High glucose couples DJ-1 with PTEN to activate PDGFRβ for renal proximal tubular cell injury

PLoS One. 2025 Jan 6;20(1):e0311828. doi: 10.1371/journal.pone.0311828. eCollection 2025.

Abstract

High glucose milieu in diabetes induces proximal tubular epithelial cells in the kidney to undergo hypertrophy and matrix protein expansion via Akt/mTORC1 signaling, leading to renal fibrosis. The familial Parkinson's disease protein DJ-1 acts as a driver of Ras-dependent tumorigenesis and protects dopaminergic neurons from apoptosis. But its function and mechanistic basis to regulate renal fibrosis is not clear. Here, we identify DJ-1 as a high glucose-promoted protein in renal proximal tubular epithelial cells. Mechanistic interrogation revealed that DJ-1 formed complex with the lipid phosphatase PTEN in high glucose-stimulated cells, resulting in phosphorylation/activation of Akt and mTORC1. siRNAs against DJ-1 decreased high glucose-stimulated Akt/mTORC1 activation. In contrast, overexpression of DJ-1 mimicked all effects of high glucose. Interestingly, inhibition of DJ-1 blocked high glucose-induced hypertrophy of proximal tubular epithelial cells and, matrix proteins fibronectin and collagen I (α2) expression while overexpression of DJ-1 mimicked the high glucose effects on these phenomena. Previously, we reported a role of PDGFRβ in proximal tubular cell injury. In exploring the mechanism of DJ-1 function, we found that siDJ-1 inhibited high glucose-induced activating and PI 3 kinase docking site tyrosine phosphorylation of PDGF receptor-β (PDGFRβ) to block phosphorylation of PI 3 kinase. Interestingly, overexpression of PTEN mimicked these effects of siDJ-1. Together, our results reveal an important role of DJ-1-PTEN nodal point for PDGFRβ activation during high glucose-induced proximal tubular epithelial cell injury.

MeSH terms

  • Animals
  • Cell Line
  • Epithelial Cells / metabolism
  • Epithelial Cells / pathology
  • Glucose* / metabolism
  • Glucose* / pharmacology
  • Humans
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Kidney Tubules, Proximal* / metabolism
  • Kidney Tubules, Proximal* / pathology
  • Mechanistic Target of Rapamycin Complex 1 / metabolism
  • Multiprotein Complexes / metabolism
  • Oncogene Proteins / genetics
  • Oncogene Proteins / metabolism
  • PTEN Phosphohydrolase* / genetics
  • PTEN Phosphohydrolase* / metabolism
  • Phosphorylation
  • Protein Deglycase DJ-1* / genetics
  • Protein Deglycase DJ-1* / metabolism
  • Proto-Oncogene Proteins c-akt / metabolism
  • Receptor, Platelet-Derived Growth Factor beta* / genetics
  • Receptor, Platelet-Derived Growth Factor beta* / metabolism
  • Signal Transduction
  • TOR Serine-Threonine Kinases / metabolism

Substances

  • PTEN Phosphohydrolase
  • Protein Deglycase DJ-1
  • Glucose
  • Receptor, Platelet-Derived Growth Factor beta
  • Proto-Oncogene Proteins c-akt
  • Mechanistic Target of Rapamycin Complex 1
  • PTEN protein, human
  • TOR Serine-Threonine Kinases
  • Multiprotein Complexes
  • PARK7 protein, human
  • Oncogene Proteins
  • PDGFRB protein, human
  • Intracellular Signaling Peptides and Proteins

Grants and funding

This work was supported by the Department of Veterans Affairs Biomedical Laboratory Research and Development Service Merit Review Award 2I01 BX000926 to GGC. GGC is a recipient of Research Career Scientist Award IK6 BX005795 from the Department of Veterans Affairs Biomedical Laboratory Research and Development Service. The funders had no role in study design, data collection and analysis, decision to publish or preparation of manuscript.