PDHA1-acetylation signaling suppresses cuproptosis to attenuate anti-androgen effect in prostate cancer

Cell Death Dis. 2026 Feb 23;17(1):243. doi: 10.1038/s41419-026-08462-1.

Abstract

Acquired resistance to enzalutamide (Enz) presents a significant challenge in castration-resistant prostate cancer (CRPC), and overcoming this resistance remains an unmet clinical need. Here, we identified cuproptosis, a copper-dependent mechanism of regulated cell death, as a key driver of Enz resistance. Both in vitro and in vivo models demonstrated that pyruvate dehydrogenase E1 alpha subunit (PDHA1) serves as a critical modulator of cuproptosis and Enz sensitivity. Mechanistically, PDHA1 increases intracellular acetyl-CoA, enhancing histone H3K27 acetylation and upregulating solute carrier family 7 member 11 (SLC7A11), which promotes cysteine uptake and glutathione (GSH) synthesis. Elevated GSH chelates intracellular copper, thereby suppressing cuproptosis and reducing Enz efficacy. Targeting PDHA1 significantly restores cuproptosis and sensitizes CRPC cells to Enz treatment. These findings underscore the potential of PDHA1 inhibition to counteract Enz resistance by reactivating cuproptosis, offering a promising therapeutic approach for treating refractory prostate cancer.

MeSH terms

  • Acetylation / drug effects
  • Androgen Antagonists* / pharmacology
  • Animals
  • Benzamides / pharmacology
  • Cell Line, Tumor
  • Copper* / metabolism
  • Drug Resistance, Neoplasm / drug effects
  • Glutathione / metabolism
  • Humans
  • Male
  • Mice
  • Mice, Nude
  • Nitriles / pharmacology
  • Phenylthiohydantoin / analogs & derivatives
  • Phenylthiohydantoin / pharmacology
  • Prostatic Neoplasms, Castration-Resistant* / drug therapy
  • Prostatic Neoplasms, Castration-Resistant* / metabolism
  • Prostatic Neoplasms, Castration-Resistant* / pathology
  • Pyruvate Dehydrogenase (Lipoamide)* / metabolism
  • Signal Transduction / drug effects

Substances

  • Benzamides
  • Copper
  • Androgen Antagonists
  • enzalutamide
  • Pyruvate Dehydrogenase (Lipoamide)
  • Phenylthiohydantoin
  • Nitriles
  • Glutathione