Evidence map›Paper›PMID 31575895›Full record

ArticleScientific reports2019

ADAM10 is Expressed by Ameloblasts, Cleaves the RELT TNF Receptor Extracellular Domain and Facilitates Enamel Development.

Atsushi Ikeda, Shifa Shahid, Benjamin R Blumberg, Maiko Suzuki, John D Bartlett

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
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

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

  1. Pooled it
  2. Integrative multi-omics and bioinformatic analysis ofThe Japanese dental science review · 2026
    Review
  3. Review
  4. Article
  5. [Frameshift mutation inBeijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · 2025
    Article
  6. ADAM10 Expression by Ameloblasts Is Essential for Proper Enamel Formation.International journal of molecular sciences · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. The Autism Spectrum Disorder-Associated Bacterial MetaboliteInternational journal of molecular sciences · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. 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

5 authors at 2 institutions in 1 country.

Atsushi IkedaDivision of Biosciences, The Ohio State University, College of Dentistry, 305W. 12th Avenue, Columbus Ohio, 43210, USA.
Shifa ShahidDivision of Biosciences, The Ohio State University, College of Dentistry, 305W. 12th Avenue, Columbus Ohio, 43210, USA.
Benjamin R BlumbergDivision of Biosciences, The Ohio State University, College of Dentistry, 305W. 12th Avenue, Columbus Ohio, 43210, USA.
Maiko SuzukiDepartment of Oral Biology and Diagnostic Sciences, The Dental College of Georgia, Augusta University, 1460 Laney Walker Blvd., Augusta Georgia, 30912, USA.
John D BartlettDivision of Biosciences, The Ohio State University, College of Dentistry, 305W. 12th Avenue, Columbus Ohio, 43210, USA. bartlett.196@osu.edu.ORCID http://orcid.org/0000-0003-2052-6299
The Ohio State University · USAugusta University · US

Funding

Enamelysin Processing Mechanisms in AmelogenesisR01DE028297 · NIDCR · OHIO STATE UNIVERSITY · PI BARTLETT, JOHN D · 2019 to 2023
$2.7M
NIDCR NIH HHS R01 DE028297
6 · The paper itself

Abstract

MMP20 cleaves cadherins and may facilitate cell movement, however MMP20 is not known to cleave tight junction or desmosome proteins. Ameloblasts had not previously been screened for membrane anchored proteases that could contribute to cell movement. Here we performed a PCR screen for proteolyticlly active A Disintegrin And Metalloproteinase (ADAM) family members. These proteinases are termed sheddases because they have a transmembrane domain and their catalytic domain on the cell surface can function to release anchored proteins. Significantly, ADAMs can be targeted to specific substrates on the cell membrane through their interaction with tetraspanins. Six ADAMs (ADAM8, 9, 10, 15, 17, 19) were expressed in mouse enamel organs. We show that Adam10 expression begins in the apical loop, continues through the secretory stage and abruptly ends at the transition stage when ameloblast migration ceases. ADAM10 cleaves cadherins and tight junction plus desmosome proteins and is well characterized for its role in cell movement. ADAM10 facilitated LS8 cell migration/invasion through a Matrigel coated membrane and we demonstrate that ADAM10, but not ADAM17 cleaves the RELT extracellular domain. This striking result is significant because RELT mutations cause amelogenesis imperfecta (AI) and this directly links ADAM10 to an important role in enamel development.

Indexed as

ADAM10 ProteinAmeloblastsAmyloid Precursor Protein SecretasesAnimalsBlotting, WesternCell MovementDental EnamelFluorescent Antibody TechniqueIn Situ HybridizationMembrane ProteinsMiceReal-Time Polymerase Chain ReactionReceptors, Tumor Necrosis FactorADAM10 ProteinAdam10 protein, mouseAmyloid Precursor Protein SecretasesMembrane ProteinsReceptors, Tumor Necrosis FactorRelt protein, mouse

Identifiers

PMID31575895
PMCPMC6773779
OpenAlexW2977738228

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.