Evidence map›Paper›PMID 36026506›Full record

ArticlePloS one2022

An in vitro workflow of neuron-laden agarose-laminin hydrogel for studying small molecule-induced amyloidogenic condition.

Poommaree Namchaiw, Patapon Bunreangsri, Piyaporn Eiamcharoen, Salita Eiamboonsert, Rungtiva P Poo-Arporn

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Poommaree NamchaiwBiological Engineering Program, Faculty of Engineering, King Mongkut's University of Technology Thonburi, Thung Kru, Bangkok, Thailand.ORCID 0000-0003-0275-6234
Patapon BunreangsriNeuroscience Center for Research and Innovation, Learning Institute, King Mongkut's University of Technology Thonburi, Thung Kru, Bangkok, Thailand.
Piyaporn EiamcharoenDepartment of Pathology, Faculty of Veterinary Medicine, Kasetsart University, Thung Kru, Bangkok, Thailand.ORCID 0000-0002-1947-9889
Salita EiamboonsertBiological Engineering Program, Faculty of Engineering, King Mongkut's University of Technology Thonburi, Thung Kru, Bangkok, Thailand.
Rungtiva P Poo-ArpornBiological Engineering Program, Faculty of Engineering, King Mongkut's University of Technology Thonburi, Thung Kru, Bangkok, Thailand.
King Mongkut's University of Technology Thonburi · THKasetsart University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In vitro studies have been popularly used to determine the cellular and molecular mechanisms for many decades. However, the traditional two-dimension (2D) cell culture which grows cells on a flat surface does not fully recapitulate the pathological phenotypes. Alternatively, the three-dimension (3D) cell culture provides cell-cell and cell-ECM interaction that better mimics tissue-like structure. Thus, it has gained increasing attention recently. Yet, the expenses, time-consuming, and complications of cellular and biomolecular analysis are still major limitations of 3D culture. Herein, we describe a cost-effective and simplified workflow of the 3D neuronal cell-laden agarose-laminin preparation and the isolation of cells, RNAs, and proteins from the scaffold. To study the effects of the amyloidogenic condition in neurons, we utilized a neuron-like cell line, SH-SY5Y, and induced the amyloidogenic condition by using an amyloid forty-two inducer (Aftin-4). The effectiveness of RNAs, proteins and cells isolation from 3D scaffold enables us to investigate the cellular and molecular mechanisms underlying amyloidogenic cascade in neuronal cells. The results show that SH-SY5Y cultured in agarose-laminin scaffold differentiated to a mature TUJ1-expressing neuron cell on day 7. Furthermore, the gene expression profile from the Aftin-4-induced amyloidogenic condition revealed the expression of relevant gene-encoding proteins in the amyloidogenic pathway, including APP, BACE1, PS1, and PS2. This platform could induce the amyloid-beta 42 secretion and entrap secreted proteins in the scaffold. The induction of amyloidogenic conditions in a 3D culture facilitates the interaction between secreted amyloid-beta and neurons, which makes it resembles the pathological environment in Alzheimer's brain. Together, this workflow is applicable for studying the cellular and molecular analysis of amyloid-induced neuronal toxicity, such as those occurred in Alzheimer's disease progression. Importantly, our method is cost-effective, reproducible, and easy to manipulate.

Indexed as

Alzheimer DiseaseNeuroblastomaAmyloidAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesHumansHydrogelsLamininNeuronsSepharoseWorkflowAmyloidAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesHydrogelsLamininSepharose

Identifiers

PMID36026506
PMCPMC9416999
OpenAlexW4293155689

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.