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2. A mutual information-based in vivo monitoring of adaptive response to targeted therapies in melanoma

Author

Bugi-Marteyn, Aurore, Noulet, Fanny, Liaudet, Nicolas, and Merat, Rastine

Subjects
Quantitative Biology - Tissues and Organs
Abstract

The mechanisms of adaptive resistance to genetic-based targeted therapies of solid malignancies have been the subject of intense research. These studies hold great promise for finding co-targetable hub/pathways which in turn would control the downstream non-genetic mechanisms of adaptive resistance. Many such mechanisms have been described in the paradigmatic BRAF-mutated melanoma model of adaptive response to BRAF inhibition. Currently, a major challenge for these mechanistic studies is to confirm in vivo, at the single-cell proteomic level, the existence of dependencies between the co-targeted hub/pathways and their downstream effectors. Moreover, the drug-induced in vivo modulation of these dependencies needs to be demonstrated. Here, we implement such single-cell-based in vivo expression dependency quantification using immunohistochemistry (IHC)-based analyses of sequential biopsies in two xenograft models. These mimic phase 2 and 3 trials in our own therapeutic strategy to prevent the adaptive response to BRAF inhibition. In this mechanistic model, the dependencies between the targeted Li2CO3-inducible hub HuR and the resistance effectors are more likely time-shifted and transient since the minority of HuRLow cells, which act as a reservoir of adaptive plasticity, switch to a HuRHigh state as they paradoxically proliferate under BRAF inhibition. Nevertheless, we show that a copula/kernel density estimator (KDE)-based quantification of mutual information (MI) efficiently captures, at the individual level, the dependencies between HuR and two relevant resistance markers pERK and EGFR, and outperforms classic expression correlation coefficients. Ultimately, the validation of MI as a predictive IHC-based metric of response to our therapeutic strategy will be carried in clinical trials., Comment: 9 pages, 5 figures Corrected typos

Published
2021
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5. Data from Integrin α5β1 Plays a Critical Role in Resistance to Temozolomide by Interfering with the p53 Pathway in High-Grade Glioma

Author

Janouskova, Hana, primary, Maglott, Anne, primary, Leger, David Y., primary, Bossert, Catherine, primary, Noulet, Fanny, primary, Guerin, Eric, primary, Guenot, Dominique, primary, Pinel, Sophie, primary, Chastagner, Pascal, primary, Plenat, François, primary, Entz-Werle, Natacha, primary, Lehmann-Che, Jacqueline, primary, Godet, Julien, primary, Martin, Sophie, primary, Teisinger, Jan, primary, and Dontenwill, Monique, primary

Published
2023
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6. Supplementary Figure 2 from Integrin α5β1 Plays a Critical Role in Resistance to Temozolomide by Interfering with the p53 Pathway in High-Grade Glioma

Author

Janouskova, Hana, primary, Maglott, Anne, primary, Leger, David Y., primary, Bossert, Catherine, primary, Noulet, Fanny, primary, Guerin, Eric, primary, Guenot, Dominique, primary, Pinel, Sophie, primary, Chastagner, Pascal, primary, Plenat, François, primary, Entz-Werle, Natacha, primary, Lehmann-Che, Jacqueline, primary, Godet, Julien, primary, Martin, Sophie, primary, Teisinger, Jan, primary, and Dontenwill, Monique, primary

Published
2023
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7. Supplementary Table 2 from Integrin α5β1 Plays a Critical Role in Resistance to Temozolomide by Interfering with the p53 Pathway in High-Grade Glioma

Author

Janouskova, Hana, primary, Maglott, Anne, primary, Leger, David Y., primary, Bossert, Catherine, primary, Noulet, Fanny, primary, Guerin, Eric, primary, Guenot, Dominique, primary, Pinel, Sophie, primary, Chastagner, Pascal, primary, Plenat, François, primary, Entz-Werle, Natacha, primary, Lehmann-Che, Jacqueline, primary, Godet, Julien, primary, Martin, Sophie, primary, Teisinger, Jan, primary, and Dontenwill, Monique, primary

Published
2023
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8. Supplementary Table 3 from Integrin α5β1 Plays a Critical Role in Resistance to Temozolomide by Interfering with the p53 Pathway in High-Grade Glioma

Author

Janouskova, Hana, primary, Maglott, Anne, primary, Leger, David Y., primary, Bossert, Catherine, primary, Noulet, Fanny, primary, Guerin, Eric, primary, Guenot, Dominique, primary, Pinel, Sophie, primary, Chastagner, Pascal, primary, Plenat, François, primary, Entz-Werle, Natacha, primary, Lehmann-Che, Jacqueline, primary, Godet, Julien, primary, Martin, Sophie, primary, Teisinger, Jan, primary, and Dontenwill, Monique, primary

Published
2023
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9. Supplementary Table 1 from Integrin α5β1 Plays a Critical Role in Resistance to Temozolomide by Interfering with the p53 Pathway in High-Grade Glioma

Author

Janouskova, Hana, primary, Maglott, Anne, primary, Leger, David Y., primary, Bossert, Catherine, primary, Noulet, Fanny, primary, Guerin, Eric, primary, Guenot, Dominique, primary, Pinel, Sophie, primary, Chastagner, Pascal, primary, Plenat, François, primary, Entz-Werle, Natacha, primary, Lehmann-Che, Jacqueline, primary, Godet, Julien, primary, Martin, Sophie, primary, Teisinger, Jan, primary, and Dontenwill, Monique, primary

Published
2023
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10. Supplementary Figure 1 from Integrin α5β1 Plays a Critical Role in Resistance to Temozolomide by Interfering with the p53 Pathway in High-Grade Glioma

Author

Janouskova, Hana, primary, Maglott, Anne, primary, Leger, David Y., primary, Bossert, Catherine, primary, Noulet, Fanny, primary, Guerin, Eric, primary, Guenot, Dominique, primary, Pinel, Sophie, primary, Chastagner, Pascal, primary, Plenat, François, primary, Entz-Werle, Natacha, primary, Lehmann-Che, Jacqueline, primary, Godet, Julien, primary, Martin, Sophie, primary, Teisinger, Jan, primary, and Dontenwill, Monique, primary

Published
2023
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11. Supplementary Figure 3 from Integrin α5β1 Plays a Critical Role in Resistance to Temozolomide by Interfering with the p53 Pathway in High-Grade Glioma

Author

Janouskova, Hana, primary, Maglott, Anne, primary, Leger, David Y., primary, Bossert, Catherine, primary, Noulet, Fanny, primary, Guerin, Eric, primary, Guenot, Dominique, primary, Pinel, Sophie, primary, Chastagner, Pascal, primary, Plenat, François, primary, Entz-Werle, Natacha, primary, Lehmann-Che, Jacqueline, primary, Godet, Julien, primary, Martin, Sophie, primary, Teisinger, Jan, primary, and Dontenwill, Monique, primary

Published
2023
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12. Supplementary Figure Legends 1-3 from Integrin α5β1 Plays a Critical Role in Resistance to Temozolomide by Interfering with the p53 Pathway in High-Grade Glioma

Author

Janouskova, Hana, primary, Maglott, Anne, primary, Leger, David Y., primary, Bossert, Catherine, primary, Noulet, Fanny, primary, Guerin, Eric, primary, Guenot, Dominique, primary, Pinel, Sophie, primary, Chastagner, Pascal, primary, Plenat, François, primary, Entz-Werle, Natacha, primary, Lehmann-Che, Jacqueline, primary, Godet, Julien, primary, Martin, Sophie, primary, Teisinger, Jan, primary, and Dontenwill, Monique, primary

Published
2023
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22. Is nutlin-3A a new therapeutic option for a subset of high grade glioma expressing a wild type P53 and high α5β1 integrin?

Author

Janouskova, Hana, Maglott, Anne, Leger, David Y, Bossert, Catherine, Noulet, Fanny, Guérin, Eric, Guenot, Dominique, Pinel, Sophie, Chastagner, Pascal, Plénat, François, Entz-Werlé, Natacha, Godet, Julien, Martin, Sophie, Dotenwill, Monique, Maquin, Didier, Laboratoire de Biophotonique et Pharmacologie - UMR 7213 (LBP), Centre National de la Recherche Scientifique (CNRS)-Réseau nanophotonique et optique, Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA)), Développement et physiopathologie de l'intestin et du pancréas, Institut National de la Santé et de la Recherche Médicale (INSERM), Signalisation, Génomique et Recherche Translationnelle en Oncologie (SIGRETO), and Université Henri Poincaré - Nancy 1 (UHP)

Subjects
[SDV.CAN] Life Sciences [q-bio]/Cancer, [SDV.CAN]Life Sciences [q-bio]/Cancer
Abstract

published in Oncologie 13(9)S4; National audience

Published
2011

23. Caveolin-1-negative head and neck squamous cell carcinoma primary tumors display increased epithelial to mesenchymal transition and prometastatic properties

Author

Jung, Alain C., primary, Ray, Anne-Marie, additional, Ramolu, Ludivine, additional, Macabre, Christine, additional, Simon, Florian, additional, Noulet, Fanny, additional, Blandin, Anne-Florence, additional, Renner, Guillaume, additional, Lehmann, Maxime, additional, Choulier, Laurence, additional, Kessler, Horst, additional, Abecassis, Joseph, additional, Dontenwill, Monique, additional, and Martin, Sophie, additional

Published
2015
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24. Measuring calpain 3 proteolytic activity using an in vitro substrate

Author

Milić, Astrid, Daniele, Nathalie, Bartoli, Marc, Lochmuller, Hans, Mora, Marina, Comi, Giacomo, Moggio, Maurizio, Noulet, Fanny, Poupiot, Jerome, Richard, Isabelle, Urtizberea, Jan A., and Richard, Isabelle

Subjects
calpain 3, proteolytic activity, in vitro, LGMD 2A, calpain 3 proteolytic activity, diagnosis, dysferlin
Abstract

Limb-girdle muscular dystrophy type 2A (LGMD2A ; OMIM 253600) is an autosomal recessive muscular disorder caused by mutations in the gene coding for calpain 3, a calcium-dependant protease. In order to improve presently available LGMD2A diagnosis, we developed an in vitro assay that can detect the proteolytic activity of calpain 3 in a muscle sample. This assay is based on the use of an inactive calpain 3 that can still be a substrate for active calpain 3 molecules that may be present in the sample to be tested. A total of 80 human biopsies consisting of 43 LGMD2A muscles and 37 controls have been analyzed with this assay. In all controls, normal calpain 3 level and activity were observed. A reduced or absent proteolytic activity was found in 32 (74%) of the LGMD2A biopsies. In the remaining 11 biopsies, normal proteolytic activity was found despite the presence of calpain 3 mutation(s), suggesting that other calpain 3 properties, possibly recognition of substrates or improper localization, should be impaired in those cases to give rise to the LGMD2A phenotype. Although the false positive results are possible, we believe that this assay is a quick and simple approach that improves LGMD2A diagnosis as it is able to test at once several calpain 3 properties.

Published
2006

26. Integrin α5β1 Plays a Critical Role in Resistance to Temozolomide by Interfering with the p53 Pathway in High-Grade Glioma

Author

Janouskova, Hana, primary, Maglott, Anne, additional, Leger, David Y., additional, Bossert, Catherine, additional, Noulet, Fanny, additional, Guerin, Eric, additional, Guenot, Dominique, additional, Pinel, Sophie, additional, Chastagner, Pascal, additional, Plenat, François, additional, Entz-Werle, Natacha, additional, Lehmann-Che, Jacqueline, additional, Godet, Julien, additional, Martin, Sophie, additional, Teisinger, Jan, additional, and Dontenwill, Monique, additional

Published
2012
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29. Contribution of a tyrosine-based motif to cellular trafficking of wild-type and truncated NPY Y1 receptors

Author

Lecat, Sandra, Ouédraogo, Moussa, Cherrier, Thomas, Noulet, Fanny, Rondé, Philippe, Glasser, Nicole, Galzi, Jean-Luc, Mely, Yves, Takeda, Kenneth, and Bucher, Bernard

Subjects
*CELL receptors, *TYROSINE, *NEUROPEPTIDE Y, *G proteins, *KIDNEY diseases, *PEPTIDES, *ALBUMINS
Abstract

Abstract: The human NPY Y1 receptor undergoes fast agonist-induced internalization via clathrin-coated pits then recycles back to the cell membrane. In an attempt to identify the molecular determinants involved in this process, we studied several C-terminal truncation mutants tagged with EFGP. In the absence of agonist, Y1 receptors lacking the last 32 C-terminal amino acids (Y1Δ32) are constitutively internalized, unlike full-length Y1 receptors. At steady state, internalized Y1Δ32 receptors co-localize with transferrin, a marker of early and recycling endosomes. Inhibition of constitutive internalization of Y1Δ32 receptors by hypertonic sucrose or by co-expression of Rab5aS34N, a dominant negative form of the small GTPase Rab5a or depletion of all three isoforms of Rab5 indicates the involvement of clathrin-coated pits. In contrast, a truncated receptor lacking the last 42 C-terminal amino acids (Y1Δ42) does not constitutively internalize, consistent with the possibility that there is a molecular determinant responsible for constitutive internalization located in the last 10 amino acids of Y1Δ32 receptors. We show that the agonist-independent internalization of Y1Δ32 receptors involves a tyrosine-based motif YXXΦ. The potential role of this motif in the behaviour of full-length Y1 receptors has also been explored. Our results indicate that a C-terminal tyrosine-based motif is critical for the constitutive internalization of truncated Y1Δ32 receptors. We suggest that this motif is masked in full-length Y1 receptors which do not constitutively internalize in the absence of agonist. [ABSTRACT FROM AUTHOR]

Published
2011
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