Proteomic analysis of ubiquitin-proteasome effects: insight into the function of eukaryotic initiation factor 5A

Oncogene. 2003 Jul 31;22(31):4819-30. doi: 10.1038/sj.onc.1206738.

Abstract

The global effect of ubiquitin-proteasome (UP) inhibitors on leukemic cell proteome was analysed. A total of 39 protein spots, affected by UP inhibitors, were identified, including 11 new apoptosis-associated proteins. They are involved in different cellular functions and four were associated with caspase-3 activation. Eukaryotic initiation factor 5A (eIF-5A) was identified in two spots; however, the peptide mass-fingerprinting for the accumulated one included a peptide with lysine50, indicating that hypusine formation was suppressed during UP inhibitor-induced apoptosis. Hypusine modification ensues immediately following translation of eIF-5A precursor, unless cells are treated with the modification inhibitors diaminoheptane. However, UP inhibitors induced a much stronger accumulation of unmodified eIF-5A compared to the effect of diaminoheptane. We further showed the unmodified eIF-5A was regulated in a proteasome-dependent manner. Inhibition of hypusine formation by diaminoheptane triggered apoptosis, but of particular interest is the finding that eIF-5A expression inhibition by antisense oligodeoxynucleotides significantly enhanced the stimulating effect of GM-CSF on cell growth. Therefore, the eIF-5A accumulation played important roles in the apoptosis induced by UP inhibitors. Moreover, hypusine inhibition in apoptosis was further revealed to be associated with the subcellular localization of eIF-5A. Our data pave the way to a better understanding of the mechanisms by which UP system has been linked to apoptosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcysteine / analogs & derivatives*
  • Acetylcysteine / pharmacology*
  • Apoptosis / drug effects
  • Apoptosis / genetics
  • Caspase 3
  • Caspases / metabolism
  • Cysteine Endopeptidases / physiology*
  • Diamines / pharmacology
  • Electrophoresis, Gel, Two-Dimensional
  • Enzyme Activation
  • Eukaryotic Translation Initiation Factor 5A
  • Gene Expression Profiling*
  • Gene Expression Regulation / drug effects*
  • Granulocyte-Macrophage Colony-Stimulating Factor / pharmacology
  • Humans
  • Leukemia, Megakaryoblastic, Acute / pathology
  • Leupeptins / pharmacology*
  • Lysine / analogs & derivatives*
  • Lysine / metabolism
  • Multienzyme Complexes / antagonists & inhibitors
  • Multienzyme Complexes / physiology*
  • Oligodeoxyribonucleotides, Antisense / pharmacology
  • Peptide Initiation Factors / genetics
  • Peptide Initiation Factors / physiology*
  • Peptide Mapping
  • Protease Inhibitors / pharmacology*
  • Proteasome Endopeptidase Complex
  • Proteomics
  • RNA-Binding Proteins*
  • Spectrometry, Mass, Electrospray Ionization
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Subcellular Fractions / chemistry
  • Tumor Cells, Cultured / drug effects
  • Tumor Cells, Cultured / metabolism
  • Ubiquitin / physiology*

Substances

  • Diamines
  • Leupeptins
  • Multienzyme Complexes
  • Oligodeoxyribonucleotides, Antisense
  • Peptide Initiation Factors
  • Protease Inhibitors
  • RNA-Binding Proteins
  • Ubiquitin
  • lactacystin
  • hypusine
  • 1,7-diaminoheptane
  • Granulocyte-Macrophage Colony-Stimulating Factor
  • CASP3 protein, human
  • Caspase 3
  • Caspases
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex
  • Lysine
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde
  • Acetylcysteine