Effects of proteasome inhibitors on rat renal fibrosis in vitro and in vivo

Nephrology (Carlton). 2011 Jan;16(1):76-86. doi: 10.1111/j.1440-1797.2010.01367.x.

Abstract

Aim: Transforming growth factor-β (TGF-β) is involved in renal tubulointerstitial fibrosis. Recently, the ubiquitin proteasome system was shown to participate in the TGF-β signalling pathway. The aim of this study was to examine the effects of proteasome inhibitors on TGF-β-induced transformation of renal fibroblasts and tubular epithelial cells in vitro and on unilateral ureteral obstruction (UUO) in vivo.

Methods: Rat renal fibroblasts NRK-49F cells and tubular epithelial cells, NRK-52E, were treated with TGF-β in the presence or absence of a proteasome inhibitor, MG132 or lactacystin. Rats were subjected to UUO and received MG132 i.p. for 7 days.

Results: In cultured renal cells, both MG132 and lactacystin inhibited TGF-β-induced α-smooth muscle actin (α-SMA) protein expression according to both western blotting and immunofluorescent study results. MG132 also suppressed TGF-β-induced mRNA expression of α-SMA and upregulation of Smad-response element reporter activity. However, MG132 did not inhibit TGF-β-induced phosphorylation and nuclear translocation of Smad2. In contrast, MG132 increased the protein level of Smad co-repressor SnoN, demonstrating that SnoN is one of the target molecules by which MG132 blocks the TGF-β signalling pathway. Although the proteasome inhibitor suppressed TGF-β-induced transformation of cultured fibroblasts and tubular epithelial cells, MG132 treatment did not ameliorate tubulointerstitial fibrosis in the rat UUO model.

Conclusion: Proteasome inhibitors attenuate TGF-β signalling by blocking Smad signal transduction in vitro, but do not inhibit renal interstitial fibrosis in vivo.

MeSH terms

  • Acetylcysteine / analogs & derivatives
  • Acetylcysteine / pharmacology
  • Actins / genetics
  • Actins / metabolism
  • Animals
  • Cells, Cultured
  • Cysteine Proteinase Inhibitors / pharmacology*
  • Disease Models, Animal
  • Epithelial Cells / cytology
  • Epithelial Cells / metabolism
  • Epithelial-Mesenchymal Transition / drug effects
  • Fibroblasts / cytology
  • Fibroblasts / metabolism
  • Fibrosis / genetics
  • Fibrosis / metabolism*
  • Kidney Diseases / metabolism*
  • Kidney Diseases / pathology
  • Leupeptins / pharmacology
  • Male
  • Nerve Tissue Proteins / metabolism
  • RNA, Messenger / metabolism*
  • Rats
  • Rats, Wistar
  • Signal Transduction / drug effects*
  • Signal Transduction / genetics
  • Smad Proteins, Receptor-Regulated / metabolism
  • Smad2 Protein / metabolism
  • Smad3 Protein / metabolism
  • Smad4 Protein / metabolism
  • Transcription Factors / metabolism
  • Transcription, Genetic / drug effects
  • Transforming Growth Factor beta / drug effects
  • Transforming Growth Factor beta / metabolism*
  • Ureteral Obstruction / metabolism
  • Ureteral Obstruction / pathology

Substances

  • Actins
  • Cysteine Proteinase Inhibitors
  • Leupeptins
  • Nerve Tissue Proteins
  • RNA, Messenger
  • Skil_v1 protein, rat
  • Smad Proteins, Receptor-Regulated
  • Smad2 Protein
  • Smad2 protein, rat
  • Smad3 Protein
  • Smad3 protein, rat
  • Smad4 Protein
  • Smad4 protein, rat
  • Transcription Factors
  • Transforming Growth Factor beta
  • smooth muscle actin, rat
  • lactacystin
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde
  • Acetylcysteine