Evidence map›Paper›PMID 24561157›Full record

ArticleBiochimica et biophysica acta2014

Number and Brightness analysis of alpha-synuclein oligomerization and the associated mitochondrial morphology alterations in live cells.

N Plotegher, E Gratton, L Bubacco

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
–field-weighted citation impact
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

45 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. α-Synuclein and biological membranes: the danger of loving too much.Chemical communications (Cambridge, England) · 2023
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. PGC-1s in the Spotlight with Parkinson's Disease.International journal of molecular sciences · 2021
    Review
  19. Article
  20. 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

3 authors.

N PlotegherDepartment of Biology, University of Padova, Italy.
E GrattonLaboratory for Fluorescence Dynamics, Department of Biomedical Engineering, University of California, Irvine, USA.
L BubaccoDepartment of Biology, University of Padova, Italy. Electronic address: luigi.bubacco@unipd.it.

Funding

Uncover Strategies Used By Biological SystemsP50GM076516 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI LANDER, ARTHUR D · 2007 to 2016
$25.1M
YEAST RIBOSOMAL STALK COMPOSITION IN VIVO BY TWO-PHOTON FCS AND PCH ANALYSISP41RR003155 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GRATTON, ENRICO · 1986 to 2011
$14.9M
TRD4: Phasor analysisP41GM103540 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI GRATTON, ENRICO · 2012 to 2020
$12.5M
NCRR NIH HHS P41 RR003155NCRR NIH HHS P41-RR03155NIGMS NIH HHS P41 GM103540NIGMS NIH HHS P50 GM076516NIGMS NIH HHS P50-GM076516
6 · The paper itself

Abstract

backgroundAlpha-synuclein oligomerization is associated to Parkinson's disease etiopathogenesis. The study of alpha-synuclein oligomerization properties in live cell and the definition of their effects on cellular viability are among fields expected to provide the knowledge required to unravel the mechanism(s) of toxicity that lead to the disease.

methodsWe used Number and Brightness method, which is a method based on fluorescence fluctuation analysis, to monitor alpha-synuclein tagged with EGFP aggregation in living SH-SY5Y cells. The presence of alpha-synuclein oligomers detected with this method was associated with intracellular structure conditions, evaluated by fluorescence confocal imaging.

resultsCells overexpressing alpha-synuclein-EGFP present a heterogeneous ensemble of oligomers constituted by less than 10 monomers, when the protein approaches a threshold concentration value of about 90nM in the cell cytoplasm. We show that the oligomeric species are partially sequestered by lysosomes and that the mitochondria morphology is altered in cells presenting oligomers, suggesting that these mitochondria may be dysfunctional.

conclusionsWe showed that alpha-synuclein overexpression in SH-SY5Y causes the formation of alpha-synuclein oligomeric species, whose presence is associated with mitochondrial fragmentation and autophagic-lysosomal pathway activation in live cells. GENERAL SIGNIFICANCE: The unique capability provided by the Number and Brightness analysis to study alpha-synuclein oligomer distribution and properties, and the study of their association to intracellular components in single live cells is important to forward our understanding of the molecular mechanisms of Parkinson's disease and it may be of general significance when applied to the study of other aggregating proteins in cellular models.

Indexed as

Protein Multimerizationalpha-SynucleinCalibrationCell Line, TumorCell SurvivalHumansLysosomesMitochondriaalpha-SynucleinFluorescenceLive imagingLysosomesOligomersParkinson's diseaseProtein aggregation

Identifiers

PMID24561157
PMCPMC4088272

What OpenQuestion holds

Textmetadata
LicenceTDM
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.