Met inhibition revokes IFNγ-induction of PD-1 ligands in MET-amplified tumours.


Journal

British journal of cancer
ISSN: 1532-1827
Titre abrégé: Br J Cancer
Pays: England
ID NLM: 0370635

Informations de publication

Date de publication:
03 2019
Historique:
received: 10 08 2018
accepted: 03 10 2018
revised: 01 10 2018
pubmed: 7 2 2019
medline: 18 12 2019
entrez: 7 2 2019
Statut: ppublish

Résumé

Interferon-induced expression of programmed cell death ligands (PD-L1/PD-L2) may sustain tumour immune-evasion. Patients featuring MET amplification, a genetic lesion driving transformation, may benefit from anti-MET treatment. We explored if MET-targeted therapy interferes with Interferon-γ modulation of PD-L1/PD-L2 in MET-amplified tumours. PD-L1/PD-L2 expression and signalling pathways downstream of MET or Interferon-γ were analysed in MET-amplified tumour cell lines and in patient-derived tumour organoids, in basal condition, upon Interferon-γ stimulation, and after anti-MET therapy. PD-L1 and PD-L2 were upregulated in MET-amplified tumour cells upon Interferon-γ treatment. This induction was impaired by JNJ-605, a selective inhibitor of MET kinase activity, and MvDN30, an antibody inducing MET proteolytic cleavage. We found that activation of JAKs/ STAT1, signal transducers downstream of the Interferon-γ receptor, was neutralised by MET inhibitors. Moreover, JAK2 and MET associated in the same signalling complex depending on MET phosphorylation. Results were confirmed in MET-amplified organoids derived from human colorectal tumours, where JNJ-605 treatment revoked Interferon-γ induced PD-L1 expression. These data show that in MET-amplified cancers, treatment with MET inhibitors counteracts the induction of PD-1 ligands by Interferon-γ. Thus, therapeutic use of anti-MET drugs may provide additional clinical benefit over and above the intended inhibition of the target oncogene.

Sections du résumé

BACKGROUND
Interferon-induced expression of programmed cell death ligands (PD-L1/PD-L2) may sustain tumour immune-evasion. Patients featuring MET amplification, a genetic lesion driving transformation, may benefit from anti-MET treatment. We explored if MET-targeted therapy interferes with Interferon-γ modulation of PD-L1/PD-L2 in MET-amplified tumours.
METHODS
PD-L1/PD-L2 expression and signalling pathways downstream of MET or Interferon-γ were analysed in MET-amplified tumour cell lines and in patient-derived tumour organoids, in basal condition, upon Interferon-γ stimulation, and after anti-MET therapy.
RESULTS
PD-L1 and PD-L2 were upregulated in MET-amplified tumour cells upon Interferon-γ treatment. This induction was impaired by JNJ-605, a selective inhibitor of MET kinase activity, and MvDN30, an antibody inducing MET proteolytic cleavage. We found that activation of JAKs/ STAT1, signal transducers downstream of the Interferon-γ receptor, was neutralised by MET inhibitors. Moreover, JAK2 and MET associated in the same signalling complex depending on MET phosphorylation. Results were confirmed in MET-amplified organoids derived from human colorectal tumours, where JNJ-605 treatment revoked Interferon-γ induced PD-L1 expression.
CONCLUSIONS
These data show that in MET-amplified cancers, treatment with MET inhibitors counteracts the induction of PD-1 ligands by Interferon-γ. Thus, therapeutic use of anti-MET drugs may provide additional clinical benefit over and above the intended inhibition of the target oncogene.

Identifiants

pubmed: 30723303
doi: 10.1038/s41416-018-0315-3
pii: 10.1038/s41416-018-0315-3
pmc: PMC6461865
doi:

Substances chimiques

B7-H1 Antigen 0
CD274 protein, human 0
PDCD1LG2 protein, human 0
Programmed Cell Death 1 Ligand 2 Protein 0
Protein Kinase Inhibitors 0
Receptors, Interferon 0
STAT1 Transcription Factor 0
Interferon-gamma 82115-62-6
MET protein, human EC 2.7.10.1
Proto-Oncogene Proteins c-met EC 2.7.10.1
Janus Kinases EC 2.7.10.2

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

527-536

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Auteurs

Valentina Martin (V)

Medical Oncology Division, Experimental Cell Therapy, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy.

Cristina Chiriaco (C)

Laboratory of Gene Transfer, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy.

Chiara Modica (C)

Department of Oncology, University of Torino, Candiolo, Torino, Italy.
Laboratory of Molecular Therapeutics and Exploratory Research, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy.

Anna Acquadro (A)

Medical Oncology Division, Experimental Cell Therapy, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy.
Department of Oncology, University of Torino, Candiolo, Torino, Italy.

Marco Cortese (M)

Laboratory of Gene Transfer, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy.
Department of Oncology, University of Torino, Candiolo, Torino, Italy.

Francesco Galimi (F)

Laboratory of Translational Cancer Medicine, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy.

Timothy Perera (T)

OCTIMET Oncology NV, Turnhoutseweg 30, Beerse, Belgium.

Loretta Gammaitoni (L)

Medical Oncology Division, Experimental Cell Therapy, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy.

Massimo Aglietta (M)

Medical Oncology Division, Experimental Cell Therapy, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy.
Department of Oncology, University of Torino, Candiolo, Torino, Italy.

Paolo M Comoglio (PM)

Laboratory of Molecular Therapeutics and Exploratory Research, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy.

Elisa Vigna (E)

Laboratory of Gene Transfer, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy. elisa.vigna@ircc.it.
Department of Oncology, University of Torino, Candiolo, Torino, Italy. elisa.vigna@ircc.it.

Dario Sangiolo (D)

Medical Oncology Division, Experimental Cell Therapy, Candiolo Cancer Institute, FPO-IRCCS, Candiolo, Torino, Italy.
Department of Oncology, University of Torino, Candiolo, Torino, Italy.

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