Evidence map›Paper›PMID 23332070›Full record

ArticleBiophysical journal2013

Cations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP.

Michele F M Sciacca, Danilo Milardi, Grazia M L Messina, Giovanni Marletta, Jeffrey R Brender, Ayyalusamy Ramamoorthy, Carmelo La Rosa

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 111 citations in OpenAlex.

  1. Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Impact of CaBiochimica et biophysica acta. Biomembranes · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

7 authors at 2 institutions in 2 countries.

Michele F M SciaccaBiophysics, University of Michigan, Ann Arbor, Michigan, USA.
Danilo Milardi
Grazia M L Messina
Giovanni Marletta
Jeffrey R Brender
Ayyalusamy Ramamoorthy
Carmelo La Rosa
University of Catania · ITUniversity of Michigan–Ann Arbor · US

Funding

Membrane Interaction and Membrane Mediated Aggregation of AmylinR21DK078885 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2009 to 2010
$411k
NIDDK NIH HHS DK078885NIDDK NIH HHS R21 DK078885
6 · The paper itself

Abstract

Disruption of the integrity of the plasma membrane by amyloidogenic proteins is linked to the pathogenesis of a number of common age-related diseases. Although accumulating evidence suggests that adverse environmental stressors such as unbalanced levels of metal ions may trigger amyloid-mediated membrane damage, many features of the molecular mechanisms underlying these events are unknown. Using human islet amyloid polypeptide (hIAPP, aka amylin), an amyloidogenic peptide associated with β-cell death in type 2 diabetes, we demonstrate that the presence of Ca(2+) ions inhibits membrane damage occurring immediately after the interaction of freshly dissolved hIAPP with the membrane, but significantly enhances fiber-dependent membrane disruption. In particular, dye leakage, quartz crystal microbalance, atomic force microscopy, and NMR experiments show that Ca(2+) ions promote a shallow membrane insertion of hIAPP, which leads to the removal of lipids from the bilayer through a detergent-like mechanism triggered by fiber growth. Because both types of membrane-damage mechanisms are common to amyloid toxicity by most amyloidogenic proteins, it is likely that unregulated ion homeostasis, amyloid aggregation, and membrane disruption are all parts of a self-perpetuating cycle that fuels amyloid cytotoxicity.

Indexed as

AmyloidAnimalsCalciumCationsCell MembraneColoring AgentsDetergentsHumansHydrophobic and Hydrophilic InteractionsIslet Amyloid PolypeptideLipid BilayersMicroscopy, Atomic ForcePhosphatidylcholinesPhosphatidylglycerolsPhosphatidylserinesQuartz Crystal Microbalance Techniques1-palmitoyl-2-oleoylglycero-3-phosphoserine1-palmitoyl-2-oleoylphosphatidylcholineAmyloidCalciumCationsColoring AgentsDetergentsIslet Amyloid PolypeptideLipid BilayerslysomyristoylphosphatidylglycerolPhosphatidylcholinesPhosphatidylglycerolsPhosphatidylserines

Identifiers

PMID23332070
PMCPMC3540246
OpenAlexW2046188801

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.