Evidence map›Paper›PMID 11447194›Full record

ArticleInfection and immunity2001

Arginine-specific protease from Porphyromonas gingivalis activates protease-activated receptors on human oral epithelial cells and induces interleukin-6 secretion.

A Lourbakos, J Potempa, J Travis, M R D'Andrea, P Andrade-Gordon, R Santulli, E J Mackie, R N Pike

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

72 citing papers in PubMed, 235 citations in OpenAlex.

  1. Review
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  7. Review
  8. Sepsis - it is all about the platelets.Frontiers in immunology · 2023
    Review
  9. Article
  10. Frontiers in immunology · 2022
    Article
  11. Review
  12. Shut-Down of Type IX Protein Secretion Alters the Host Immune Response toFrontiers in cellular and infection microbiology · 2022
    Article
  13. Article
  14. Article
  15. Ca mobilization and signaling pathways induced by rRgpB in human gingival fibroblast.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2021
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

12 more citing papers are in PubMed but not listed here.

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 5 institutions in 3 countries.

A LourbakosDepartment of Biochemistry & Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
J Potempa
J Travis
M R D'Andrea
P Andrade-Gordon
R Santulli
E J Mackie
R N Pike
Springhouse · USMonash University · AUJagiellonian University · PLUniversity of Georgia · USUniversity of Melbourne · AU

Funding

BACTERIAL PROTEINASES IN PERIODONTAL DISEASER01DE009761 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 1991 to 2012
$3.8M
NIDCR NIH HHS DE 09761NIDCR NIH HHS R01 DE009761
6 · The paper itself

Abstract

Periodontitis is a chronic inflammatory disease affecting oral tissues. Oral epithelial cells represent the primary barrier against bacteria causing the disease. We examined the responses of such cells to an arginine-specific cysteine proteinase (RgpB) produced by a causative agent of periodontal disease, Porphyromonas gingivalis. This protease caused an intracellular calcium transient in an oral epithelial cell line (KB), which was dependent on its enzymatic activity. Since protease-activated receptors (PARs) might mediate such signaling, reverse transcription-PCR was used to characterize the range of these receptors expressed in the KB cells. The cells were found to express PAR-1, PAR-2, and PAR-3, but not PAR-4. In immunohistochemical studies, human gingival epithelial cells were found to express PAR-1, PAR-2, and PAR-3 on their surface, but not PAR-4, indicating that the cell line was an effective model for the in vivo situation. PAR-1 and PAR-2 expression was confirmed in intracellular calcium mobilization assays by treatment of the cells with the relevant receptor agonist peptides. Desensitization experiments strongly indicated that signaling of the effects of RgpB was occurring through PAR-1 and PAR-2. Studies with cells individually transfected with each of these two receptors confirmed that they were both activated by RgpB. Finally, it was shown that, in the oral epithelial cell line, PAR activation by the bacterial protease-stimulated secretion of interleukin-6. This induction of a powerful proinflammatory cytokine suggests a mechanism whereby cysteine proteases from P. gingivalis might mediate inflammatory events associated with periodontal disease on first contact with a primary barrier of cells.

Indexed as

Adhesins, BacterialAnimalsCalciumCell LineCHO CellsCricetinaeCysteine EndopeptidasesEndopeptidasesEpithelial CellsGene ExpressionGingipain Cysteine EndopeptidasesGingivaHemagglutininsHumansInterleukin-6Mouth MucosaAdhesins, Bacterialarginine proteaseCalciumCysteine EndopeptidasesEndopeptidasesGingipain Cysteine EndopeptidasesHemagglutininsInterleukin-6protease-activated receptor 3Receptor, PAR-1Receptor, PAR-2Receptors, Thrombin

Identifiers

PMID11447194
PMCPMC98608
OpenAlexW2137691973

What OpenQuestion holds

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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.