Modulation of proteasome activity by vitamin E in THP-1 monocytes

Adelina Munteanu, Roberta Ricciarelli, Sara Massone, Jean Marc Zingg

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


In THP-1 monocytes, cellular proteasome inhibition by ritonavir or ALLN is associated with increased production of oxidative stress. Both compounds produced comparable amounts of oxidative stress; however, normalization by α-tocopherol occurred solely after inhibition by ritonavir, and not by ALLN. Similar to that, α-tocopherol could normalize the reduced formation of 3-nitrotyrosine-modified proteins only after ritonavir treatment. In the absence of any proteasome inhibitor, intrinsic cellular proteasome activity was not modulated by α-, β-, and γ-tocopherols; however, δ-tocopherol, α-tocotrienol, and α-tocopheryl phosphate could significantly inhibit cellular proteasome activity and increased the level of p27Kip1 and p53. Since oxidative stress was reduced by α-tocopherol only after proteasome inhibition by ritonavir and not by ALLN, it is concluded that, in this experimental system, α-tocopherol does not act as an antioxidant but interferes with the inhibitory effect of ritonavir.

Original languageEnglish (US)
Pages (from-to)771-780
Number of pages10
JournalIUBMB life
Issue number12
StatePublished - Oct 27 2007
Externally publishedYes


  • 3-nitrotyrosine
  • ALLN
  • Atherosclerosis
  • CD36
  • Oxidative stress
  • Proliferation
  • Proteasome
  • Ritonavir
  • Scavenger receptors

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology


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