bioRxiv Science⌕ Search

bioRxiv · 10.1101/2024.12.13.627927

PARP inhibitor counteracts Temozolomide Resistance in Glioblastoma Multiforme

Abstract

BackgroundGlioblastoma multiforme (GBM) is the most common malignant primary brain tumour in adults and is invariably associated with poor prognosis. Resistance to Temozolomide (TMZ), the standard chemotherapeutic agent, remains a major clinical challenge, particularly due to DNA mismatch repair (MMR) deficiencies. The aim of this study was to determine whether combining TMZ with the poly(ADP-ribose) polymerase inhibitor Olaparib (OLA) could overcome TMZ resistance in GBM. MethodsWe conducted in vitro experiments using U251 cell-line, including a TMZ-resistant derivative, and primary GBM cultures derived from patient tumours. A CRISPR/Cas9 knockout screen was employed to identify genes involved in TMZ resistance. Cell viability, proliferation, and morphology were assessed following treatment with TMZ, OLA, or their combination. ResultsThe CRISPR screen identified inactivation of MMR pathway genes as key mediators of TMZ resistance. Co-treatment with OLA and TMZ demonstrated synergistic cytotoxicity in both parental and TMZ-resistant U251 cells, as well as in primary GBM cultures at diagnosis or relapse. Notably, OLA restored sensitivity to TMZ in MMR-deficient contexts and in tumours expressing O6-methylguanine-DNA-methyltransferase (MGMT). The combination treatment induced persistent DNA damage, cell cycle disruption, and cell death. ConclusionsThese findings provide strong preclinical evidence that combining TMZ with OLA can effectively overcome key mechanisms of TMZ resistance in GBM. This approach offers a promising therapeutic strategy warranting further clinical investigation. IMPORTANCE OF THE STUDYTemozolomide (TMZ) resistance remains a major therapeutic obstacle in glioblastoma (GBM), often driven by MMR deficiency or MGMT expression. While poly(ADP-ribose) polymerase (PARP) inhibitors have shown potential in other cancers, their role in overcoming TMZ resistance in GBM has remained unclear. In this study, a CRISPR screen identified MMR deficiency as a key driver of TMZ resistance. We further demonstrate that co-treatment with the PARP inhibitor Olaparib (OLA) restores TMZ sensitivity in both MMR-deficient and MGMT-expressing GBM cells and patient-derived cultures. These findings provide strong preclinical evidence supporting PARP inhibition as a promising therapeutic strategy to overcome chemoresistance in GBM and justify further clinical investigation. KEY POINTSO_LIPARP inhibitor Olaparib restores temozolomide sensitivity in resistant GBM cells C_LIO_LICombination therapy overcomes resistance driven by MMR deficiency or MGMT expression C_LIO_LIDual treatment induces persistent DNA damage and apoptosis in glioblastoma primary cultures C_LI

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Samarut, E., Tabourel, G., Briand, J., Landais, Y., Gratas, C., Cartron, P.-F., Vallette, F., Oliver, L., Serandour, A. A.. 2024-12-16. PARP inhibitor counteracts Temozolomide Resistance in Glioblastoma Multiforme. https://doi.org/10.1101/2024.12.13.627927

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Tet2-Clonal Hematopoiesis Promotes Whereas Dnmt3a-CH Inhibits Breast Cancer Progression During Aging

Clonal hematopoiesis of indeterminate potential (CHIP) driven by somatic mutations in blood cells increases with age and is associated with adverse outcomes in cancer patients. How CHIP mutations influence solid tumor progression remains unclear. Using inducible murine models of Dnmt3a- or Tet2-mutant CHIP combined with orthotopic syngeneic breast cancer models, we demonstrate that upon aging Dnmt3a-mutant CHIP prevents whereas Tet2-mutant CHIP drives breast cancer progression. Dnmt3a-mutant immune infiltrates established interferon-mediated MHCIIhigh tumor-associated macrophages (TAMs) that supported cytotoxic CD8+ T cell-mediated tumor rejection. In contrast, Tet2-mutant TAMs exhibited an inflammatory, immunosuppressive phenotype characterized by increased IL-1 and CXCL2 production, reduced MHCII expression, and impaired T cell recruitment and activation. Therapeutic blockade of IL-1R1 or CXCR2 reduced tumor progression in aged Tet2-mutant CHIP mice and partially restored anti-tumor immunity. These findings establish that the effects of CHIP on cancer are mutation- and age-dependent and identify IL-1/CXCL2-driven inflammation as a therapeutic vulnerability of tumor-promoting Tet2-mutant CHIP.

cancer biology↗

Single Nucleus Profiling Reveals Rewired Tumor-Immune-Stromal Cell Communication in Plasmacytoid Urothelial Carcinoma

Plasmacytoid urothelial carcinoma (PUC) is an aggressive histologic subtype of bladder cancer associated with worse patient outcomes and therapeutic response compared to conventional urothelial carcinoma (CUC). While recent work has demonstrated metastatic lymph nodes from PUC tumors have an inflamed phenotype, how the tumor microenvironment (TME) and crosstalk between tumor, stromal, and immune cells in primary PUC bladder tumors differs from those in CUC remains poorly understood. The impact of these differences on response to immunotherapy is also unknown. To understand TME differences between CUC and PUC and their impact on cell signaling, we performed single nucleus RNA sequencing on PUC and CUC tumors, as well as Xenium spatial transcriptomics on a mixed CUC / PUC tumor. We identified increased signaling between PUC-enriched, CDH1-low urothelial cells, immunosuppressive lipid-associated macrophages, and SFRP2+/CTHRC1+ fibroblasts in PUC tumors compared to CUC. Spatial transcriptomics identified increased macrophage infiltration in PUC histology and colocalization of PUC tumor cells, immunosuppressive macrophages, and SFRP2+ fibroblasts. Taken together, this study delineates PUC architecture and demonstrates interplay CDH1-low tumor cells, EMT, and immunosuppressive macrophages, identifying possible therapeutic vulnerabilities in PUC.

cancer biology↗

The Phospholipase A2 Activity of Peroxiredoxin 6 Protects Hepatocarcinoma Cells Against Ferroptosis and Mitophagy Impairment

Peroxiredoxin 6 (PRDX6) is a moonlighting protein that plays a key role in regulating redox homeostasis and lipid metabolism through its unique dual peroxidase and calcium-independent phospholipase A2 (iPLA2) activities. Here, we generated a stable HepG2 cell line harboring a D140A mutation to selectively ablate iPLA2 activity, and we compared its phenotype with that of wild-type (WT) and PRDX6-knockout (KO) cells. D140A exhibited low ROS leves, similar to WT cells, confirming that oxidative stress is due to peroxidase deficiency. In contrast, D140A cells displayed higher lipid peroxidation than WT cells, though significantly lower than that of KO cells. Furthermore, the D140A mutant mirrored the KO phenotype regarding intracellular ferrous iron accumulation, impaired lipid droplet biogenesis, and the downregulation of the key ferroptosis regulator GPX4. Mechanistically, integrated proteomic, lipidomic, and enzymatic analyses revealed that a deficiency in iPLA2 activity of PRDX6 disrupted the release of key lipid species necessary for cell structure and signaling. Consequently, organelles involved in lipid synthesis and trafficking, such as peroxisomes, endoplasmic reticulum, mitochondria and lipid droplet, were affected. Specifically, we found that mitochondria exhibited a reduction in cristae and a diminished capacity for mitophagy and autophagy, which ultimately makes cells much more susceptible to erastin-induced ferroptotic cell death. Taken together, our findings demonstrate that PRDX6 iPLA2 activity uniquely coordinates organelle lipid homeostasis and mitophagy to protect cancer cells from ferroptotic cell death. Consequently, the use of iPLA2 inhibitors such as MJ33, which decreased PRDX6 iPLA2 activity to a level comparable to the mutant D140A, could represent a promising therapeutic strategy for inducing ferroptotic cell death in hepatocellular carcinoma.

cancer biology↗