Evidence map›Paper›PMID 17937677›Full record

ArticleClinical and experimental immunology2007

Blockade of protease-activated receptors on T cells correlates with altered proteolysis of CD27 by gingipains of Porphyromonas gingivalis.

L W P Yun, A A Decarlo, N Hunter

Open access · bronzeAbstract read
In one paragraph

Article in Clinical and experimental immunology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

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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

3 authors at 2 institutions in 3 countries.

L W P YunInstitute of Dental Research, Westmead Millennium Institute and Centre for Oral Health, Westmead Hospital, Sydney, New South Wales, Australia. plwyun@yahoo.com
A A Decarlo
N Hunter
Millennium Institute · BRAgenta Biotechnologies (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cysteine proteinases, termed gingipains, of Porphyromonas gingivalis are able to inactivate a broad range of host proteins involved in cellular responses and have been implicated as key virulence factors in the onset and progression of adult periodontitis. In the present study, the high molecular weight Arg-gingipain, RgpA, produced a time- and concentration-dependent hydrolysis of the tumour necrosis factor (TNF)-alpha receptor family member CD27 on resting T cells. As a consequence of CD27 degradation, a reduction in CD27-ligation dependent co-stimulatory CD40L expression was observed. Concomitantly, RgpA activated the protease-activated receptors (PAR)-1, PAR-2 and PAR-4 and induced CD69 and CD25 expression on T cells, thereby demonstrating T cell activation. The Lys-gingipain Kgp demonstrated a low capacity to degrade CD27 but the ability to affect CD27 expression and biological activity was increased when T cells were pretreated with blocking peptide against PAR-2. CD70, the ligand for CD27 induced on activated B cells, was significantly reduced by RgpA treatment and weakly affected by Kgp. These findings suggest that while RgpA can activate T cells through PARs, the parallel action of direct hydrolysis of membrane CD27 as well as CD70 indicates a potential down-regulatory effect through inhibition of CD27/CD70-mediated cell activation in periodontitis.

Indexed as

Adhesins, BacterialAntigens, CDAntigens, Differentiation, T-LymphocyteCD27 LigandCD40 LigandCD4-Positive T-LymphocytesCD69 AntigensCell CycleCells, CulturedCysteine EndopeptidasesDose-Response Relationship, ImmunologicExtracellular FluidFormaldehydeGingipain Cysteine EndopeptidasesHumansInterleukin-2 Receptor alpha SubunitAdhesins, BacterialAntigens, CDAntigens, Differentiation, T-LymphocyteCD27 LigandCD40 LigandCD69 AntigensCysteine EndopeptidasesFormaldehydeGingipain Cysteine EndopeptidasesInterleukin-2 Receptor alpha SubunitLectins, C-TypeparaformPolymersReceptors, Proteinase-ActivatedTumor Necrosis Factor Receptor Superfamily, Member 7

Identifiers

PMID17937677
PMCPMC2219361
OpenAlexW2032625696

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.