Evidence map›Paper›PMID 23313574›Full record

ArticleBiochimica et biophysica acta2013

Cleavage of extracellular matrix in periodontitis: gingipains differentially affect cell adhesion activities of fibronectin and tenascin-C.

Sabrina Ruggiero, Raluca Cosgarea, Jan Potempa, Barbara Potempa, Sigrun Eick, Matthias Chiquet

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 49 citations in OpenAlex.

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  19. Metabolic cooperativity betweenJournal of oral microbiology · 2020
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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

6 authors at 4 institutions in 4 countries.

Sabrina RuggieroDepartment of Orthodontics and Dentofacial Orthopedics, University of Bern, Switzerland.
Raluca Cosgarea
Jan Potempa
Barbara Potempa
Sigrun Eick
Matthias Chiquet
University of Bern · CHIuliu Hațieganu University of Medicine and Pharmacy · ROJagiellonian University · PLUniversity of Louisville · US

Funding

BACTERIAL PROTEINASES IN PERIODONTAL DISEASER01DE009761 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 1991 to 2012
$3.8M
NIDCR NIH HHS DE09761NIDCR NIH HHS R01 DE009761
6 · The paper itself

Abstract

Gingipains are cysteine proteases that represent major virulence factors of the periodontopathogenic bacterium Porphyromonas gingivalis. Gingipains are reported to degrade extracellular matrix (ECM) of periodontal tissues, leading to tissue destruction and apoptosis. The exact mechanism is not known, however. Fibronectin and tenascin-C are pericellular ECM glycoproteins present in periodontal tissues. Whereas fibronectin mediates fibroblast adhesion, tenascin-C binds to fibronectin and inhibits its cell-spreading activity. Using purified proteins in vitro, we asked whether fibronectin and tenascin-C are cleaved by gingipains at clinically relevant concentrations, and how fragmentation by the bacterial proteases affects their biological activity in cell adhesion. Fibronectin was cleaved into distinct fragments by all three gingipains; however, only arginine-specific HRgpA and RgpB but not lysine-specific Kgp destroyed its cell-spreading activity. This result was confirmed with recombinant cell-binding domain of fibronectin. Of the two major tenascin-C splice variants, the large but not the small was a substrate for gingipains, indicating that cleavage occurred primarily in the alternatively spliced domain. Surprisingly, cleavage of large tenascin-C variant by all three gingipains generated fragments with increased anti-adhesive activity towards intact fibronectin. Fibronectin and tenascin-C fragments were detected in gingival crevicular fluid of a subset of periodontitis patients. We conclude that cleavage by gingipains directly affects the biological activity of both fibronectin and tenascin-C in a manner that might lead to increased cell detachment and loss during periodontal disease.

Indexed as

Adhesins, BacterialCysteine EndopeptidasesFibronectinsPeriodontitisTenascinAlternative SplicingAnimalsApoptosisArginineCell AdhesionCells, CulturedExtracellular MatrixFibroblastsGingipain Cysteine EndopeptidasesHumansLysineAdhesins, BacterialArginineCysteine EndopeptidasesFibronectinsGingipain Cysteine EndopeptidasesLysineTenascin

Identifiers

PMID23313574
PMCPMC4188551
OpenAlexW2019675891

What OpenQuestion holds

Textmetadata
LicenceTDM
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.