Integrin αV Inhibition by GMI, a Ganoderma Microsporum Immunomodulatory Protein, Abolish Stemness and Migration in EGFR‐Mutated Lung Cancer Cells Resistant to Osimertinib

ABSTRACT Integrins, the receptors of the extracellular matrix, are critical in the proliferation and metastasis of cancer cells. GMI, a Ganoderma microsporum immunomodulatory protein, possesses anticancer and antivirus abilities. The object of this study is to investigate the role of GMI in the inte...

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Published inEnvironmental toxicology Vol. 39; no. 12; pp. 5238 - 5249
Main Authors Kang, Yu‐Ting, Chang, Hui‐Yi, Hsieh, Ya‐Chu, Chou, Chia‐Hsuan, Hsin, I‐Lun, Ko, Jiunn‐Liang
Format Journal Article
LanguageEnglish
Published Hoboken, USA John Wiley & Sons, Inc 01.12.2024
Wiley Subscription Services, Inc
Subjects
cancer stem cells
Cell migration
Cell proliferation
Cell viability
Chromatography
ecotoxicology
Epidermal growth factor receptors
Extracellular matrix
family
Ganoderma
GMI
Immunomodulation
Immunomodulators
integrin
Integrins
Liquid chromatography
Lung cancer
lung neoplasms
Lungs
Mass spectrometry
Mass spectroscopy
Metastases
metastasis
Microsporum
migration
mutation
Neoplasms
osimertinib‐resistance
Proteins
Signal transduction
Stem cells
Targeted cancer therapy
Tumors
Western blotting
Xenotransplantation
lung cancer
migration
GMI
osimertinib‐resistance
cancer stem cells
integrin
Online AccessGet full text
ISSN1520-4081
1522-7278
1522-7278
DOI10.1002/tox.24399

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Abstract ABSTRACT Integrins, the receptors of the extracellular matrix, are critical in the proliferation and metastasis of cancer cells. GMI, a Ganoderma microsporum immunomodulatory protein, possesses anticancer and antivirus abilities. The object of this study is to investigate the role of GMI in the integrins signaling pathway in lung cancer cells that harbor the EGFR L858R/T790M double mutation and osimertinib‐resistance. Liquid chromatography‐mass spectrometry and western blot assay were used to investigate the effect of GMI on inhibiting the protein expressions of integrins in H1975 cells. The migration ability and xenograft tumor growth of H1975 were suppressed by GMI. To elucidate the role of the integrin family in lung cancer resistant to osimertinib (AZD‐9291, Tagrisso), H1975 cells were used to establish the osimertinib‐resistant cells, named H1975/TR cells. The expressions of Integrin αV and stemness markers were much higher in H1975/TR cells than in H1975 cells. GMI suppressed cell viability, tumor spheroid growth, and the expressions of integrin αV and β1 in H1975/TR cells. Furthermore, GMI suppressed the expressions of stemness markers and formation of tumor spheres via blocking integrin αV signaling cascade. This is the first study to reveal the novel function of GMI in constraining cancer stem cells and migration by abolishing the integrin αV‐related signaling pathway in EGFR‐mutated and osimertinib‐resistant lung cancer cells.
AbstractList Integrins, the receptors of the extracellular matrix, are critical in the proliferation and metastasis of cancer cells. GMI, a Ganoderma microsporum immunomodulatory protein, possesses anticancer and antivirus abilities. The object of this study is to investigate the role of GMI in the integrins signaling pathway in lung cancer cells that harbor the EGFR L858R/T790M double mutation and osimertinib‐resistance. Liquid chromatography‐mass spectrometry and western blot assay were used to investigate the effect of GMI on inhibiting the protein expressions of integrins in H1975 cells. The migration ability and xenograft tumor growth of H1975 were suppressed by GMI. To elucidate the role of the integrin family in lung cancer resistant to osimertinib (AZD‐9291, Tagrisso), H1975 cells were used to establish the osimertinib‐resistant cells, named H1975/TR cells. The expressions of Integrin αV and stemness markers were much higher in H1975/TR cells than in H1975 cells. GMI suppressed cell viability, tumor spheroid growth, and the expressions of integrin αV and β1 in H1975/TR cells. Furthermore, GMI suppressed the expressions of stemness markers and formation of tumor spheres via blocking integrin αV signaling cascade. This is the first study to reveal the novel function of GMI in constraining cancer stem cells and migration by abolishing the integrin αV‐related signaling pathway in EGFR‐mutated and osimertinib‐resistant lung cancer cells.
Integrins, the receptors of the extracellular matrix, are critical in the proliferation and metastasis of cancer cells. GMI, a Ganoderma microsporum immunomodulatory protein, possesses anticancer and antivirus abilities. The object of this study is to investigate the role of GMI in the integrins signaling pathway in lung cancer cells that harbor the EGFR L858R/T790M double mutation and osimertinib-resistance. Liquid chromatography-mass spectrometry and western blot assay were used to investigate the effect of GMI on inhibiting the protein expressions of integrins in H1975 cells. The migration ability and xenograft tumor growth of H1975 were suppressed by GMI. To elucidate the role of the integrin family in lung cancer resistant to osimertinib (AZD-9291, Tagrisso), H1975 cells were used to establish the osimertinib-resistant cells, named H1975/TR cells. The expressions of Integrin αV and stemness markers were much higher in H1975/TR cells than in H1975 cells. GMI suppressed cell viability, tumor spheroid growth, and the expressions of integrin αV and β1 in H1975/TR cells. Furthermore, GMI suppressed the expressions of stemness markers and formation of tumor spheres via blocking integrin αV signaling cascade. This is the first study to reveal the novel function of GMI in constraining cancer stem cells and migration by abolishing the integrin αV-related signaling pathway in EGFR-mutated and osimertinib-resistant lung cancer cells.Integrins, the receptors of the extracellular matrix, are critical in the proliferation and metastasis of cancer cells. GMI, a Ganoderma microsporum immunomodulatory protein, possesses anticancer and antivirus abilities. The object of this study is to investigate the role of GMI in the integrins signaling pathway in lung cancer cells that harbor the EGFR L858R/T790M double mutation and osimertinib-resistance. Liquid chromatography-mass spectrometry and western blot assay were used to investigate the effect of GMI on inhibiting the protein expressions of integrins in H1975 cells. The migration ability and xenograft tumor growth of H1975 were suppressed by GMI. To elucidate the role of the integrin family in lung cancer resistant to osimertinib (AZD-9291, Tagrisso), H1975 cells were used to establish the osimertinib-resistant cells, named H1975/TR cells. The expressions of Integrin αV and stemness markers were much higher in H1975/TR cells than in H1975 cells. GMI suppressed cell viability, tumor spheroid growth, and the expressions of integrin αV and β1 in H1975/TR cells. Furthermore, GMI suppressed the expressions of stemness markers and formation of tumor spheres via blocking integrin αV signaling cascade. This is the first study to reveal the novel function of GMI in constraining cancer stem cells and migration by abolishing the integrin αV-related signaling pathway in EGFR-mutated and osimertinib-resistant lung cancer cells.
ABSTRACT Integrins, the receptors of the extracellular matrix, are critical in the proliferation and metastasis of cancer cells. GMI, a Ganoderma microsporum immunomodulatory protein, possesses anticancer and antivirus abilities. The object of this study is to investigate the role of GMI in the integrins signaling pathway in lung cancer cells that harbor the EGFR L858R/T790M double mutation and osimertinib‐resistance. Liquid chromatography‐mass spectrometry and western blot assay were used to investigate the effect of GMI on inhibiting the protein expressions of integrins in H1975 cells. The migration ability and xenograft tumor growth of H1975 were suppressed by GMI. To elucidate the role of the integrin family in lung cancer resistant to osimertinib (AZD‐9291, Tagrisso), H1975 cells were used to establish the osimertinib‐resistant cells, named H1975/TR cells. The expressions of Integrin αV and stemness markers were much higher in H1975/TR cells than in H1975 cells. GMI suppressed cell viability, tumor spheroid growth, and the expressions of integrin αV and β1 in H1975/TR cells. Furthermore, GMI suppressed the expressions of stemness markers and formation of tumor spheres via blocking integrin αV signaling cascade. This is the first study to reveal the novel function of GMI in constraining cancer stem cells and migration by abolishing the integrin αV‐related signaling pathway in EGFR‐mutated and osimertinib‐resistant lung cancer cells.
Author Kang, Yu‐Ting
Chang, Hui‐Yi
Hsin, I‐Lun
Chou, Chia‐Hsuan
Ko, Jiunn‐Liang
Hsieh, Ya‐Chu
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Keywords lung cancer
migration
GMI
osimertinib‐resistance
cancer stem cells
integrin
Language English
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Notes The two correspondence authors are contributed equally to this work.
Funding
This work was supported by the Taiwan National Science and Technology Council (grant number: MOST 111‐2320‐B‐040‐018‐MY3).
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Snippet ABSTRACT Integrins, the receptors of the extracellular matrix, are critical in the proliferation and metastasis of cancer cells. GMI, a Ganoderma microsporum...
Integrins, the receptors of the extracellular matrix, are critical in the proliferation and metastasis of cancer cells. GMI, a Ganoderma microsporum...
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SubjectTerms cancer stem cells
Cell migration
Cell proliferation
Cell viability
Chromatography
ecotoxicology
Epidermal growth factor receptors
Extracellular matrix
family
Ganoderma
GMI
Immunomodulation
Immunomodulators
integrin
Integrins
Liquid chromatography
Lung cancer
lung neoplasms
Lungs
Mass spectrometry
Mass spectroscopy
Metastases
metastasis
Microsporum
migration
mutation
Neoplasms
osimertinib‐resistance
Proteins
Signal transduction
Stem cells
Targeted cancer therapy
Tumors
Western blotting
Xenotransplantation
Title Integrin αV Inhibition by GMI, a Ganoderma Microsporum Immunomodulatory Protein, Abolish Stemness and Migration in EGFR‐Mutated Lung Cancer Cells Resistant to Osimertinib
URI https://onlinelibrary.wiley.com/doi/abs/10.1002%2Ftox.24399
https://www.ncbi.nlm.nih.gov/pubmed/39152744
https://www.proquest.com/docview/3128524685
https://www.proquest.com/docview/3094044968
https://www.proquest.com/docview/3154167199
Volume 39
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