Accumulation of phosphorylated tyrosine hydroxylase into insoluble protein aggregates by inhibition of an ubiquitin–proteasome system in PC12D cells

@article{Kawahata2009AccumulationOP,
  title={Accumulation of phosphorylated tyrosine hydroxylase into insoluble protein aggregates by inhibition of an ubiquitin–proteasome system in PC12D cells},
  author={Ichiro Kawahata and Hirofumi Tokuoka and H M Shahriar Parvez and Hiroshi Ichinose},
  journal={Journal of Neural Transmission},
  year={2009},
  volume={116},
  pages={1571-1578}
}
Tyrosine hydroxylase (TH) is a rate-limiting enzyme for the biosynthesis of catecholamines including dopamine. The relationship between proteasomal dysfunction and the etiology of Parkinson’s disease has been suggested, but it is unknown if TH protein is affected by proteasomal dysfunctions. Here, we examined the effect of inhibition of ubiquitin–proteasomal pathway on biochemical characteristics of TH protein in the neuronal cells. Inhibition of 20S or 26S proteasome by proteasome inhibitor I… CONTINUE READING
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Immunohistochemical analyses of human brain-stem type Lewy bodies and the localization of phosphorylated tyrosine hydroxylase in the midbrain

  • I Kawahata, S Yagishita, K Hasegawa, I Natatsu, T Nagatsu, H Ichinose
  • Biogenic Amines
  • 2009
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