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Article ; Online: Local delivery of doxorubicin prodrug via lipid nanocapsule-based hydrogel for the treatment of glioblastoma.

Wang, Mingchao / Bergès, Raphaël / Malfanti, Alessio / Préat, Véronique / Bastiancich, Chiara

Drug delivery and translational research

2023

Abstract: Glioblastoma (GBM) recurrences appear in most cases around the resection cavity borders and arise from residual GBM cells that cannot be removed by surgery. Here, we propose a novel treatment that combines the advantages of nanomedicine and local drug ... ...

Abstract	Glioblastoma (GBM) recurrences appear in most cases around the resection cavity borders and arise from residual GBM cells that cannot be removed by surgery. Here, we propose a novel treatment that combines the advantages of nanomedicine and local drug delivery to target these infiltrating GBM cells. We developed an injectable lipid nanocapsule (LNC)-based formulation loaded with lauroyl-doxorubicin prodrug (DOXC
Language	English
Publishing date	2023-10-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	2590155-2
ISSN	2190-3948 ; 2190-393X
ISSN (online)	2190-3948
ISSN	2190-393X
DOI	10.1007/s13346-023-01456-y
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Article ; Online: Low concentrations of vorinostat decrease EB1 expression in GBM cells and affect microtubule dynamics, cell survival and migration.

Perez, Thomas / Bergès, Raphaël / Maccario, Hélène / Oddoux, Sarah / Honoré, Stéphane

Oncotarget

2021 Volume 12, Issue 4, Page(s) 304–315

Abstract: Glioblastoma multiform (GBM) is the most frequent primitive brain tumor with a high recurrence and mortality. Histone deacetylase inhibitors (HDACi) have evoked great interest because they are able to change transcriptomic profiles to promote tumor cell ... ...

Abstract	Glioblastoma multiform (GBM) is the most frequent primitive brain tumor with a high recurrence and mortality. Histone deacetylase inhibitors (HDACi) have evoked great interest because they are able to change transcriptomic profiles to promote tumor cell death but also induce side effects due to the lack of selectivity. We show in this paper new anticancer properties and mechanisms of action of low concentrations of vorinostat on various GBM cells which acts by affecting microtubule cytoskeleton in a non-histone 3 (H3) manner. Indeed, vorinostat induces tubulin acetylation and detyrosination, affects EB stabilizing cap on microtubule plus ends and suppresses microtubule dynamic instability. We previously identified EB1 overexpression as a marker of bad prognostic in GBM. Interestingly, we show for the first time to our knowledge, a strong decrease of EB1 expression in GBM cells by a drug. Altogether, our results suggest that low dose vorinostat, which is more selective for HDAC6 inhibition, could therefore represent an interesting therapeutic option for GBM especially in patients with EB1 overexpressing tumor with lower expected side effects. A validation of our hypothesis is needed during future clinical trials with this drug in GBM.
Language	English
Publishing date	2021-02-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.27892
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Article ; Online: Deciphering the Action of Neuraminidase in Glioblastoma Models.

Baeza-Kallee, Nathalie / Bergès, Raphaël / Hein, Victoria / Cabaret, Stéphanie / Garcia, Jeremy / Gros, Abigaëlle / Tabouret, Emeline / Tchoghandjian, Aurélie / Colin, Carole / Figarella-Branger, Dominique

International journal of molecular sciences

2023 Volume 24, Issue 14

Abstract: Glioblastoma (GBM) contains cancer stem cells (CSC) that are resistant to treatment. GBM CSC expresses glycolipids recognized by the A2B5 antibody. A2B5, induced by the enzyme ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyl transferase 3 (ST8Sia3), plays ...

Abstract	Glioblastoma (GBM) contains cancer stem cells (CSC) that are resistant to treatment. GBM CSC expresses glycolipids recognized by the A2B5 antibody. A2B5, induced by the enzyme ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyl transferase 3 (ST8Sia3), plays a crucial role in the proliferation, migration, clonogenicity and tumorigenesis of GBM CSC. Our aim was to characterize the resulting effects of neuraminidase that removes A2B5 in order to target GBM CSC. To this end, we set up a GBM organotypic slice model; quantified A2B5 expression by flow cytometry in U87-MG, U87-ST8Sia3 and GBM CSC lines, treated or not by neuraminidase; performed RNAseq and DNA methylation profiling; and analyzed the ganglioside expression by liquid chromatography-mass spectrometry in these cell lines, treated or not with neuraminidase. Results demonstrated that neuraminidase decreased A2B5 expression, tumor size and regrowth after surgical removal in the organotypic slice model but did not induce a distinct transcriptomic or epigenetic signature in GBM CSC lines. RNAseq analysis revealed that
MeSH term(s)	Humans ; Glioblastoma/metabolism ; Neuraminidase/genetics ; Neuraminidase/metabolism ; Brain Neoplasms/metabolism ; Cell Line, Tumor ; Cell Proliferation ; Neoplastic Stem Cells/metabolism
Chemical Substances	Neuraminidase (EC 3.2.1.18)
Language	English
Publishing date	2023-07-19
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms241411645
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Article ; Online: EB1-dependent long survival of glioblastoma-grafted mice with the oral tubulin-binder BAL101553 is associated with inhibition of tumor angiogenesis.

Bergès, Raphaël / Tchoghandjian, Aurélie / Sergé, Arnauld / Honoré, Stéphane / Figarella-Branger, Dominique / Bachmann, Felix / Lane, Heidi A / Braguer, Diane

Oncotarget

2020 Volume 11, Issue 8, Page(s) 759–774

Abstract: Glioblastoma (GBM) are aggressive brain tumors with limited treatment options. Cancer stem-like cells (CSLCs) contribute to GBM invasiveness, representing promising targets. BAL101553, a prodrug of BAL27862, is a novel small molecule tubulin-binding ... ...

Abstract	Glioblastoma (GBM) are aggressive brain tumors with limited treatment options. Cancer stem-like cells (CSLCs) contribute to GBM invasiveness, representing promising targets. BAL101553, a prodrug of BAL27862, is a novel small molecule tubulin-binding agent, promoting tumor cell death through spindle assembly checkpoint activation, which is currently in Phase 1/2a in advanced solid tumor patients including GBM. This study aimed to evaluate long-term daily oral BAL101553 treatment of mice orthotopically grafted with GBM CSLCs (GBM6) according to EB1 expression-level, and to decipher its mechanism of action on GBM stem cells. Oral treatment with BAL101553 for 100 days provoked a large EB1 expression level-dependent survival benefit, together with a decrease in tumor growth and brain invasion. Formation of vascular structures by the fluorescent GBM6-GFP-sh0 cells, mimicking endothelial vascular networks, was observed in the brains of control grafted mice. Following BAL101553 treatment, vessels were no longer detectable, suggesting inhibition of the endothelial trans-differentiation of GBM stem cells.
Language	English
Publishing date	2020-02-25
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.27374
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Article ; Online: Combination drug screen targeting glioblastoma core vulnerabilities reveals pharmacological synergisms.

EBioMedicine

2023 Volume 95, Page(s) 104752

Abstract: Background: Pharmacological synergisms are an attractive anticancer strategy. However, with more than 5000 approved-drugs and compounds in clinical development, identifying synergistic treatments represents a major challenge.: Methods: High- ... ...

Abstract	Background: Pharmacological synergisms are an attractive anticancer strategy. However, with more than 5000 approved-drugs and compounds in clinical development, identifying synergistic treatments represents a major challenge. Methods: High-throughput screening was combined with target deconvolution and functional genomics to reveal targetable vulnerabilities in glioblastoma. The role of the top gene hit was investigated by RNA interference, transcriptomics and immunohistochemistry in glioblastoma patient samples. Drug combination screen using a custom-made library of 88 compounds in association with six inhibitors of the identified glioblastoma vulnerabilities was performed to unveil pharmacological synergisms. Glioblastoma 3D spheroid, organotypic ex vivo and syngeneic orthotopic mouse models were used to validate synergistic treatments. Findings: Nine targetable vulnerabilities were identified in glioblastoma and the top gene hit RRM1 was validated as an independent prognostic factor. The associations of CHK1/MEK and AURKA/BET inhibitors were identified as the most potent amongst 528 tested pairwise drug combinations and their efficacy was validated in 3D spheroid models. The high synergism of AURKA/BET dual inhibition was confirmed in ex vivo and in vivo glioblastoma models, without detectable toxicity. Interpretation: Our work provides strong pre-clinical evidence of the efficacy of AURKA/BET inhibitor combination in glioblastoma and opens new therapeutic avenues for this unmet medical need. Besides, we established the proof-of-concept of a stepwise approach aiming at exploiting drug poly-pharmacology to unveil druggable cancer vulnerabilities and to fast-track the identification of synergistic combinations against refractory cancers. Funding: This study was funded by institutional grants and charities.
MeSH term(s)	Animals ; Mice ; Glioblastoma/drug therapy ; Glioblastoma/genetics ; Aurora Kinase A ; Drug Synergism ; Cell Line, Tumor ; Antineoplastic Agents/pharmacology ; Drug Combinations
Chemical Substances	Aurora Kinase A (EC 2.7.11.1) ; Antineoplastic Agents ; Drug Combinations
Language	English
Publishing date	2023-08-10
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2851331-9
ISSN	2352-3964
ISSN (online)	2352-3964
DOI	10.1016/j.ebiom.2023.104752
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Article: Glycolipids Recognized by A2B5 Antibody Promote Proliferation, Migration, and Clonogenicity in Glioblastoma Cells.

Baeza-Kallee, Nathalie / Bergès, Raphaël / Soubéran, Aurélie / Colin, Carole / Denicolaï, Emilie / Appay, Romain / Tchoghandjian, Aurélie / Figarella-Branger, Dominique

Cancers

2019 Volume 11, Issue 9

Abstract: A2B5+ cells isolated from human glioblastomas exhibit cancer stem cell properties. The A2B5 epitope belongs to the sialoganglioside family and is synthetized by the ST8 alpha-N-acetyl-neuraminidase α-2,8-sialyltransferase 3 (ST8SIA3) enzyme. Glycolipids ... ...

Abstract	A2B5+ cells isolated from human glioblastomas exhibit cancer stem cell properties. The A2B5 epitope belongs to the sialoganglioside family and is synthetized by the ST8 alpha-N-acetyl-neuraminidase α-2,8-sialyltransferase 3 (ST8SIA3) enzyme. Glycolipids represent attractive targets for solid tumors; therefore, the aim of this study was to decipher A2B5 function in glioblastomas. To this end, we developed cell lines expressing various levels of A2B5 either by genetically manipulating ST8SIA3 or by using neuraminidase. The overexpression of ST8SIA3 in low-A2B5-expressing cells resulted in a dramatic increase of A2B5 immunoreactivity. ST8SIA3 overexpression increased cell proliferation, migration, and clonogenicity in vitro and tumor growth when cells were intracranially grafted. Conversely, lentiviral ST8SIA3 inactivation in low-A2B5-expressing cells resulted in reduced proliferation, migration, and clonogenicity in vitro and extended mouse survival. Furthermore, in the shST8SIA3 cells, we found an active apoptotic phenotype. In high-A2B5-expressing cancer stem cells, lentiviral delivery of shST8SIA3 stopped cell growth. Neuraminidase treatment, which modifies the A2B5 epitope, impaired cell survival, proliferation, self-renewal, and migration. Our findings prove the crucial role of the A2B5 epitope in the promotion of proliferation, migration, clonogenicity, and tumorigenesis, pointing at A2B5 as an attractive therapeutic target for glioblastomas.
Language	English
Publishing date	2019-08-28
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers11091267
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Article ; Online: Axon cytoskeleton proteins specifically modulate oligodendrocyte growth and differentiation in vitro.

Fressinaud, Catherine / Berges, Raphaël / Eyer, Joël

Neurochemistry international

2012 Volume 60, Issue 1, Page(s) 78–90

Abstract: In multiple sclerosis (MS) remyelination by oligodendrocytes (OL) is incomplete, and it is associated with a decrease in axonal neurofilaments (NF) and tubulin (TUB). To determine whether these proteins could participate directly in MS remyelination ... ...

Abstract	In multiple sclerosis (MS) remyelination by oligodendrocytes (OL) is incomplete, and it is associated with a decrease in axonal neurofilaments (NF) and tubulin (TUB). To determine whether these proteins could participate directly in MS remyelination failure, or indirectly through proteins that are co-associated, we have analysed their effects in pure OL cultures. Rat brain NF fractions, recovered by successive centrifugations increase either OL progenitor (OLP) proliferation (2nd pellet, P2), or only their maturation (P5), whereas albumin, liver and skin proteins, as well as recombinant GFAP or purified actin were ineffective. NF (P2) copurify mainly with TUB, as well as with other proteins, like MAPs, Tau, spectrin β2, and synapsin 2. These purified, or recombinant, proteins increased OLP proliferation without delaying their maturation, and appeared responsible for the proliferation observed with P2 fractions. Among putative signaling pathways mediating these effects Fyn kinase was not involved. Whereas NF did not alter the growth of cultured astrocytes, the NF associated proteins enhanced their proliferation. This suggests that NF and their associated proteins exert specific effects on OL development, broadening the field of axon-oligodendrocyte interactions. In case of axon damage in vivo, extracellular release of such axonal proteins could regulate remyelination and astrocytic gliosis.
MeSH term(s)	Animals ; Astrocytes/cytology ; Astrocytes/metabolism ; Axons/chemistry ; Axons/physiology ; Cell Differentiation/drug effects ; Cells, Cultured ; Cytoskeletal Proteins/pharmacology ; Neurofilament Proteins/pharmacology ; Oligodendroglia/cytology ; Oligodendroglia/drug effects ; Oligodendroglia/metabolism ; Rats ; Rats, Sprague-Dawley
Chemical Substances	Cytoskeletal Proteins ; Neurofilament Proteins
Language	English
Publishing date	2012-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	283190-9
ISSN	1872-9754 ; 0197-0186
ISSN (online)	1872-9754
ISSN	0197-0186
DOI	10.1016/j.neuint.2011.10.011
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Zs.A 1610: Show issues

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Article ; Online: Proscillaridin A exerts anti-tumor effects through GSK3β activation and alteration of microtubule dynamics in glioblastoma.

Berges, Raphael / Denicolai, Emilie / Tchoghandjian, Aurélie / Baeza-Kallee, Nathalie / Honore, Stephane / Figarella-Branger, Dominique / Braguer, Diane

Cell death & disease

2018 Volume 9, Issue 10, Page(s) 984

Abstract: Glioblastoma (GBM) is characterized by highly aggressive growth and invasive behavior. Due to the highly lethal nature of GBM, new therapies are urgently needed and repositioning of existing drugs is a promising approach. We have previously shown the ... ...

Abstract	Glioblastoma (GBM) is characterized by highly aggressive growth and invasive behavior. Due to the highly lethal nature of GBM, new therapies are urgently needed and repositioning of existing drugs is a promising approach. We have previously shown the activity of Proscillaridin A (ProA), a cardiac glycoside inhibitor of the Na(+)/K(+) ATPase (NKA) pump, against proliferation and migration of GBM cell lines. ProA inhibited tumor growth in vivo and increased mice survival after orthotopic grafting of GBM cells. This study aims to decipher the mechanism of action of ProA in GBM tumor and stem-like cells. ProA displayed cytotoxic activity on tumor and stem-like cells grown in 2D and 3D culture, but not on healthy cells as astrocytes or oligodendrocytes. Even at sub-cytotoxic concentration, ProA impaired cell migration and disturbed EB1 accumulation at microtubule (MT) plus-ends and MT dynamics instability. ProA activates GSK3β downstream of NKA inhibition, leading to EB1 phosphorylation on S155 and T166, EB1 comet length shortening and MT dynamics alteration, and finally inhibition of cell migration and cytotoxicity. Similar results were observed with digoxin. Therefore, we disclosed here a novel pathway by which ProA and digoxin modulate MT-governed functions in GBM tumor and stem-like cells. Altogether, our results support ProA and digoxin as potent candidates for drug repositioning in GBM.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Animals ; Antineoplastic Agents/pharmacology ; Astrocytes/metabolism ; Brain Neoplasms/pathology ; Cell Line, Tumor ; Cell Movement/drug effects ; Cell Proliferation/drug effects ; Glioblastoma/pathology ; Glycogen Synthase Kinase 3 beta/metabolism ; Humans ; Ion Pumps/metabolism ; Mice ; Microtubule-Associated Proteins/antagonists & inhibitors ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Phosphorylation/drug effects ; Polymerization/drug effects ; Proscillaridin/pharmacology ; Tubulin/metabolism
Chemical Substances	Antineoplastic Agents ; Ion Pumps ; MAPRE1 protein, human ; Microtubule-Associated Proteins ; Tubulin ; Glycogen Synthase Kinase 3 beta (EC 2.7.11.1) ; Adenosine Triphosphatases (EC 3.6.1.-) ; Proscillaridin (KC6BL281EN)
Language	English
Publishing date	2018-09-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-018-1018-7
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Article ; Online: Structure-function analysis of the glioma targeting NFL-TBS.40-63 peptide corresponding to the tubulin-binding site on the light neurofilament subunit.

Berges, Raphael / Balzeau, Julien / Takahashi, Masayuki / Prevost, Chantal / Eyer, Joel

PloS one

2012 Volume 7, Issue 11, Page(s) e49436

Abstract: We previously reported that a 24 amino acid peptide (NFL-TBS.40-63) corresponding to the tubulin-binding site located on the light neurofilament subunit, selectively enters in glioblastoma cells where it disrupts their microtubule network and inhibits ... ...

Abstract	We previously reported that a 24 amino acid peptide (NFL-TBS.40-63) corresponding to the tubulin-binding site located on the light neurofilament subunit, selectively enters in glioblastoma cells where it disrupts their microtubule network and inhibits their proliferation. Here, we analyzed the structure-function relationships using an alanine-scanning strategy, in order to identify residues essential for these biological activities. We showed that the majority of modified peptides present a decreased or total loss to penetrate in these cells, or to alter microtubules. Correspondingly, circular dichroism measurements showed that this peptide forms either β-sheet or α-helix structures according to the solvent and that alanine substitution modified or destabilized the structure, in relation with changes in the biological activities. Moreover, substitution of serine residues by phosphoserine or aspartic acid concomitantly decreased the cell penetrating activity and the structure stability. These results indicate the importance of structure for the activities, including selectivity to glioblastoma cells of this peptide, and its regulation by phosphorylation.
MeSH term(s)	Alanine/metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Binding Sites ; Brain Neoplasms/metabolism ; Brain Neoplasms/pathology ; Cell Line, Tumor ; Circular Dichroism ; Endocytosis ; Glioma/metabolism ; Glioma/pathology ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis/genetics ; Mutant Proteins/chemistry ; Mutant Proteins/metabolism ; Neurofilament Proteins/chemistry ; Neurofilament Proteins/metabolism ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Phosphorylation ; Protein Binding ; Protein Folding ; Protein Stability ; Structure-Activity Relationship ; Tubulin/metabolism
Chemical Substances	Mutant Proteins ; NFL-TBS.40-63 peptide ; Neurofilament Proteins ; Peptide Fragments ; Tubulin ; neurofilament protein L ; Alanine (OF5P57N2ZX)
Language	English
Publishing date	2012-11-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0049436
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Article ; Online: A tubulin binding peptide targets glioma cells disrupting their microtubules, blocking migration, and inducing apoptosis.

Berges, Raphael / Balzeau, Julien / Peterson, Alan C / Eyer, Joel

Molecular therapy : the journal of the American Society of Gene Therapy

2012 Volume 20, Issue 7, Page(s) 1367–1377

Abstract: Despite aggressive treatment regimes, glioma remains a largely fatal disease. Current treatment limitations are attributed to the precarious locations within the brain where such tumors grow, their highly infiltrative nature precluding complete resection ...

Abstract	Despite aggressive treatment regimes, glioma remains a largely fatal disease. Current treatment limitations are attributed to the precarious locations within the brain where such tumors grow, their highly infiltrative nature precluding complete resection and lack of specificity among agents capable of attenuating their growth. Here, we show that in vitro, glioma cells of diverse origins internalize a peptide encompassing a tubulin-binding site (TBS) on the neurofilament light protein. The internalized peptide disrupts the microtubule network, inhibits migration and proliferation, and leads to apoptosis. Using an intracerebral transplant model, we show that most, if not all, of these responses to peptide exposure also occur in vivo. Notably, a single intratumor injection significantly attenuates tumor growth, while neither peptide uptake nor downstream consequences are observed elsewhere in the host nervous system. Such preferential uptake suggests that the peptide may have potential as a primary or supplementary glioblastoma treatment modality by exploiting its autonomous microtubule-disrupting activity or engaging its capacity to selectively target glioma cells with other cell-disrupting cargos.
MeSH term(s)	Animals ; Apoptosis/drug effects ; Brain/metabolism ; Brain Neoplasms/drug therapy ; Cell Line, Tumor ; Cell Movement/drug effects ; Cell Proliferation/drug effects ; Female ; Glioma/drug therapy ; Microtubules/drug effects ; Neurofilament Proteins/metabolism ; Neurofilament Proteins/pharmacology ; Neurofilament Proteins/therapeutic use ; Peptide Fragments/metabolism ; Peptide Fragments/pharmacology ; Peptide Fragments/therapeutic use ; Protein Binding ; Random Allocation ; Rats ; Rats, Inbred F344 ; Tubulin/metabolism
Chemical Substances	Neurofilament Proteins ; Peptide Fragments ; Tubulin ; neurofilament protein L
Language	English
Publishing date	2012-04-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2010592-7
ISSN	1525-0024 ; 1525-0016
ISSN (online)	1525-0024
ISSN	1525-0016
DOI	10.1038/mt.2012.45
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