The role of tissue transglutaminase in 1-methyl-4-phenylpyridinium (MPP+)-induced toxicity in differentiated human SH-SY5Y neuroblastoma cells

Katy E. Beck, Luigi A. De Girolamo, Martin Griffin, E. Ellen Billett

Research output: Contribution to journalArticlepeer-review

Abstract

Tissue transglutaminase (TG2) can induce post-translational modification of proteins, resulting in protein cross-linking or incorporation of polyamines into substrates, and can also function as a signal transducing G protein. The role of TG2 in the formation of insoluble cross-links has led to its implication in some neurodegenerative conditions. Exposure of pre-differentiated SH-SY5Y cells to the Parkinsonian neurotoxin 1-methyl-4-phenylpyridinium ion (MPP+) resulted in significant dose-dependent reductions in TG2 protein levels, measured by probing Western blots with a TG2-specific antibody. Transglutaminase (TG) transamidating activity, on the other hand, monitored by incorporation of a polyamine pseudo-substrate into cellular proteins, was increased. Inhibitors of TG (putrescine) and TG2 (R283) exacerbated MPP+ toxicity, suggesting that activation of TG2 may promote a survival response in this toxicity paradigm.
Original languageEnglish
Pages (from-to)46-51
Number of pages6
JournalNeuroscience Letters
Volume405
Issue number1-2
DOIs
Publication statusPublished - 11 Sep 2006

Keywords

  • Parkinson's disease
  • MPP+
  • tissue transglutaminase
  • SH-SY5Y human neuroblastoma
  • cell viability

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