Evidence map›Paper›PMID 26975317›Full record

ArticleNeurochemical research2016

Expression of Tyrosine Hydroxylase is Negatively Regulated Via Prion Protein.

Marcio Henrique Mello da Luz, Isaias Glezer, Andre Machado Xavier, Marcelo Alberti Paiva da Silva, Jessica Monteiro Volejnik Pino, Thiago Panaro Zamith, Taynara Fernanda Vieira, Bruno Brito Antonio, Hanna Karen Moreira Antunes, Vilma Regina Martins and 1 more

Abstract read
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In one paragraph

Article in Neurochemical research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 32% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Article
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

11 authors at 3 institutions in 1 country.

Marcio Henrique Mello da LuzDepartamento de Bioquímica, UNIFESP, Edifício de Pesquisa II, Rua Pedro de Toledo, 669, 8o andar, São Paulo, SP, CEP 04039-032, Brazil.
Isaias GlezerDepartamento de Bioquímica, UNIFESP, Edifício de Pesquisa II, Rua Pedro de Toledo, 669, 8o andar, São Paulo, SP, CEP 04039-032, Brazil.
Andre Machado XavierDepartamento de Bioquímica, UNIFESP, Edifício de Pesquisa II, Rua Pedro de Toledo, 669, 8o andar, São Paulo, SP, CEP 04039-032, Brazil.
Marcelo Alberti Paiva da SilvaDepartamento de Bioquímica, UNIFESP, Edifício de Pesquisa II, Rua Pedro de Toledo, 669, 8o andar, São Paulo, SP, CEP 04039-032, Brazil.
Jessica Monteiro Volejnik PinoDepartamento de Bioquímica, UNIFESP, Edifício de Pesquisa II, Rua Pedro de Toledo, 669, 8o andar, São Paulo, SP, CEP 04039-032, Brazil.
Thiago Panaro ZamithDepartamento de Bioquímica, UNIFESP, Edifício de Pesquisa II, Rua Pedro de Toledo, 669, 8o andar, São Paulo, SP, CEP 04039-032, Brazil.
Taynara Fernanda VieiraDepartamento de Bioquímica, UNIFESP, Edifício de Pesquisa II, Rua Pedro de Toledo, 669, 8o andar, São Paulo, SP, CEP 04039-032, Brazil.
Bruno Brito AntonioDepartamento de Psicobiologia, UNIFESP, São Paulo, SP, Brazil.
Hanna Karen Moreira AntunesDepartamento de Biociência, UNIFESP, São Paulo, SP, Brazil.
Vilma Regina MartinsAC Camargo Cancer Center, São Paulo, SP, Brazil.
Kil Sun LeeDepartamento de Bioquímica, UNIFESP, Edifício de Pesquisa II, Rua Pedro de Toledo, 669, 8o andar, São Paulo, SP, CEP 04039-032, Brazil. kslee@unifesp.br.ORCID http://orcid.org/0000-0002-2390-2774
Universidade Federal de São Paulo · BRAC Camargo Hospital · BRFundação de Apoio à Universidade Federal de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular prion protein (PrP(C)) is a glycoprotein of the plasma membrane that plays pleiotropic functions by interacting with multiple signaling complexes at the cell surface. Recently, a number of studies have reported the involvement of PrP(C) in dopamine metabolism and signaling, including its interactions with tyrosine hydroxylase (TH) and dopamine receptors. However, the outcomes reported by independent studies are still debatable. Therefore in this study, we investigated the effects of PrP(C) on the TH expression during the differentiation of N2a cells with dibutyryl-cAMP, a well-known cAMP analog that activates TH transcription. Upon differentiation, TH was induced with concomitant reduction of PrP(C) at protein level, but not at mRNA level. shRNA-mediated PrP(C) reduction increased the basal level of TH at both mRNA and protein levels without dibutyryl-cAMP treatment. This phenotype was reversed by re-expression of PrP(C). PrP(C) knockdown also potentiated the effect of dibutyryl-cAMP on TH expression. Our findings suggest that PrP(C) has suppressive effects on TH expression. As a consequence, altered PrP(C) functions may affect the regulation of dopamine metabolism and related neurological disorders.

Indexed as

Gene Expression Regulation, EnzymologicAnimalsCell DifferentiationCell Line, TumorDopamineMicePrPC ProteinsTyrosine 3-MonooxygenaseDopaminePrPC ProteinsTyrosine 3-MonooxygenaseCellular prion proteinDopamine metabolismGene expressionTyrosine hydroxylase

Identifiers

PMID26975317
OpenAlexW2296829484

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.