Quantitative proteome analysis of the 20S proteasome of apoptotic Jurkat T cells Academic Article Article uri icon

Overview

MeSH Major

  • Cell Transformation, Viral
  • Oncogenes
  • Receptors, Cell Surface

abstract

  • Regulated proteolysis plays important roles in cell biology and pathological conditions. A crosstalk exists between apoptosis and the ubiquitin-proteasome system, two pathways responsible for regulated proteolysis executed by different proteases. To investigate whether the apoptotic process also affects the 20S proteasome, we performed three independent SILAC-based quantitative proteome approaches: 1-DE/MALDI-MS, small 2-DE/MALDI-MS and large 2-DE/nano-LC-ESI-MS. Taking the results of all experiments together, no quantitative changes were observed for the α- and β-subunits of the 20S proteasome except for subunit α7. This protein was identified in two protein spots with a down-regulation of the more acidic protein species (α7a) and up-regulation of the more basic protein species (α7b) during apoptosis. The difference in these two α7 protein species could be attributed to oxidation of cysteine-41 to cysteine sulfonic acid and phosphorylation at serine-250 near the C terminus in α7a, whereas these modifications were missing in α7b. These results pointed to the biological significance of posttranslational modifications of proteasome subunit α7 after induction of apoptosis.© 2010 Springer-Verlag.

publication date

  • July 2011

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1007/s00726-010-0575-6

PubMed ID

  • 20364280

Additional Document Info

start page

  • 351

end page

  • 361

volume

  • 41

number

  • 2