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ter Hoeve, N.

Publications and source records attributed to ter Hoeve, N..

2 recordsLinked to original sources

DDX3 Regulates the Innate Immune Response to Bone Sarcomas

Osteosarcoma (OS) and Ewing sarcoma (EWS) are the most common malignant bone tumors in children and adolescents, with survival rates around 25% in metastatic disease and few advances in treatment in decades. High DDX3 expression has been reported across various sarcoma subtypes. Depending on the context, DDX3 appears to have opposing roles in regulating the tumor immune microenvironment. Within macrophages, DDX3 promotes inflammatory cytokine expression and supports immune cell function. In contrast, in tumor cells DDX3 suppresses a pro-inflammatory state by unwinding dsRNAs, preventing a Type I interferon response. We show that inhibiting DDX3 with RK-33 leads to dsRNA accumulation, inducing a Type I interferon response and broader inflammatory gene expression changes across multiple sarcoma models, shifting macrophage polarization toward a pro-inflammatory M1-like phenotype. To evaluate whether this innate immune microenvironmental remodeling could translate into clinical benefit, we assessed the therapeutic efficacy of RK-33 alone or in combination with mifamurtide, an immunostimulant, in immune competent mouse models of osteosarcoma, with metastatic burden as the primary outcome. We found that in the absence of MYC over-expression, the combination treatment significantly reduced metastatic spread. These findings support targeting DDX3 as a novel innate immune based therapeutic strategy and highlight that the tumors molecular landscape critically influences therapeutic responsiveness.

cancer biology↗

RNA Helicase DDX3 Regulates RAD51 Localization and DNA Damage Repair in Ewing Sarcoma

We previously demonstrated that RNA helicase DDX3X (DDX3) can be a therapeutic target in Ewing sarcoma (EWS), but its role in EWS biology remains unclear. The present work demonstrates that DDX3 plays a unique role in DNA damage repair (DDR). We show that DDX3 interacts with several proteins involved in homologous recombination, including RAD51, RECQL1, RPA32, and XRCC2. In particular, DDX3 colocalizes with RAD51 and RNA:DNA hybrid structures in the cytoplasm of EWS cells. Inhibition of DDX3 RNA helicase activity increases cytoplasmic RNA:DNA hybrids, sequestering RAD51 in the cytoplasm, which impairs nuclear translocation of RAD51 to sites of double-stranded DNA breaks thus increasing sensitivity of EWS to radiation treatment, both in vitro and in vivo. This discovery lays the foundation for exploring new therapeutic approaches directed at manipulating DDR protein localization in solid tumors.

cancer biology↗