cisplatin

SIRT3 promotes GC progression and chemoresistance by deacetylating and stabilizing the mitochondrial ADP/ATP translocator SLC25A6 (ANT3), thereby enhancing mitochondrial metabolic activity. The SIRT3-ANT3 axis represents a novel molecular mechanism driving GC malignancy and chemoresistance and may serve as a promising therapeutic target for improving treatment efficacy in GC.

Six prognostic genes, particularly RAB25 and PLAU, influence ESCC progression and immune microenvironment remodeling.

These findings suggest that rapamycin enhances the mechanistic efficacy of cisplatin by specifically targeting and reducing cisplatin-induced stemness (CD133+ CSC population). This study proposes a viable combination therapy for HNSCC involving an mTOR inhibitor and a platinum-based drug to overcome CSC-mediated resistance.

P1, N=55, Active, not recruiting, Boehringer Ingelheim | Recruiting --> Active, not recruiting

P3, N=861, Active, not recruiting, AstraZeneca | Recruiting --> Active, not recruiting | Trial primary completion date: Nov 2027 --> Nov 2028

P3, N=330, Active, not recruiting, Radiation Therapy Oncology Group | Trial completion date: Jan 2025 --> Nov 2028 | Trial primary completion date: Jan 2025 --> Nov 2028 | Completed --> Active, not recruiting

P3, N=379, Completed, Children's Oncology Group | Active, not recruiting --> Completed | Trial completion date: Jun 2028 --> Mar 2026

P2, N=31, Completed, Biotheus Inc. | Recruiting --> Completed | N=55 --> 31 | Trial completion date: Jun 2026 --> Mar 2026 | Trial primary completion date: Jun 2026 --> Mar 2026

We report the case of a 26-year-old man with a primary mediastinal yolk sac tumor who progressed despite multimodal therapy, including etoposide, ifosfamide, and cisplatin chemotherapy, high-dose carboplatin and etoposide with autologous stem cell transplantation, gemcitabine and paclitaxel, surgical debulking, and radiation therapy. No further disease-directed therapies were available, and he ultimately died from progressive metastatic disease. This case highlights the aggressive biology of platinum-resistant primary mediastinal yolk sac tumors, illustrates primary resistance to programmed death-1 inhibition, and underscores the urgent need for more effective salvage strategies in this high-risk population.

In addition, mTOR pathway activity and responsiveness to mTOR inhibitors (rapamycin and ipatasertib) and chemotherapeutic agents (cisplatin) were assessed. Compared with 2D monolayer cultures, 3D TMSs exhibited reduced mTOR signaling activity, which led to significantly decreased sensitivity to mTOR inhibition. These findings indicate that 3D bioprinted breast cancer models recapitulate key structural and signaling features of in situ tumors more accurately than 2D systems, highlighting their potential value for preclinical drug testing and mechanistic studies.

This study comprehensively identifies the vessel-threatening effects of cisplatin (CDDP), carboplatin (CBP), and oxaliplatin (OXA) and aims to compile an analytical model. The results suggest activation of the oxidative stress pathway through Nrf2 inhibition and increased ICAM1 levels, alongside pathway‑specific alterations such as reduced HIF1A and NOS3 expression and decreased VCAM1 levels. Early cardiovascular monitoring and Nrf2‑targeted therapy warrant further investigation.

The most potent derivative identified was 2-(3-(benzo[d]thiazol-2-yl)-1H-indol-1-yl)-N-(2,4-dimethoxyphenyl)acetamide (9d) which demonstrated IC50 values of 7.9 ± 1.6, 16.1 ± 0.5, and 9.3 ± 2.2 µM against A549, SW480, and HepG2 cells, respectively, comparable or even superior to those of cisplatin (IC50s were 5.7 ± 1.6, 15.2 ± 0.3, and 14.3 ± 1.9 µM for A549, SW480, and HepG2 cells, respectively)...In silico predictions regarding drug-likeness, pharmacokinetics, and toxicological characteristics suggest that the promising derivative 9d could be proposed as a potential anticancer drug for further preclinical studies. Molecular docking studies revealed that 9d was well accommodated within the endothelial growth factor receptor (EGFR) active site.