Jul 2026· Clinical Cancer Research· Vol 32, pp. B027-B027· 0 citations
TL;DR
It is shown that glioma models are dependent on TXNRD1 for survival, but acquire adaptive antioxidant changes to survive TXNRD1 loss, and the underlying mechanism using thioredoxin reductase 1 (TrxR1) inhibitors and TXNRD1 knockout (KO) models is validated.
Abstract
Astrocytoma and oligodendroglioma are initiated by missense mutations in isocitrate dehydrogenase 1 and 2 genes (IDH1/2). The mutant IDH1 protein acquires neomorphic activity, producing (R)-2-hydroxyglutarate, which interferes with α-ketoglutarate-dependent epigenetic processes. These effects result in metabolic and epigenetic changes that impair cellular differentiation and promotes tumorigenesis Whole-genome CRISPR/Cas9 knockout screens were conducted using isogenic IDH1-mutant and wild-type (WT) U-87 MG cells and identified the thioredoxin reductase 1 gene (TXNRD1) as a selective dependency in IDH1-mutants. This work sought to validate this dependency and detail the underlying mechanism using thioredoxin reductase 1 (TrxR1) inhibitors and TXNRD1 knockout (KO) models. Antiproliferative potency of TrxR1 inhibitors (auranofin, TRi-1) were similar in IDH1 WT and mutant cells when assessed in both 2D monolayer and 3D soft agar colony assays. Glutathione levels and reduced:oxidized glutathione ratios were decreased similarly in IDH1-mutant and WT cells following TrxR1 inhibition, consistent with increased oxidative stress. Reactive oxygen species (ROS) measured using ROS-Glo™ or CM-H2DCFDA dye were increased following acute treatment with TRi-1 or auranofin. In the ROS-Glo™ studies, ROS levels were modestly higher in IDH1-mutant compared with WT cells. Loss of membrane integrity prevented CM-H2DCFDA dye retention and decreased the ability to accurately assess intracellular ROS. This observed change was consistent with induction of disulfidptosis, which was supported by rapid morphological rounding of cells upon TrxR1 inhibitor treatment, suggestive of actin cytoskeletal collapse. Rescue of TrxR1 inhibitor-treated cultures was achieved using co-treatment with reducing agents (NAC, DTT or TCEP), supporting disulfidptosis as the cell death mechanism. Overall, both IDH1-mutant and WT cells displayed similar sensitivity to TrxR1 inhibition. To confirm the effect of TXNRD1 KO observed in the screen, multiguide RNA-Cas9 ribonucleoproteins were used to generate TXNRD1 knockouts. Neither IDH1-mutant nor WT cells tolerated acute TXNRD1 KO, although some surviving clonal KO lines were developed after several weeks. These KO clones displayed slower growth kinetics and impaired growth in soft agar. In contrast to TrxR1 inhibition, TXNRD1 KO clones displayed decreased CM-H2DCFDA signal compared with unedited cells, suggesting lower basal ROS levels. Quantitative proteomics implicated changes in several metabolic pathways, including amino acid, fatty acid and NRF2 activity, as compensatory mechanisms of TXNRD1 loss in both IDH1-mutant and WT cells. Despite these changes, glutathione levels and reduced:oxidized glutathione ratios were similar in TXNRD1 KO and unedited cell lines. These findings demonstrate that glioma models are dependent on TXNRD1 for survival, but acquire adaptive antioxidant changes to survive TXNRD1 loss. TrxR1 inhibition is acutely cytotoxic, via induction of disulfidptosis, with similar effects in IDH1-mutant and WT models.
Sophia F. O'Brien-Gortner, Dinar Rani K, Daniel Conole, Tet-Woo Lee, Stephen MF. Jamieson, Dean C. Singleton. CRISPR screens identify thioredoxin reductase 1 as a target for inducing disulfidptosis in IDH1-mutant glioma models [abstract]. In: Proceedings of AACR Drug Discovery and Development (AACR D3) Conference; 2026 Jul 21-24; Boston, MA. Philadelphia (PA): AACR; Clin Cancer Res 2026;32(14_Suppl):Abstract nr B027.
An selective, on-target, and well-tolerated DHODH inhibitor, GLIO-1, that is effective in IDH-mutant gliomas is developed and nominated as a new pan-cancer biomarker and targeted therapy pairing, KDM6A inactivation and GLIO-1, that is poised for clinical translation.
Alexander C-Y. Tsai, Mathew D. Lin, V. Puliyappadamba et al.· Clinical Cancer Research· 0 citations
Dual blockade of mutant IDH and glutaminolysis represents a novel, cross-entity therapeutic regimen and offers a promising treatment avenue for rare, surgically challenging IDH-mutant gliomas.
An selective, on-target, and well-tolerated DHODH inhibitor, GLIO-1, that is effective in IDH-mutant gliomas is developed and nominated as a new pan-cancer biomarker and targeted therapy pairing, KDM6A inactivation and GLIO-1, that is poised for clinical translation.
Alexander C-Y. Tsai, Mathew D. Lin, V. Puliyappadamba et al.· Clinical Cancer Research· 0 citations
Loss of the tricarboxylic acid (TCA) cycle enzymes succinate dehydrogenase B (SDHB) and fumarate hydratase (FH) in renal cell carcinoma (RCC) leads to accumulation of the oncometabolites succinate and fumarate, which impair homologous recombination (HR) repair through inhibition of KDM4A/B and aberrant H3K9 hypermethylation at DNA break sites, respectively. These alterations disrupt epigenetic regulation and DNA damage response pathways, potentially creating therapeutic vulnerabilities to DNA-damaging agents, including alkylators. We investigated this vulnerability in SDHB- and FH-deficient RCC models by comparing the activity of KL-50, a novel imidazotetrazine alkylator, with the clinically established agent temozolomide (TMZ). TMZ mediates cytotoxicity predominantly via O6-methylguanine DNA adducts, which are directly reversed by O6-methylguanine-DNA methyltransferase (MGMT). In the absence of MGMT, O6-methylguanine mispairs during replication and triggers the mismatch repair (MMR) pathway, leading to futile repair cycling, replication stress, and cell death. However, TMZ efficacy is frequently limited by acquired MMR inactivation. Mechanistically, KL-50 transfers a 2-fluoroethyl group to O6-guanine to generate O6-(2-fluoroethyl)guanine (O6FEtG), which undergoes spontaneous chemical rearrangement in MGMT-deficient cells to form DNA interstrand crosslinks (ICLs), driving MMR-independent cell death. Using CRISPR, we generated SDHB- and FH-deficient Renca RCC models. We tested KL50 sensitivity in Renca isogenic cells by performing in vitro cell viability assays using serial dilutions of TMZ or KL50 to determine half-maximal inhibitory concentration (IC50) values. For in vivo studies, murine flank tumor models were treated with TMZ or KL-50 (25 mg/kg) or vehicle control via oral gavage on a 5-days-on/2-days-off schedule for two cycles. Tumor volumes were monitored twice weekly, with study endpoints defined as tumor burden >2000 mm3 or ≥20% body weight loss, and Kaplan–Meier survival analyses performed using the Mantel–Cox test. To assess the role of MGMT, MGMT-isogenic SDHB-deficient models were generated through stable MGMT overexpression. SDHB- and FH-deficient models demonstrated marked sensitivity to KL-50 relative to TMZ in both in vitro and in vivo settings. Both parental models exhibited baseline MGMT silencing, consistent with the hypermethylated phenotype previously reported in FH- and SDHB-mutant tumors, suggesting enrichment of MGMT-deficient tumors within these RCC subtypes. Restoration of MGMT expression conferred resistance to both KL-50 and TMZ, establishing MGMT status as a key determinant of therapeutic response. Collectively, these findings identify FH- and SDHB-mutant RCC as a molecularly defined subset characterised by epigenetic MGMT silencing, which may confer selective vulnerability to KL-50. Given that KL-50 retains activity independent of MMR status, it has the potential to overcome resistance mechanisms that have historically constrained the clinical utility of TMZ in this disease context.
Suparna M. Basu, Ranjini Sundaram, Brian Shuch, Susan Gueble, Juan C. Vasquez. Targeting metabolic–DNA repair vulnerabilities in SDHB- and FH-deficient renal cell carcinoma with the novel alkylating agent KL-50 [abstract]. In: Proceedings of AACR Drug Discovery and Development (AACR D3) Conference; 2026 Jul 21-24; Boston, MA. Philadelphia (PA): AACR; Clin Cancer Res 2026;32(14_Suppl):Abstract nr A060.
Suparna M. Basu, R. Sundaram, Brian Shuch et al.· Clinical Cancer Research· 0 citations
Isocitrate dehydrogenase (IDH) enzymes convert isocitrate to α-ketoglutarate. When IDH1 or IDH2 is mutated, the enzyme gains a new function, and the oncometabolite D-2-hydroxyglutarate (D-2-HG) accumulates. Its epigenetic and metabolic effects depend on the tumor context. This review classifies mutant IDH inhibitors by chemical scaffold and relates their binding in the allosteric pocket to structure-activity trends, isoform selectivity, brain penetration, and clinical outcome. Mutant IDH1, mutant IDH2, pan-IDH, and covalent inhibitors are compared, with lessons from successful and failed clinical candidates. Resistance is treated separately: secondary mutations, isoform switching, metabolic adaptation, rational combinations, PROTAC degraders, and biomarkers. Since reduced 2-HG indicates target engagement rather than clinical benefit, design priorities for the next generation of IDH-directed agents are outlined.
Moataz A. Shaldam, Anwar A. El-Hamaky, Nourhan A. Khattab et al.· Drug Discovery Today· 0 citations
Co-mutations of asxl1 and IDH2 are associated with aggressive acute myeloid leukemia (AML), yet the underlying mechanisms have remained poorly understood. We generated a zebrafish model combining asxl1 mutation and IDH2R172K mutation that recapitulates the clinicopathologic and molecular features of high-risk AML with differentiation blockade and reduced animal survival. The double mutant exhibited promoter hypermethylation, downregulation of tet2 expression, and showed global changes in methylation profiles. Genes pertaining to MAPK and AP-1 pathway were upregulated, associated with NADPH oxidase (NOX) expression and an increase in reactive oxygen species (ROS). Single-cell RNA-sequencing confirmed differentiation arrest in HSC-progenitor with activation of MAPK and AP-1 signaling. The double mutants showed resistance to the IDH2 inhibitor but were sensitive to ROS or DNA methylation targeting. In silico analysis of gene expression of human AML carrying co-mutation of ASXL1/IDH2 also showed activation of the MAPK and AP-1 pathway. Our findings underscored an epigenetic-metabolic signaling circuit driving leukemogenesis and revealed novel therapeutic strategies for this AML subtype.
Fangfang He, Yao Ruan, Lingge Tu et al.· Blood Advances· 0 citations
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