Evidence map›Paper›PMID 26121967›Full record

ArticleClinical oral investigations2016

Interaction of enamel matrix proteins with human periodontal ligament cells.

Harsh D Amin, Irwin Olsen, Jonathan Knowles, Michel Dard, Nikolaos Donos

Open access · hybridAbstract read
In one paragraph

Article in Clinical oral investigations, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.

  1. Amelogenin-Derived Peptides in Bone Regeneration: A Systematic Review.International journal of molecular sciences · 2021
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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

5 authors at 3 institutions in 3 countries.

Harsh D AminDivision of Biomaterials and Tissue Engineering, UCL Eastman Dental Institute, University College London, London, UK.
Irwin OlsenDivision of Biomaterials and Tissue Engineering, UCL Eastman Dental Institute, University College London, London, UK. i.olsen@ucl.ac.uk.
Jonathan KnowlesDivision of Biomaterials and Tissue Engineering, UCL Eastman Dental Institute, University College London, London, UK.
Michel DardDepartment of Periodontology and Implant Dentistry, New York University, College of Dentistry, New York, USA.
Nikolaos DonosPeriodontology Unit, UCL Eastman Dental Institute, University College London, London, UK. n.donos@ucl.ac.uk.
Eastman Dental Hospital · GBNew York University · USUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectivesIt has recently been shown that enamel matrix derivative (EMD) components (Fraction C, containing <6 kDa peptides (mainly a 5.3 kDa tyrosine-rich amelogenin peptide (TRAP)), and Fraction A, containing a mixture of >6 kDa peptides (including a leucine-rich amelogenin peptide (LRAP))) differentially regulate osteogenic differentiation of periodontal ligament (PDL) cells. The present study examined whether EMD and the EMD Fractions (i) bind and internalize into PDL cells and (ii) precipitate and form insoluble complexes on PDL cells. MATERIALS AND

methodsBiotin-labelled EMD/EMD Fractions were incubated with PDL cells under various different culture conditions and confocal and electron microscopies were carried out to examine the binding and intracellular trafficking of these proteins.

resultsThe results reported here show, for the first time, that at least some components in Fraction A and the TRAP peptide in Fraction C can bind and be internalized by human PDL cells via receptor-mediated endocytosis. In addition, Fraction A was found to form insoluble aggregate-like structures on PDL cells, whereas Fraction C was soluble in culture media.

conclusionSoluble amelogenin isoform TRAP appears to be internalizing into a subset of PDL cells. Moreover, TRAP uptake is most likely controlled by receptor-mediated endocytosis. CLINICAL RELEVANCE: Information on interaction between PDL cells and EMD/TRAP might prove useful in designing targeted interventions (i.e. use of chemically prepared soluble amelogenin peptides) to repair/regenerate periodontal tissues. Such interventions can also (i) avoid the use of rather crude animal-derived enamel matrix protein (EMP)/EMD preparation and (ii) preparation of cost-effective and more controlled chemically synthesized amelogenin peptides for the clinical use.

Indexed as

Cell DifferentiationCells, CulturedDental Enamel ProteinsHumansMicroscopy, ConfocalMicroscopy, Electron, ScanningOsteogenesisPeriodontal LigamentStaining and LabelingDental Enamel Proteinsenamel matrix proteinsEMDEMD uptakeIntracellular traffickingPeriodontal ligament cellsReceptor-mediated endocytosis

Identifiers

PMID26121967
PMCPMC4762925
OpenAlexW855998425

What OpenQuestion holds

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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.