Evidence map›Paper›PMID 27853822›Full record

ArticleEuropean biophysics journal : EBJ2017

Endogenously generated amyloid-β increases stiffness in human neuroblastoma cells.

Zhuoyang Lu, Hua Li, Chen Hou, Yunhua Peng, Jiangang Long, Jiankang Liu

Abstract read
PubMed Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.2field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. Frontiers in cell and developmental biology · 2022
    Article
  4. Article
  5. 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

6 authors at 1 institution in 1 country.

Zhuoyang LuThe Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China.
Hua LiThe Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China.
Chen HouThe Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China.
Yunhua PengThe Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China.
Jiangang LongThe Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China. jglong@mail.xjtu.edu.cn.
Jiankang LiuThe Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China. j.liu@mail.xjtu.edu.cn.
Xi'an Jiaotong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid-β (Aβ) is widely recognized as toxic to neuronal cells. Its deposition on plasma and intracellular membranes and aggregation into amyloid plaques can disturb the composition and physiological function of neurons. Whether a physical property of cells, such as stiffness, is altered by endogenously overexpressed Aβ has not yet been investigated. In this study, we used human neuroblastoma cells stably overexpressing amyloid precursor protein (APP) and its Swedish mutant form (APPswe) to measure the changes in cell stiffness. Our results showed that the stiffness of cells overexpressing APP or APPswe was higher than that of control SH-SY5Y cells. Either reducing levels of Aβ with the γ secretase inhibitor DAPT or blocking the membrane calcium channel formed by Aβ with tromethamine decreased cell stiffness to a level close to the control SH-SY5Y cells. Our results suggested that Aβ, not APP, contributed to increased cell stiffness and that closure of calcium channels formed by Aβ can alleviate the effects of Aβ on membrane stiffness.

Indexed as

Mechanical PhenomenaAmyloid beta-PeptidesBiomechanical PhenomenaCell Line, TumorHumansNeuroblastomaPeptide FragmentsAmyloid beta-Peptidesamyloid beta-protein (1-40)Peptide FragmentsAlzheimer’s diseaseAmyloid-βAtomic force microscopyHuman neuroblastoma cellsStiffness

Identifiers

PMID27853822
OpenAlexW2549969944

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.