Evidence map›Paper›PMID 20837477›Full record

ArticleThe Journal of biological chemistry2010

Entamoeba histolytica cysteine proteinase 5 binds integrin on colonic cells and stimulates NFkappaB-mediated pro-inflammatory responses.

Yongzhong Hou, Leanne Mortimer, Kris Chadee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Membranes · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Taxon-Specific Proteins of the PathogenicFrontiers in cellular and infection microbiology · 2021
    Review
  12. The NF-κB Pathway: Modulation byFrontiers in cellular and infection microbiology · 2021
    Review
  13. Article
  14. Acetylcholine UpregulatesFrontiers in cellular and infection microbiology · 2020
    Article
  15. Article
  16. Article
  17. Editorial: Recent Progresses in Amebiasis.Frontiers in cellular and infection microbiology · 2019
    Article
  18. Article
  19. Beyond the Matrix: The Many Non-ECM Ligands for Integrins.International journal of molecular sciences · 2018
    Review
  20. Frontiers in cellular and infection microbiology · 2018
    Article
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 1 country.

Yongzhong HouDepartment of Microbiology and Infectious Diseases, University of Calgary Health Sciences Centre, Calgary, Alberta T2N 4N1, Canada.
Leanne Mortimer
Kris Chadee
University of Calgary · CAHealth Sciences Centre · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Integrins are important mammalian receptors involved in normal cellular functions and the pathogenesis of inflammation and disease. Entamoeba histolytica is a protozoan parasite that colonizes the gut, and in 10% of infected individuals, causes amebic colitis and liver abscess resulting in 10(5) deaths/year. E. histolytica-induced host inflammatory responses are critical in the pathogenesis of the disease, yet the host and parasite factors involved in disease are poorly defined. Here we show that pro-mature cysteine proteinase 5 (PCP5), a major virulent factor that is abundantly secreted and/or present on the surface of ameba, binds via its RGD motif to α(V)β(3) integrin on Caco-2 colonic cells and stimulates NFκB-mediated pro-inflammatory responses. PCP5 RGD binding to α(V)β(3) integrin triggered integrin-linked kinase(ILK)-mediated phosphorylation of Akt-473 that bound and induced the ubiquitination of NF-κB essential modulator (NEMO). As NEMO is required for activation of the IKKα-IKKβ complex and NFκB signaling, these events markedly up-regulated pro-inflammatory mediator expressions in vitro in Caco-2 cells and in vivo in colonic loop studies in wild-type and Muc2(-/-) mice lacking an intact protective mucus barrier. These results have revealed that EhPCP5 RGD motif is a ligand for α(V)β(3) integrin-mediated adhesion on colonic cells and represents a novel mechanism that E. histolytica trophozoites use to trigger an inflammatory response in the pathogenesis of intestinal amebiasis.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsBlotting, WesternCaco-2 CellsCysteine ProteasesCytokinesDysentery, AmebicEntamoeba histolyticaHost-Pathogen InteractionsHumansI-kappa B KinaseImmunoprecipitationInflammationIntegrin alphaVbeta3MiceCysteine ProteasesCytokinesI-kappa B KinaseIntegrin alphaVbeta3Muc2 protein, mouseMucin-2NF-kappa BProto-Oncogene Proteins c-aktProtozoan Proteins

Identifiers

PMID20837477
PMCPMC2975174
OpenAlexW2045704709

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.