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Novel Small-Molecule Protein Phosphatase 2A-Activating Agents

Life Sciences
Therapeutics
College
College of Pharmacy
Researchers
Chen, Ching-Shih
Kulp, Samuel
Wang, Dasheng
Licensing Manager
Paschall, Christopher
614-688-2727
paschall.12@osu.edu

T2009-087 Activation of protein phosphatase 2-A (PP2A) as a target for anticancer therapy with small molecules.

The Need

Previous work indicates that vitamin E succinate (VES) induces apoptosis in different types of cancers cells without significant toxicity to normal cells. Despite advances in the pre-clinical translation of VES in cancer therapy, the mechanisms underlying the effect of this redox-inactive vitamin E derivative on apoptosis remain elusive. To develop better pharmaceuticals that exploit the anti-tumor qualities of VES, the mechanisms that induce apoptosis must be defined.

The Technology

Researchers at The Ohio State University, led by Dr. Ching-Shih Chen, discovered that VES mediates the dephosphorylation of Akt and MAP kinases in LNCaP and PC-3 cells through the activation of protein phosphatase 2-A (PP2A) activity. PP2A downregulates the phosphorylation/activity of Ras targets to antagonize oncogenic signaling. Therefore, activation of PP2A represents a therapeutically relevant strategy to block tumorigenesis and cancer progression. Insight into this PP2A mechanism suggests that VES could be pharmacologically exploited to generate potent small-molecules for the treatment of malignancies.

Commercial Applications

  • Oncology therapeutics
  • Pharmaceuticals

Benefits/Advantages

  • Potent small molecule therapeutic
  • Induces apoptosis in cancer cells through activation of PP2A
  • Perturbs various signaling mechanisms associated with ontogenesis, tumor progression, and metastasis
  • Displays efficacy as a therapeutic without incurring significant toxicity to normal cells