Evidence map›Paper›PMID 33670800›Full record

ArticleInternational journal of molecular sciences2021

Copper Dependent Modulation of α-Synuclein Phosphorylation in Differentiated SHSY5Y Neuroblastoma Cells.

Marco Greco, Chiara Carmela Spinelli, Lidia De Riccardis, Alessandro Buccolieri, Simona Di Giulio, Debora Musarò, Claudia Pagano, Daniela Manno, Michele Maffia

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. 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

9 authors at 1 institution in 1 country.

Marco GrecoDepartment of Mathematics and Physics "E. De Giorgi", University of Salento, 73100 Lecce, Italy.
Chiara Carmela SpinelliDepartment of Biological and Environmental Science and Technology, University of Salento, 73100 Lecce, Italy.ORCID 0000-0003-4948-5814
Lidia De RiccardisDepartment of Biological and Environmental Science and Technology, University of Salento, 73100 Lecce, Italy.
Alessandro BuccolieriDepartment of Biological and Environmental Science and Technology, University of Salento, 73100 Lecce, Italy.ORCID 0000-0002-8657-9468
Simona Di GiulioDepartment of Biological and Environmental Science and Technology, University of Salento, 73100 Lecce, Italy.
Debora MusaròDepartment of Biological and Environmental Science and Technology, University of Salento, 73100 Lecce, Italy.
Claudia PaganoDepartment of Biological and Environmental Science and Technology, University of Salento, 73100 Lecce, Italy.
Daniela MannoDepartment of Mathematics and Physics "E. De Giorgi", University of Salento, 73100 Lecce, Italy.ORCID 0000-0002-5843-8772
Michele MaffiaDepartment of Biological and Environmental Science and Technology, University of Salento, 73100 Lecce, Italy.ORCID 0000-0003-0665-4534
University of Salento · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Copper (Cu) dyshomeostasis plays a pivotal role in several neuropathologies, such as Parkinson's disease (PD). Metal accumulation in the central nervous system (CNS) could result in loss-of-function of proteins involved in Cu metabolism and redox cycling, generating reactive oxygen species (ROS). Moreover, neurodegenerative disorders imply the presence of an excess of misfolded proteins known to lead to neuronal damage. In PD, Cu accumulates in the brain, binds α-synuclein, and initiates its aggregation. We assessed the correlation between neuronal differentiation, Cu homeostasis regulation, and α-synuclein phosphorylation. At this purpose, we used differentiated SHSY5Y neuroblastoma cells to reproduce some of the characteristics of the dopaminergic neurons. Here, we reported that differentiated cells expressed a significantly higher amount of a copper transporter protein 1 (CTR1), increasing the copper uptake. Cells also showed a significantly more phosphorylated form of α-synuclein, further increased by copper treatment, without modifications in α-synuclein levels. This effect depended on the upregulation of the polo-like kinase 2 (PLK2), whereas the levels of the relative protein phosphatase 2A (PP2A) remained unvaried. No changes in the oxidative state of the cells were identified. The Cu dependent alteration of α-synuclein phosphorylation pattern might potentially offer new opportunities for clinical intervention.

Indexed as

alpha-SynucleinCell DifferentiationCell Line, TumorCell SurvivalCopperCopper-Transporting ATPasesCopper Transport ProteinsHumansMolecular ChaperonesNeuroblastomaPhosphorylationProtein Serine-Threonine Kinasesalpha-SynucleinATOX1 protein, humanATP7A protein, humanCopperCopper-Transporting ATPasesCopper Transport ProteinsMolecular ChaperonesPLK2 protein, humanProtein Serine-Threonine Kinasescopperoxidative stressParkinson’s disease (PD)ROSα-synuclein

Identifiers

PMID33670800
PMCPMC7922547
OpenAlexW3133117543

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.