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August 28, 2026Journal of Cell Communication and SignalingOpen Access

FOXO6 inhibits SMURF2‐mediated ubiquitination and degradation of NR4A1 to promote retinal pigment epithelial cell ferroptosis in diabetic retinopathy

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Authors

QCQiao ChenBSBo SuKXKe Xu

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Overview

Preclinical study reveals FOXO6 drives retinal epithelial ferroptosis via SMURF2 and NR4A1 in diabetic retinopathy models, indicating a therapeutic pathway to prevent vision loss.

Key Points

  • To investigate the upstream regulatory mechanisms controlling retinal pigment epithelial cell ferroptosis under hyperglycemic conditions in diabetic retinopathy.
  • Examined high glucose-treated human ARPE-19 cells and a diabetic mouse model.
  • Assessed ferroptosis, iron accumulation, and lipid peroxidation using biochemical assays, Western blotting, fluorescence probes, and histological staining.
  • Evaluated molecular interactions and transcriptional regulation via co-immunoprecipitation, GST pull-down, chromatin immunoprecipitation, and luciferase reporter assays.
  • High glucose upregulated NR4A1 in ARPE-19 cells, whereas NR4A1 knockdown reduced iron accumulation, lipid peroxidation, and ferroptosis markers.
  • SMURF2 directly bound NR4A1 to promote its ubiquitination and degradation, while high glucose-induced FOXO6 repressed SMURF2 transcription.
  • SMURF2 overexpression mitigated high glucose-induced ARPE-19 ferroptosis and mouse retinal injury, which was reversed by NR4A1 co-overexpression or SMURF2 knockdown.

Cite This Study

Chen et al. (2026) studied this question.

synapsesocial.com/papers/6a91467bd15324a1df3aa1d4https://doi.org/10.1002/ccs3.70108
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