Evidence map›Paper›PMID 33569677›Full record

ArticleClinical oral investigations2021

Biochemical and immunohistochemical analysis of tissue inhibitor of metalloproteinases-1 in human sound dentin.

Pietro Gobbi, Tatjana Maravic, Allegra Comba, Claudia Mazzitelli, Edoardo Mancuso, Mirella Falconi, Lorenzo Breschi, Annalisa Mazzoni

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Clinical oral investigations, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.2field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
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

8 authors at 2 institutions in 1 country.

Pietro GobbiDepartment of Biomolecular Sciences, Carlo Bo Urbino University, Via Aurelio Saffi 2, 61029, Urbino, Italy.
Tatjana MaravicDepartment of Biomedical and Neuromotor Sciences, DIBINEM, University of Bologna - Alma Mater Studiorum, Via San Vitale 59, 40125, Bologna, Italy.
Allegra CombaDepartment of Biomedical and Neuromotor Sciences, DIBINEM, University of Bologna - Alma Mater Studiorum, Via San Vitale 59, 40125, Bologna, Italy.
Claudia MazzitelliDepartment of Biomedical and Neuromotor Sciences, DIBINEM, University of Bologna - Alma Mater Studiorum, Via San Vitale 59, 40125, Bologna, Italy.
Edoardo MancusoDepartment of Biomedical and Neuromotor Sciences, DIBINEM, University of Bologna - Alma Mater Studiorum, Via San Vitale 59, 40125, Bologna, Italy.
Mirella FalconiDepartment of Biomedical and Neuromotor Sciences, DIBINEM, University of Bologna - Alma Mater Studiorum, Via San Vitale 59, 40125, Bologna, Italy.
Lorenzo BreschiDepartment of Biomedical and Neuromotor Sciences, DIBINEM, University of Bologna - Alma Mater Studiorum, Via San Vitale 59, 40125, Bologna, Italy. lorenzo.breschi@unibo.it.ORCID http://orcid.org/0000-0001-7621-226X
Annalisa MazzoniDepartment of Biomedical and Neuromotor Sciences, DIBINEM, University of Bologna - Alma Mater Studiorum, Via San Vitale 59, 40125, Bologna, Italy.
University of Bologna · ITUniversity of Urbino · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectivesMatrix metalloproteases (MMPs) are a family of enzymes that operate a proteolytic activity at the level of the extracellular matrix. MMPs are regulated by tissue inhibitors of metalloproteinases (TIMPs) that can ubiquitously bind different enzyme forms. The study aims to identify a morfo-functional association between TIMP-1 and MMP-2 and -9 in human dentin. MATERIALS AND

methodsProteins were extracted from demineralized human sound dentin powder and centrifuged to separate two aliquots with different molecular weights of proteins, higher and lower than 30 kDa. In each aliquot, the evaluation of the presence of TIMP-1/MMP-2 and TIMP-1/MMP-9 was performed using co-immunoprecipitation/immunoblotting analysis. The distribution of TIMP-1, in association with MMP-2 and -9, was investigated using a double immunohistochemical technique. Furthermore, the activity of TIMP-1 was measured by reverse zymography, where acrylamide gel was copolymerized with gelatin and recombinant MMP-2.

resultsCo-immunoprecipitation/immunoblotting analysis showed the association TIMP-1/MMP-2 and TIMP-1/MMP-9 in human sound dentin. Electron microscopy evaluation revealed a diffuse presence of TIMP-1 tightly associated with MMP-2 and -9. Reverse zymography analysis confirmed that TIMP-1 present in human dentin is active and can bind different MMPs isoforms.

conclusionsThe strict association of TIMP-1 with MMP-2 and -9 in situ appeared a constant finding in the human sound dentin. CLINICAL RELEVANCE: Considering the role of TIMP-1, MMP-2, and MMP-9 within the connective tissues, clinically applicable protocols could be developed in the future to increase or decrease the level of TIMPs in human dentin to regulate the activity of MMPs, contributing to reduce caries progression and collagen degradation.

Indexed as

Matrix Metalloproteinase 2Tissue Inhibitor of Metalloproteinase-1DentinHumansMatrix Metalloproteinase 9Matrix MetalloproteinasesTissue Inhibitor of MetalloproteinasesMatrix Metalloproteinase 2Matrix Metalloproteinase 9Matrix MetalloproteinasesMMP2 protein, humanMMP9 protein, humanTIMP1 protein, humanTissue Inhibitor of Metalloproteinase-1Tissue Inhibitor of MetalloproteinasesBiochemical analysisImmunohistochemical analysisMMPsTIMPs

Identifiers

PMID33569677
PMCPMC8342377
OpenAlexW3126251077

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.