that DAPK plays important roles in both cetuximab and erlotinib resistance, and that gene silencing through promoter methylation is one of the key mechanisms of developed resistance to anti-EGFR therapeutic agents. In conclusion, DAPK could be a novel target to overcome resistance to anti-EGFR agents to improve the therapeutic benefit, and further evaluation of DAPK methylation as a potential biomarker of drug response is needed.</description><identifier>ISSN: 1538-4101</identifier><identifier>EISSN: 1551-4005</identifier><identifier>DOI: 10.4161/cc.20120</identifier><identifier>PMID: 22487682</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>Antibodies, Monoclonal - chemistry ; Antibodies, Monoclonal - pharmacology ; Antibodies, Monoclonal, Humanized ; Antineoplastic Agents - chemistry ; Antineoplastic Agents - pharmacology ; Apoptosis Regulatory Proteins - antagonists & inhibitors ; Apoptosis Regulatory Proteins - genetics ; Apoptosis Regulatory Proteins - metabolism ; Binding ; Biology ; Bioscience ; Calcium ; Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors ; Calcium-Calmodulin-Dependent Protein Kinases - genetics ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Cancer ; Carcinoma, Non-Small-Cell Lung - enzymology ; Carcinoma, Non-Small-Cell Lung - pathology ; Carcinoma, Squamous Cell - enzymology ; Carcinoma, Squamous Cell - pathology ; Cell ; Cell Line, Tumor ; Cetuximab ; Cycle ; DAPK ; Death-Associated Protein Kinases ; DNA Methylation - drug effects ; Drug Resistance, Neoplasm ; erlotinib ; Erlotinib Hydrochloride ; Head and Neck Neoplasms - enzymology ; Head and Neck Neoplasms - pathology ; Humans ; Landes ; Lung Neoplasms - enzymology ; Lung Neoplasms - pathology ; methylation ; NSCLC ; Organogenesis ; Promoter Regions, Genetic ; Proteins ; Quinazolines - chemistry ; Quinazolines - pharmacology ; RNA Interference ; RNA, Small Interfering - metabolism</subject><ispartof>Cell cycle (Georgetown, Tex.), 2012-04, Vol.11 (8), p.1656-1663</ispartof><rights>Copyright © 2012 Landes Bioscience 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c497t-c75be57ba26e6fb1dbd843cd165e135be9808db4c8db3870784ec0535c1be2fa3</citedby><cites>FETCH-LOGICAL-c497t-c75be57ba26e6fb1dbd843cd165e135be9808db4c8db3870784ec0535c1be2fa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3341232/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3341232/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22487682$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ogawa, Takenori</creatorcontrib><creatorcontrib>Liggett, Thomas E.</creatorcontrib><creatorcontrib>Melnikov, Anatoliy A.</creatorcontrib><creatorcontrib>Monitto, Constance L.</creatorcontrib><creatorcontrib>Kusuke, Daniela</creatorcontrib><creatorcontrib>Shiga, Kiyoto</creatorcontrib><creatorcontrib>Kobayashi, Toshimitsu</creatorcontrib><creatorcontrib>Horii, Akira</creatorcontrib><creatorcontrib>Chatterjee, Aditi</creatorcontrib><creatorcontrib>Levenson, Victor V.</creatorcontrib><creatorcontrib>Koch, Wayne M.</creatorcontrib><creatorcontrib>Sidransky, David</creatorcontrib><creatorcontrib>Chang, Xiaofei</creatorcontrib><title>Methylation of death-associated protein kinase is associated with cetuximab and erlotinib resistance</title><title>Cell cycle (Georgetown, Tex.)</title><addtitle>Cell Cycle</addtitle><description>Anti-EGFR therapy is among the most promising molecular targeted therapies against cancer developed in the past decade. However, drug resistance eventually arises in most, if not all, treated patients. Emerging evidence has linked epigenetic changes, such as DNA methylation at CpG islands, to the development of resistance to multiple anticancer drugs. In addition, genes that are differentially methylated have increasingly been appreciated as a source of clinically relevant biomarker candidates. To identify genes that are specifically methylated during the evolution of resistance to anti-EGFR therapeutic agents, we performed a methylation-specific array containing a panel of 56 genes that are commonly known to be regulated through promoter methylation in two parental non-small cell lung cancer (NSCLC) and head and neck squamous cell carcinoma (HNSCC) cell lines and their resistant derivatives to either erlotinib or cetuximab. We found that death-associated protein kinase (DAPK) was hypermethylated in drug-resistant derivatives generated from both parental cell lines. Restoration of DAPK into the resistant NSCLC cells by stable transfection re-sensitized the cells to both erlotinib and cetuximab. Conversely, siRNA-mediated knockdown of DAPK induced resistance in the parental sensitive cells. These results demonstrate that DAPK plays important roles in both cetuximab and erlotinib resistance, and that gene silencing through promoter methylation is one of the key mechanisms of developed resistance to anti-EGFR therapeutic agents. In conclusion, DAPK could be a novel target to overcome resistance to anti-EGFR agents to improve the therapeutic benefit, and further evaluation of DAPK methylation as a potential biomarker of drug response is needed.</description><subject>Antibodies, Monoclonal - chemistry</subject><subject>Antibodies, Monoclonal - pharmacology</subject><subject>Antibodies, Monoclonal, Humanized</subject><subject>Antineoplastic Agents - chemistry</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Apoptosis Regulatory Proteins - antagonists & inhibitors</subject><subject>Apoptosis Regulatory Proteins - genetics</subject><subject>Apoptosis Regulatory Proteins - metabolism</subject><subject>Binding</subject><subject>Biology</subject><subject>Bioscience</subject><subject>Calcium</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - genetics</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Cancer</subject><subject>Carcinoma, Non-Small-Cell Lung - enzymology</subject><subject>Carcinoma, Non-Small-Cell Lung - pathology</subject><subject>Carcinoma, Squamous Cell - enzymology</subject><subject>Carcinoma, Squamous Cell - pathology</subject><subject>Cell</subject><subject>Cell Line, Tumor</subject><subject>Cetuximab</subject><subject>Cycle</subject><subject>DAPK</subject><subject>Death-Associated Protein Kinases</subject><subject>DNA Methylation - drug effects</subject><subject>Drug Resistance, Neoplasm</subject><subject>erlotinib</subject><subject>Erlotinib Hydrochloride</subject><subject>Head and Neck Neoplasms - enzymology</subject><subject>Head and Neck Neoplasms - pathology</subject><subject>Humans</subject><subject>Landes</subject><subject>Lung Neoplasms - enzymology</subject><subject>Lung Neoplasms - pathology</subject><subject>methylation</subject><subject>NSCLC</subject><subject>Organogenesis</subject><subject>Promoter Regions, Genetic</subject><subject>Proteins</subject><subject>Quinazolines - chemistry</subject><subject>Quinazolines - pharmacology</subject><subject>RNA Interference</subject><subject>RNA, Small Interfering - metabolism</subject><issn>1538-4101</issn><issn>1551-4005</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE9vEzEQxS0EoqVF4hMgH7ls63-761yQUAQUqVUv9GyN7dnGsLEj2yXNt8dtICri0IvH0ntv5ulHyDvOzhQf-LlzZ4JxwV6QY973vFOM9S8f_lJ3ijN-RN6U8oMxoccFf02OhFB6HLQ4Jv4K62o3Qw0p0jRRj1BXHZSSXICKnm5yqhgi_RkiFKSh0CfiNtQVdVjv7sMaLIXoKeY51RCDpRlLKBWiw1PyaoK54Ns_84TcfPn8fXnRXV5__bb8dNk5tRhr58beYj9aEAMOk-Xeeq2k83zokcumLTTT3irXHqlHNmqFjvWyd9yimECekI_7vZs7u0bvMNYMs9nk1i7vTIJg_lViWJnb9MtIqbiQoi34sF_gciol43TIcmYeSBvnzCPpZn3_9NbB-BdtM5zvDXPDgsWGVFzARuNgvb6FLSyXnBttNn5qCfZMol2HXIOb8dBC7iMhTimvYZvy7E2F3ZzylBv7UIz8r_tvslOxog</recordid><startdate>20120415</startdate><enddate>20120415</enddate><creator>Ogawa, Takenori</creator><creator>Liggett, Thomas E.</creator><creator>Melnikov, Anatoliy A.</creator><creator>Monitto, Constance L.</creator><creator>Kusuke, Daniela</creator><creator>Shiga, Kiyoto</creator><creator>Kobayashi, Toshimitsu</creator><creator>Horii, Akira</creator><creator>Chatterjee, Aditi</creator><creator>Levenson, Victor V.</creator><creator>Koch, Wayne M.</creator><creator>Sidransky, David</creator><creator>Chang, Xiaofei</creator><general>Taylor & Francis</general><general>Landes Bioscience</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>5PM</scope></search><sort><creationdate>20120415</creationdate><title>Methylation of death-associated protein kinase is associated with cetuximab and erlotinib resistance</title><author>Ogawa, Takenori ; Liggett, Thomas E. ; Melnikov, Anatoliy A. ; Monitto, Constance L. ; Kusuke, Daniela ; Shiga, Kiyoto ; Kobayashi, Toshimitsu ; Horii, Akira ; Chatterjee, Aditi ; Levenson, Victor V. ; Koch, Wayne M. ; Sidransky, David ; Chang, Xiaofei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c497t-c75be57ba26e6fb1dbd843cd165e135be9808db4c8db3870784ec0535c1be2fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Antibodies, Monoclonal - chemistry</topic><topic>Antibodies, Monoclonal - pharmacology</topic><topic>Antibodies, Monoclonal, Humanized</topic><topic>Antineoplastic Agents - chemistry</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Apoptosis Regulatory Proteins - antagonists & inhibitors</topic><topic>Apoptosis Regulatory Proteins - genetics</topic><topic>Apoptosis Regulatory Proteins - metabolism</topic><topic>Binding</topic><topic>Biology</topic><topic>Bioscience</topic><topic>Calcium</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - genetics</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>Cancer</topic><topic>Carcinoma, Non-Small-Cell Lung - enzymology</topic><topic>Carcinoma, Non-Small-Cell Lung - pathology</topic><topic>Carcinoma, Squamous Cell - enzymology</topic><topic>Carcinoma, Squamous Cell - pathology</topic><topic>Cell</topic><topic>Cell Line, Tumor</topic><topic>Cetuximab</topic><topic>Cycle</topic><topic>DAPK</topic><topic>Death-Associated Protein Kinases</topic><topic>DNA Methylation - drug effects</topic><topic>Drug Resistance, Neoplasm</topic><topic>erlotinib</topic><topic>Erlotinib Hydrochloride</topic><topic>Head and Neck Neoplasms - enzymology</topic><topic>Head and Neck Neoplasms - pathology</topic><topic>Humans</topic><topic>Landes</topic><topic>Lung Neoplasms - enzymology</topic><topic>Lung Neoplasms - pathology</topic><topic>methylation</topic><topic>NSCLC</topic><topic>Organogenesis</topic><topic>Promoter Regions, Genetic</topic><topic>Proteins</topic><topic>Quinazolines - chemistry</topic><topic>Quinazolines - pharmacology</topic><topic>RNA Interference</topic><topic>RNA, Small Interfering - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ogawa, Takenori</creatorcontrib><creatorcontrib>Liggett, Thomas E.</creatorcontrib><creatorcontrib>Melnikov, Anatoliy A.</creatorcontrib><creatorcontrib>Monitto, Constance L.</creatorcontrib><creatorcontrib>Kusuke, Daniela</creatorcontrib><creatorcontrib>Shiga, Kiyoto</creatorcontrib><creatorcontrib>Kobayashi, Toshimitsu</creatorcontrib><creatorcontrib>Horii, Akira</creatorcontrib><creatorcontrib>Chatterjee, Aditi</creatorcontrib><creatorcontrib>Levenson, Victor V.</creatorcontrib><creatorcontrib>Koch, Wayne M.</creatorcontrib><creatorcontrib>Sidransky, David</creatorcontrib><creatorcontrib>Chang, Xiaofei</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell cycle (Georgetown, Tex.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ogawa, Takenori</au><au>Liggett, Thomas E.</au><au>Melnikov, Anatoliy A.</au><au>Monitto, Constance L.</au><au>Kusuke, Daniela</au><au>Shiga, Kiyoto</au><au>Kobayashi, Toshimitsu</au><au>Horii, Akira</au><au>Chatterjee, Aditi</au><au>Levenson, Victor V.</au><au>Koch, Wayne M.</au><au>Sidransky, David</au><au>Chang, Xiaofei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Methylation of death-associated protein kinase is associated with cetuximab and erlotinib resistance</atitle><jtitle>Cell cycle (Georgetown, Tex.)</jtitle><addtitle>Cell Cycle</addtitle><date>2012-04-15</date><risdate>2012</risdate><volume>11</volume><issue>8</issue><spage>1656</spage><epage>1663</epage><pages>1656-1663</pages><issn>1538-4101</issn><eissn>1551-4005</eissn><abstract>Anti-EGFR therapy is among the most promising molecular targeted therapies against cancer developed in the past decade. However, drug resistance eventually arises in most, if not all, treated patients. Emerging evidence has linked epigenetic changes, such as DNA methylation at CpG islands, to the development of resistance to multiple anticancer drugs. In addition, genes that are differentially methylated have increasingly been appreciated as a source of clinically relevant biomarker candidates. To identify genes that are specifically methylated during the evolution of resistance to anti-EGFR therapeutic agents, we performed a methylation-specific array containing a panel of 56 genes that are commonly known to be regulated through promoter methylation in two parental non-small cell lung cancer (NSCLC) and head and neck squamous cell carcinoma (HNSCC) cell lines and their resistant derivatives to either erlotinib or cetuximab. We found that death-associated protein kinase (DAPK) was hypermethylated in drug-resistant derivatives generated from both parental cell lines. Restoration of DAPK into the resistant NSCLC cells by stable transfection re-sensitized the cells to both erlotinib and cetuximab. Conversely, siRNA-mediated knockdown of DAPK induced resistance in the parental sensitive cells. These results demonstrate that DAPK plays important roles in both cetuximab and erlotinib resistance, and that gene silencing through promoter methylation is one of the key mechanisms of developed resistance to anti-EGFR therapeutic agents. In conclusion, DAPK could be a novel target to overcome resistance to anti-EGFR agents to improve the therapeutic benefit, and further evaluation of DAPK methylation as a potential biomarker of drug response is needed.</abstract><cop>United States</cop><pub>Taylor & Francis</pub><pmid>22487682</pmid><doi>10.4161/cc.20120</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - pharmacology Antibodies, Monoclonal, Humanized Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology Apoptosis Regulatory Proteins - antagonists & inhibitors Apoptosis Regulatory Proteins - genetics Apoptosis Regulatory Proteins - metabolism Binding Biology Bioscience Calcium Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors Calcium-Calmodulin-Dependent Protein Kinases - genetics Calcium-Calmodulin-Dependent Protein Kinases - metabolism Cancer Carcinoma, Non-Small-Cell Lung - enzymology Carcinoma, Non-Small-Cell Lung - pathology Carcinoma, Squamous Cell - enzymology Carcinoma, Squamous Cell - pathology Cell Cell Line, Tumor Cetuximab Cycle DAPK Death-Associated Protein Kinases DNA Methylation - drug effects Drug Resistance, Neoplasm erlotinib Erlotinib Hydrochloride Head and Neck Neoplasms - enzymology Head and Neck Neoplasms - pathology Humans Landes Lung Neoplasms - enzymology Lung Neoplasms - pathology methylation NSCLC Organogenesis Promoter Regions, Genetic Proteins Quinazolines - chemistry Quinazolines - pharmacology RNA Interference RNA, Small Interfering - metabolism |
title | Methylation of death-associated protein kinase is associated with cetuximab and erlotinib resistance |
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