Protien expression profiling of mouse thymoma upon exposure to the tricothecene deoxynivalenol (DON) Implications for its mechanism of action

A.M. Osman, J.L.A. Pennings, M.H. Blokland, A.A.C.M. Peijnenburg, H. van Loveren

    Research output: Contribution to journalArticleAcademicpeer-review

    16 Citations (Scopus)

    Abstract

    The objective of this work was to investigate whether proteomic analysis of thymoma cells treated with the trichothecene deoxynivalenol (DON) as compared to non-treated (control) cells would reveal differential protein expression, and thus would contribute to a better understanding of the mechanisms of its toxicity. For that purpose the mouse thymoma cell line EL4 was exposed to 0.5 microM DON for 6 hr. A total of 30 proteins were affected after exposure of EL4 cells to DON. Most of these proteins were up-regulated and included key metabolic enzymes (e.g., fatty acid synthase, aldose reductase, carbamoyl phosphate synthetase, glucose-6-phosphate isomerase), chaperones (e.g., HSP9AB1 and HSP70), enzymes implicated in protein folding (PDI and ERO1-l alpha), and proteins involved in protein degradation (ubiquitin-conjugating enzyme (E1) and proteasome subunit alpha type-1). In addition, an IgE-binding protein with a molecular weight of 60 kDa and My-binding protein 1a (MYBBP1A), a transcription factor, were found to be up-regulated by DON. The observed up-regulation of MYBBP1A, a known repressor of a number of transcription factors such as PGC-1 alpha, C-myb, and p65 of the NF-kappaB family, suggests that this protein might play a role in the mechanism of DON toxicity.
    Original languageEnglish
    Pages (from-to)147-156
    JournalJournal of Immunotoxicology
    Volume7
    Issue number3
    DOIs
    Publication statusPublished - 2010

    Keywords

    • ribotoxic stress-response
    • myb-binding-protein
    • gene-expression
    • vomitoxin deoxynivalenol
    • proteomic analysis
    • induced apoptosis
    • immune-response
    • cdna-clones
    • activation
    • kinase

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