Brigatinib combined with anti-EGFR antibody overcomes osimertinib resistance in EGFR-mutated non-small-cell lung cancer

Osimertinib has been demonstrated to overcome the epidermal growth factor receptor (EGFR)-T790M, the most relevant acquired resistance to first-generation EGFR–tyrosine kinase inhibitors (EGFR–TKIs). However, the C797S mutation, which impairs the covalent binding between the cysteine residue at posi...

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Vydáno v:	Nature communications Ročník 8; číslo 1; s. 14768
Hlavní autoři:	Uchibori, Ken, Inase, Naohiko, Araki, Mitsugu, Kamada, Mayumi, Sato, Shigeo, Okuno, Yasushi, Fujita, Naoya, Katayama, Ryohei
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	London Nature Publishing Group UK 13.03.2017 Nature Publishing Group Nature Portfolio
Témata:	13/31 13/95 38/109 631/67/1059/2326 631/67/1612/1350 64/60 Acrylamides Aniline Compounds Animals Antibodies, Monoclonal - pharmacology Antineoplastic Agents - pharmacology Antineoplastic Combined Chemotherapy Protocols Carcinoma, Non-Small-Cell Lung - drug therapy Carcinoma, Non-Small-Cell Lung - genetics Carcinoma, Non-Small-Cell Lung - mortality Carcinoma, Non-Small-Cell Lung - pathology Cell Line, Tumor Cetuximab - chemistry Cetuximab - pharmacology Drug Resistance, Neoplasm ErbB Receptors - antagonists & inhibitors ErbB Receptors - chemistry ErbB Receptors - genetics ErbB Receptors - metabolism Gene Expression Humanities and Social Sciences Humans Lung cancer Lung Neoplasms - drug therapy Lung Neoplasms - genetics Lung Neoplasms - mortality Lung Neoplasms - pathology Mice Mice, Nude Molecular Dynamics Simulation multidisciplinary Mutation Organophosphorus Compounds - chemistry Organophosphorus Compounds - pharmacology Panitumumab Piperazines - pharmacology Protein Kinase Inhibitors - pharmacology Pyrimidines - chemistry Pyrimidines - pharmacology Science Science (multidisciplinary) Survival Analysis Tumor Burden - drug effects Xenograft Model Antitumor Assays
ISSN:	2041-1723, 2041-1723
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Abstract	Osimertinib has been demonstrated to overcome the epidermal growth factor receptor (EGFR)-T790M, the most relevant acquired resistance to first-generation EGFR–tyrosine kinase inhibitors (EGFR–TKIs). However, the C797S mutation, which impairs the covalent binding between the cysteine residue at position 797 of EGFR and osimertinib, induces resistance to osimertinib. Currently, there are no effective therapeutic strategies to overcome the C797S/T790M/activating-mutation (triple-mutation)-mediated EGFR–TKI resistance. In the present study, we identify brigatinib to be effective against triple-mutation-harbouring cells in vitro and in vivo . Our original computational simulation demonstrates that brigatinib fits into the ATP-binding pocket of triple-mutant EGFR. The structure–activity relationship analysis reveals the key component in brigatinib to inhibit the triple-mutant EGFR. The efficacy of brigatinib is enhanced markedly by combination with anti-EGFR antibody because of the decrease of surface and total EGFR expression. Thus, the combination therapy of brigatinib with anti-EGFR antibody is a powerful candidate to overcome triple-mutant EGFR. Resistance to EGFR-tyrosine kinase inhibitors in non-small-cell lung cancer is mediated by the C797S/T790M/activating mutation. Here, the authors identify brigatinib as a potential drug that in combination with anti-EGFR can overcome resistance in mutated cells.
AbstractList	Osimertinib has been demonstrated to overcome the epidermal growth factor receptor (EGFR)-T790M, the most relevant acquired resistance to first-generation EGFR-tyrosine kinase inhibitors (EGFR-TKIs). However, the C797S mutation, which impairs the covalent binding between the cysteine residue at position 797 of EGFR and osimertinib, induces resistance to osimertinib. Currently, there are no effective therapeutic strategies to overcome the C797S/T790M/activating-mutation (triple-mutation)-mediated EGFR-TKI resistance. In the present study, we identify brigatinib to be effective against triple-mutation-harbouring cells in vitro and in vivo. Our original computational simulation demonstrates that brigatinib fits into the ATP-binding pocket of triple-mutant EGFR. The structure-activity relationship analysis reveals the key component in brigatinib to inhibit the triple-mutant EGFR. The efficacy of brigatinib is enhanced markedly by combination with anti-EGFR antibody because of the decrease of surface and total EGFR expression. Thus, the combination therapy of brigatinib with anti-EGFR antibody is a powerful candidate to overcome triple-mutant EGFR. Osimertinib has been demonstrated to overcome the epidermal growth factor receptor (EGFR)-T790M, the most relevant acquired resistance to first-generation EGFR–tyrosine kinase inhibitors (EGFR–TKIs). However, the C797S mutation, which impairs the covalent binding between the cysteine residue at position 797 of EGFR and osimertinib, induces resistance to osimertinib. Currently, there are no effective therapeutic strategies to overcome the C797S/T790M/activating-mutation (triple-mutation)-mediated EGFR–TKI resistance. In the present study, we identify brigatinib to be effective against triple-mutation-harbouring cells in vitro and in vivo. Our original computational simulation demonstrates that brigatinib fits into the ATP-binding pocket of triple-mutant EGFR. The structure–activity relationship analysis reveals the key component in brigatinib to inhibit the triple-mutant EGFR. The efficacy of brigatinib is enhanced markedly by combination with anti-EGFR antibody because of the decrease of surface and total EGFR expression. Thus, the combination therapy of brigatinib with anti-EGFR antibody is a powerful candidate to overcome triple-mutant EGFR. Resistance to EGFR-tyrosine kinase inhibitors in non-small-cell lung cancer is mediated by the C797S/T790M/activating mutation. Here, the authors identify brigatinib as a potential drug that in combination with anti-EGFR can overcome resistance in mutated cells. Resistance to EGFR-tyrosine kinase inhibitors in non-small-cell lung cancer is mediated by the C797S/T790M/activating mutation. Here, the authors identify brigatinib as a potential drug that in combination with anti-EGFR can overcome resistance in mutated cells. Osimertinib has been demonstrated to overcome the epidermal growth factor receptor (EGFR)-T790M, the most relevant acquired resistance to first-generation EGFR–tyrosine kinase inhibitors (EGFR–TKIs). However, the C797S mutation, which impairs the covalent binding between the cysteine residue at position 797 of EGFR and osimertinib, induces resistance to osimertinib. Currently, there are no effective therapeutic strategies to overcome the C797S/T790M/activating-mutation (triple-mutation)-mediated EGFR–TKI resistance. In the present study, we identify brigatinib to be effective against triple-mutation-harbouring cells in vitro and in vivo . Our original computational simulation demonstrates that brigatinib fits into the ATP-binding pocket of triple-mutant EGFR. The structure–activity relationship analysis reveals the key component in brigatinib to inhibit the triple-mutant EGFR. The efficacy of brigatinib is enhanced markedly by combination with anti-EGFR antibody because of the decrease of surface and total EGFR expression. Thus, the combination therapy of brigatinib with anti-EGFR antibody is a powerful candidate to overcome triple-mutant EGFR. Osimertinib has been demonstrated to overcome the epidermal growth factor receptor (EGFR)-T790M, the most relevant acquired resistance to first-generation EGFR–tyrosine kinase inhibitors (EGFR–TKIs). However, the C797S mutation, which impairs the covalent binding between the cysteine residue at position 797 of EGFR and osimertinib, induces resistance to osimertinib. Currently, there are no effective therapeutic strategies to overcome the C797S/T790M/activating-mutation (triple-mutation)-mediated EGFR–TKI resistance. In the present study, we identify brigatinib to be effective against triple-mutation-harbouring cells in vitro and in vivo . Our original computational simulation demonstrates that brigatinib fits into the ATP-binding pocket of triple-mutant EGFR. The structure–activity relationship analysis reveals the key component in brigatinib to inhibit the triple-mutant EGFR. The efficacy of brigatinib is enhanced markedly by combination with anti-EGFR antibody because of the decrease of surface and total EGFR expression. Thus, the combination therapy of brigatinib with anti-EGFR antibody is a powerful candidate to overcome triple-mutant EGFR. Resistance to EGFR-tyrosine kinase inhibitors in non-small-cell lung cancer is mediated by the C797S/T790M/activating mutation. Here, the authors identify brigatinib as a potential drug that in combination with anti-EGFR can overcome resistance in mutated cells.
ArticleNumber	14768
Author	Sato, Shigeo Fujita, Naoya Araki, Mitsugu Okuno, Yasushi Katayama, Ryohei Uchibori, Ken Inase, Naohiko Kamada, Mayumi
Author_xml	– sequence: 1 givenname: Ken surname: Uchibori fullname: Uchibori, Ken organization: Cancer Chemotherapy Center, Japanese Foundation for Cancer Research, Department of Respiratory Medicine, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University – sequence: 2 givenname: Naohiko surname: Inase fullname: Inase, Naohiko organization: Department of Respiratory Medicine, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University – sequence: 3 givenname: Mitsugu surname: Araki fullname: Araki, Mitsugu organization: RIKEN Advanced Institute for Computational Science – sequence: 4 givenname: Mayumi surname: Kamada fullname: Kamada, Mayumi organization: Graduate School of Medicine, Kyoto University – sequence: 5 givenname: Shigeo surname: Sato fullname: Sato, Shigeo organization: Cancer Chemotherapy Center, Japanese Foundation for Cancer Research – sequence: 6 givenname: Yasushi surname: Okuno fullname: Okuno, Yasushi organization: RIKEN Advanced Institute for Computational Science, Graduate School of Medicine, Kyoto University – sequence: 7 givenname: Naoya surname: Fujita fullname: Fujita, Naoya organization: Cancer Chemotherapy Center, Japanese Foundation for Cancer Research – sequence: 8 givenname: Ryohei orcidid: 0000-0001-7394-895X surname: Katayama fullname: Katayama, Ryohei email: ryohei.katayama@jfcr.or.jp organization: Cancer Chemotherapy Center, Japanese Foundation for Cancer Research
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/28287083$$D View this record in MEDLINE/PubMed
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Snippet	Osimertinib has been demonstrated to overcome the epidermal growth factor receptor (EGFR)-T790M, the most relevant acquired resistance to first-generation... Resistance to EGFR-tyrosine kinase inhibitors in non-small-cell lung cancer is mediated by the C797S/T790M/activating mutation. Here, the authors identify...
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Title	Brigatinib combined with anti-EGFR antibody overcomes osimertinib resistance in EGFR-mutated non-small-cell lung cancer
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