Evidence map›Paper›PMID 16988242›Full record

ArticleInfection and immunity2006

Gingipains from Porphyromonas gingivalis W83 synergistically disrupt endothelial cell adhesion and can induce caspase-independent apoptosis.

Shaun M Sheets, Jan Potempa, James Travis, Hansel M Fletcher, Carlos A Casiano

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.7field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 63 citations in OpenAlex.

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  10. Roles of Porphyromonas gingivalis and its virulence factors in periodontitis.Advances in protein chemistry and structural biology · 2020
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  13. Oral Mucosal Epithelial Cells.Frontiers in immunology · 2019
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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

5 authors at 3 institutions in 2 countries.

Shaun M SheetsDepartment of Biochemistry and Microbiology, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA. ssheets04b@llu.edu
Jan Potempa
James Travis
Hansel M Fletcher
Carlos A Casiano
Loma Linda University · USJagiellonian University · PLUniversity of Georgia · US

Funding

BACTERIAL PROTEINASES IN PERIODONTAL DISEASER01DE009761 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 1991 to 2012
$3.8M
Studies on virulence regulation in PorphyromonasR01DE013664 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2002 to 2011
$3.3M
Studies on the virulence regulation in PorphyromonasR56DE013664 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2014 to 2014
$291k
NIDCR NIH HHS DE09761NIDCR NIH HHS DE13664NIDCR NIH HHS DE13664-S1NIDCR NIH HHS R01 DE009761NIDCR NIH HHS R01 DE013664NIDCR NIH HHS R56 DE013664PHS HHS A144088
6 · The paper itself

Abstract

We have shown previously that gingipains from Porphyromonas gingivalis W83 can induce cell detachment, cell adhesion molecule (CAM) cleavage, and apoptosis in endothelial cells; however, the specific roles of the individual gingipains are unclear. Using purified gingipains, we determined that each of the gingipains can cleave CAMs to varying degrees with differing kinetics. Kgp and HRgpA work together to quickly detach endothelial cells. Interestingly, in the absence of active caspases, both gingipain-active W83 extracts and purified HRgpA and RgpB induce apoptotic morphology, suggesting that the gingipains can induce both caspase-dependent and caspase-independent apoptosis. Using z-VAD-FMK to inhibit Kgp activity and leupeptin to inhibit Rgp activity in gingipain-active W83 extracts, we investigated the relative significance of the synergistic role of the gingipains. z-VAD-FMK or leupeptin delayed, but did not inhibit, cell detachment induced by gingipain-active W83 extracts or purified gingipains. There was partial cleavage of N-cadherin and cleavage of VE-cadherin was not inhibited. Degradation of integrin beta1 was inhibited only in the presence of z-VAD-FMK. These results further clarify the role P. gingivalis plays in tissue destruction occurring in the periodontal pocket.

Indexed as

ApoptosisAdhesins, BacterialAmino Acid Chloromethyl KetonesAnimalsCaspase InhibitorsCaspasesCattleCell AdhesionCell Adhesion MoleculesCells, CulturedCysteine EndopeptidasesCysteine Proteinase InhibitorsEndothelial CellsGingipain Cysteine EndopeptidasesPorphyromonas gingivalisAdhesins, BacterialAmino Acid Chloromethyl Ketonesbenzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketoneCaspase InhibitorsCaspasesCell Adhesion MoleculesCysteine EndopeptidasesCysteine Proteinase InhibitorsGingipain Cysteine Endopeptidases

Identifiers

PMID16988242
PMCPMC1594922
OpenAlexW2018824898

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.