Evidence map›Paper›PMID 19756365›Full record

ArticleJournal of neural transmission (Vienna, Austria : 1996)2009

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

Ichiro Kawahata, Hirofumi Tokuoka, Hasan Parvez, Hiroshi Ichinose

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of neural transmission (Vienna, Austria : 1996), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.7field-weighted citation impact, top 31% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. T-Type CaInternational journal of molecular sciences · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. Fatty Acid-Binding Protein 3 is Critical for α-Synuclein Uptake and MPPInternational journal of molecular sciences · 2019
    Article
  11. Human tyrosine hydroxylase in Parkinson's disease and in related disorders.Journal of neural transmission (Vienna, Austria : 1996) · 2019
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Complex molecular regulation of tyrosine hydroxylase.Journal of neural transmission (Vienna, Austria : 1996) · 2014
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Ichiro KawahataGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259-B7, Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan.
Hirofumi Tokuoka
Hasan Parvez
Hiroshi Ichinose
Tokyo Institute of Technology · JPCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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, or MG-132 in NGF-differentiated PC12D cells induced dot-like immunoreactivities with the anti-(40)Ser-phosphorylated TH (p40-TH) antibody. These dots were tightly co-localized with ubiquitin and positive to Thioflavine-S staining. These dot-like immunoreactivities were not obvious when immunostaining was performed against total-TH or choline acetyltransferase. Western blotting analysis showed time-dependent increase of p40-TH in the Triton-insoluble fractions. We also examined the effect of okadaic acid, an inhibitor of protein phosphatase 2A, which is a phosphatase acting on p40-TH. Okadaic acid increased the amount of insoluble p40-TH. These data suggest that p40-TH is prone to be insolubilized and aggregated by dysfunction of an ubiquitin-proteasome system in PC12D cells.

Indexed as

AnimalsCholine O-AcetyltransferaseCysteine Proteinase InhibitorsEnzyme InhibitorsLeupeptinsNeuronsOkadaic AcidOligopeptidesPC12 CellsPhosphorylationProteasome Endopeptidase ComplexProteasome InhibitorsProtein MultimerizationProtein Phosphatase 2RatsTime FactorsATP dependent 26S proteasebenzyloxycarbonyl-isoleucyl-glutamyl(O-tert-butyl)-alanyl-leucinalbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCholine O-AcetyltransferaseCysteine Proteinase InhibitorsEnzyme InhibitorsLeupeptinsOkadaic AcidOligopeptidesProteasome Endopeptidase ComplexProteasome InhibitorsProtein Phosphatase 2Tyrosine 3-MonooxygenaseUbiquitin

Identifiers

PMID19756365
OpenAlexW2013120967

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.