Evidence map›Paper›PMID 10661319›Full record

ArticleThe Histochemical journal1999

Stromelysin-1 (MMP-3) in forming enamel and predentine in rat incisor-coordinated distribution with proteoglycans suggests a functional role.

R Hall, D Septier, G Embery, M Goldberg

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in The Histochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 91 citations in OpenAlex.

  1. Allelic and Genotypic Distribution ofClinics and practice · 2025
    Article
  2. Article
  3. Matrix metalloproteinase inhibitors in restorative dentistry.Journal of conservative dentistry and endodontics · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. [Progress on matrix metalloproteinase inhibitors].Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2017
    Article
  11. Genetic Association ofInternational journal of dentistry · 2017
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Dentin: structure, composition and mineralization.Frontiers in bioscience (Elite edition) · 2011
    Review
  19. The NH2-terminal and COOH-terminal fragments of dentin matrix protein 1 (DMP1) localize differently in the compartments of dentin and growth plate of bone.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2009
    Article
  20. 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

4 authors at 4 institutions in 2 countries.

R HallBasic Dental Science, Dental School, University of Wales College of Medicine, Cardiff, UK.
D Septier
G Embery
M Goldberg
Assistance Publique – Hôpitaux de Paris · FRUniversité Paris Cité · FRUniversity Dental Hospital on Cardiff University · GBUniversity of Wales · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Stromelysin-1 (matrix metalloproteinase-3) or proteoglycanase was visualized by light and electron microscopy immunolabelling in the forming zone of rat incisors. In predentine, labelling was more dense at the transition zone between the inner proximal third and the two outer thirds. Odontoblast processes were also positively stained, mostly in predentine and to a lesser degree in dentine. The dentine-enamel junction was intensely labelled, whereas dentine and forming enamel were only faintly stained. Gold-antibodies complexes were seen inside secretory ameloblasts and odontoblasts in cytosolic locations. The distribution of stromelysin-1 was compared with the distribution of 2-B-6 epitope, an antibody recognizing chondroitin-4-sulphate/dermatan sulphate and which showed a decreasing gradient from the proximal zone to the distal part of predentine. In contrast, both 5-D-4, an anti-keratan sulphate antibody and an anti-lumican antibody displayed a reversed distribution, with an increase seen from the proximal and central thirds to the distal part of predentine. This coordinated distribution suggests that stromelysin-1 may have a functional role, being implicated in predentine in the degradation of chondroitin-4-sulphate/dermatan sulphate-containing proteoglycans, and consequently allowing keratan sulphate proteoglycan concentration to increase near the border where mineralization is initiated.

Indexed as

AmeloblastsAnimalsChondroitin Sulfate ProteoglycansChondroitin SulfatesDental EnamelDentinDextran SulfateIncisorKeratan SulfateLumicanMaleMatrix Metalloproteinase 3OdontoblastsProteoglycansRatsRats, Sprague-DawleyChondroitin Sulfate ProteoglycansChondroitin SulfatesDextran SulfateKeratan SulfateLumicanLum protein, ratMatrix Metalloproteinase 3Proteoglycans

Identifiers

PMID10661319
OpenAlexW347936593

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.