Analysis of genomic and non-genomic signaling of estrogen receptor in PDX models of breast cancer treated with a combination of the PI3K inhibitor alpelisib (BYL719) and fulvestrant.


Journal

Breast cancer research : BCR
ISSN: 1465-542X
Titre abrégé: Breast Cancer Res
Pays: England
ID NLM: 100927353

Informations de publication

Date de publication:
21 05 2021
Historique:
received: 05 10 2020
accepted: 26 04 2021
entrez: 22 5 2021
pubmed: 23 5 2021
medline: 1 1 2022
Statut: epublish

Résumé

Endocrine therapies targeting estrogen signaling have significantly improved breast cancer (BC) patient survival, although 40% of ERα-positive BCs do not respond to those therapies. Aside from genomic signaling, estrogen triggers non-genomic pathways by forming a complex containing methylERα/Src/PI3K, a hallmark of aggressiveness and resistance to tamoxifen. We aimed to confirm the prognostic value of this complex and investigated whether its targeting could improve tumor response in vivo. The interaction of ERα/Src and ERα/PI3K was studied by proximity ligation assay (PLA) in a cohort of 440 BC patients. We then treated patient-derived BC xenografts (PDXs) with fulvestrant or the PI3K inhibitor alpelisib (BYL719) alone or in combination. We analyzed their anti-proliferative effects on 6 ERα+ and 3 ERα- PDX models. Genomic and non-genomic estrogen signaling were assessed by measuring ERα/PI3K interaction by PLA and the expression of estrogen target genes by RT-QPCR, respectively. We confirmed that ERα/Src and ERα/PI3K interactions were associated with a trend to poorer survival, the latter displaying the most significant effects. In ERα+ tumors, the combination of BYL719 and fulvestrant was more effective than fulvestrant alone in 3 models, irrespective of PI3K, PTEN status, or ERα/PI3K targeting. Remarkably, resistance to fulvestrant was associated with non-genomic ERα signaling, since genomic degradation of ERα was unaltered in these tumors, whereas the treatment did not diminish the level of ERα/PI3K interaction. Interestingly, in 2 ERα- models, fulvestrant alone impacted tumor growth, and this was associated with a decrease in ERα/PI3K interaction. Our results demonstrate that ERα/PI3K may constitute a new prognostic marker, as well as a new target in BC. Indeed, resistance to fulvestrant in ERα+ tumors was associated with a lack of impairment of ERα/PI3K interaction in the cytoplasm. In addition, an efficient targeting of ERα/PI3K in ERα- tumors could constitute a promising therapeutic option.

Sections du résumé

BACKGROUND
Endocrine therapies targeting estrogen signaling have significantly improved breast cancer (BC) patient survival, although 40% of ERα-positive BCs do not respond to those therapies. Aside from genomic signaling, estrogen triggers non-genomic pathways by forming a complex containing methylERα/Src/PI3K, a hallmark of aggressiveness and resistance to tamoxifen. We aimed to confirm the prognostic value of this complex and investigated whether its targeting could improve tumor response in vivo.
METHODS
The interaction of ERα/Src and ERα/PI3K was studied by proximity ligation assay (PLA) in a cohort of 440 BC patients. We then treated patient-derived BC xenografts (PDXs) with fulvestrant or the PI3K inhibitor alpelisib (BYL719) alone or in combination. We analyzed their anti-proliferative effects on 6 ERα+ and 3 ERα- PDX models. Genomic and non-genomic estrogen signaling were assessed by measuring ERα/PI3K interaction by PLA and the expression of estrogen target genes by RT-QPCR, respectively.
RESULTS
We confirmed that ERα/Src and ERα/PI3K interactions were associated with a trend to poorer survival, the latter displaying the most significant effects. In ERα+ tumors, the combination of BYL719 and fulvestrant was more effective than fulvestrant alone in 3 models, irrespective of PI3K, PTEN status, or ERα/PI3K targeting. Remarkably, resistance to fulvestrant was associated with non-genomic ERα signaling, since genomic degradation of ERα was unaltered in these tumors, whereas the treatment did not diminish the level of ERα/PI3K interaction. Interestingly, in 2 ERα- models, fulvestrant alone impacted tumor growth, and this was associated with a decrease in ERα/PI3K interaction.
CONCLUSIONS
Our results demonstrate that ERα/PI3K may constitute a new prognostic marker, as well as a new target in BC. Indeed, resistance to fulvestrant in ERα+ tumors was associated with a lack of impairment of ERα/PI3K interaction in the cytoplasm. In addition, an efficient targeting of ERα/PI3K in ERα- tumors could constitute a promising therapeutic option.

Identifiants

pubmed: 34020697
doi: 10.1186/s13058-021-01433-8
pii: 10.1186/s13058-021-01433-8
pmc: PMC8139055
doi:

Substances chimiques

Biomarkers, Tumor 0
Phosphoinositide-3 Kinase Inhibitors 0
Receptors, Estrogen 0
Thiazoles 0
Alpelisib 08W5N2C97Q
Fulvestrant 22X328QOC4
Proto-Oncogene Proteins pp60(c-src) 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

57

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Auteurs

Julien Jacquemetton (J)

Université de Lyon, F-69000, Lyon, France.
Inserm U1052, Centre de Recherche en Cancérologie de Lyon, F-69000, Lyon, France.
CNRS UMR5286, Centre de Recherche en Cancérologie de Lyon, F-69000, Lyon, France.

Loay Kassem (L)

Clinical Oncology Department, Faculty of Medicine, Cairo University, Cairo, Egypt.

Coralie Poulard (C)

Université de Lyon, F-69000, Lyon, France.
Inserm U1052, Centre de Recherche en Cancérologie de Lyon, F-69000, Lyon, France.
CNRS UMR5286, Centre de Recherche en Cancérologie de Lyon, F-69000, Lyon, France.

Ahmed Dahmani (A)

Translational Research Department, Institut Curie, PSL University, 75005, Paris, France.

Ludmilla De Plater (L)

Translational Research Department, Institut Curie, PSL University, 75005, Paris, France.

Elodie Montaudon (E)

Translational Research Department, Institut Curie, PSL University, 75005, Paris, France.

Laura Sourd (L)

Translational Research Department, Institut Curie, PSL University, 75005, Paris, France.

Ludivine Morisset (L)

Translational Research Department, Institut Curie, PSL University, 75005, Paris, France.

Rania El Botty (R)

Translational Research Department, Institut Curie, PSL University, 75005, Paris, France.

Sophie Chateau-Joubert (S)

École Nationale Vétérinaire d'Alfort, BioPôle Alfort, 94704, Maisons-Alfort Cedex, France.

Sophie Vacher (S)

Genetics Department, Institut Curie, Paris, France.

Ivan Bièche (I)

Genetics Department, Institut Curie, Paris, France.

Isabelle Treilleux (I)

Université de Lyon, F-69000, Lyon, France.
Inserm U1052, Centre de Recherche en Cancérologie de Lyon, F-69000, Lyon, France.
CNRS UMR5286, Centre de Recherche en Cancérologie de Lyon, F-69000, Lyon, France.
Pathology Department, Centre Léon Bérard, F-69000, Lyon, France.

Olivier Trédan (O)

Université de Lyon, F-69000, Lyon, France.
Inserm U1052, Centre de Recherche en Cancérologie de Lyon, F-69000, Lyon, France.
CNRS UMR5286, Centre de Recherche en Cancérologie de Lyon, F-69000, Lyon, France.
Medical Oncology Department, Centre Léon Bérard, F-69000, Lyon, France.

Elisabetta Marangoni (E)

Translational Research Department, Institut Curie, PSL University, 75005, Paris, France.

Muriel Le Romancer (M)

Université de Lyon, F-69000, Lyon, France. muriel.leromancer@lyon.unicancer.fr.
Inserm U1052, Centre de Recherche en Cancérologie de Lyon, F-69000, Lyon, France. muriel.leromancer@lyon.unicancer.fr.
CNRS UMR5286, Centre de Recherche en Cancérologie de Lyon, F-69000, Lyon, France. muriel.leromancer@lyon.unicancer.fr.
Centre de Recherche en Cancérologie de Lyon, INSERM 1052, CNRS 5286, Centre Léon Bérard, Bâtiment D, 28 rue Laennec, 69373, Lyon Cedex 08, France. muriel.leromancer@lyon.unicancer.fr.

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