Evidence map›Paper›PMID 31947546›Full record

ArticleBiomolecules2020

Apolipoprotein E Interferes with IAPP Aggregation and Protects Pericytes from IAPP-Induced Toxicity.

Anna L Gharibyan, Tohidul Islam, Nina Pettersson, Solmaz A Golchin, Johanna Lundgren, Gabriella Johansson, Mélany Genot, Nina Schultz, Malin Wennström, Anders Olofsson

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. 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
1.7field-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, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Role of the Pancreatic Islet Microvasculature in Health and Disease.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
    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

10 authors at 2 institutions in 1 country.

Anna L GharibyanDepartment of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå, Sweden.
Tohidul IslamDepartment of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå, Sweden.
Nina PetterssonDepartment of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå, Sweden.
Solmaz A GolchinDepartment of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå, Sweden.
Johanna LundgrenDepartment of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå, Sweden.
Gabriella JohanssonDepartment of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå, Sweden.
Mélany GenotDepartment of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå, Sweden.
Nina SchultzClinical Memory Research Unit, Department of Clinical Sciences Malmö, Lund University, 21428 Malmö, Sweden.
Malin WennströmClinical Memory Research Unit, Department of Clinical Sciences Malmö, Lund University, 21428 Malmö, Sweden.
Anders OlofssonDepartment of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå, Sweden.
Umeå University · SELund University · SE

Funding

Åhlén-stiftelsen 193061Demensfonden 2019FAMY-Norrbotten 03/2019Hjärnfonden FO2018-0334Insamlingsstiftelsen at Umeå University FS 2.1.6-2396-18Stiftelsen Gamla Tjänarinnor 2018-00718Stiftelsen Olle Engkvist Byggmästare 199-0469
6 · The paper itself

Abstract

Apolipoprotein E (ApoE) has become a primary focus of research after the discovery of its strong linkage to Alzheimer's disease (AD), where the ApoE4 variant is the highest genetic risk factor for this disease. ApoE is commonly found in amyloid deposits of different origins, and its interaction with amyloid-β peptide (Aβ), the hallmark of AD, is well known. However, studies on the interaction of ApoEs with other amyloid-forming proteins are limited. Islet amyloid polypeptide (IAPP) is an amyloid-forming peptide linked to the development of type-2 diabetes and has also been shown to be involved in AD pathology and vascular dementia. Here we studied the impact of ApoE on IAPP aggregation and IAPP-induced toxicity on blood vessel pericytes. Using both in vitro and cell-based assays, we show that ApoE efficiently inhibits the amyloid formation of IAPP at highly substoichiometric ratios and that it interferes with both nucleation and elongation. We also show that ApoE protects the pericytes against IAPP-induced toxicity, however, the ApoE4 variant displays the weakest protective potential. Taken together, our results suggest that ApoE has a generic amyloid-interfering property and can be protective against amyloid-induced cytotoxicity, but there is a loss of function for the ApoE4 variant.

Indexed as

Alzheimer DiseaseAmyloidApolipoprotein E4Apolipoproteins ECell LineDiabetes Mellitus, Type 2HumansIslet Amyloid PolypeptidePericytesProtein AggregatesProtein Aggregation, PathologicalAmyloidApolipoprotein E4Apolipoproteins EIslet Amyloid PolypeptideProtein Aggregatesapolipoprotein EcytotoxicityIAPP amyloidpericytesThioflavin T

Identifiers

PMID31947546
PMCPMC7022431
OpenAlexW3000133363

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.