Evidence map›Paper›PMID 10899852›Full record

ArticleInfection and immunity2000

Differential modulation and subsequent blockade of mitogenic signaling and cell cycle progression by Pasteurella multocida toxin.

B A Wilson, L R Aminova, V G Ponferrada, M Ho

Erratum issuedOpen access · greenAbstract readComparative Study
In one paragraph

Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Substrate specificity of Pasteurella multocida toxin for α subunits of heterotrimeric G proteins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Pasteurella multocida toxin activation of heterotrimeric G proteins by deamidation.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  16. Article
  17. Article
  18. Pasteurella multocida toxin as a tool for studying Gq signal transduction.Reviews of physiology, biochemistry and pharmacology · 2004
    Review
  19. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

B A WilsonDepartment of Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA. bawilson@life.uiuc.edu
L R Aminova
V G Ponferrada
M Ho
University of Illinois Urbana-Champaign · US

Funding

Pasteurella multocida toxin: Structure and ActivityR01AI038396 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI WILSON, BRENDA A. · 2004 to 2008
$1.7M
PASTEURELLA MULTOCIDA TOXIN--STRUCTURE AND ACTIVITYR29AI038396 · NIAID · WRIGHT STATE UNIVERSITY · PI WILSON, BRENDA A. · 1996 to 2000
$105k
NIAID NIH HHS AI38396NIAID NIH HHS R01 AI038396NIAID NIH HHS R29 AI038396
6 · The paper itself

Abstract

The intracellularly acting protein toxin of Pasteurella multocida (PMT) causes numerous effects in cells, including activation of inositol 1,4,5-trisphosphate (IP(3)) signaling, Ca(2+) mobilization, protein phosphorylation, morphological changes, and DNA synthesis. The direct intracellular target of PMT responsible for activation of the IP(3) pathway is the G(q/11)alpha-protein, which stimulates phospholipase C (PLC) beta1. The relationship between PMT-mediated activation of the G(q/11)-PLC-IP(3) pathway and its ability to promote mitogenesis and cellular proliferation is not clear. PMT stimulation of p42/p44 mitogen-activated protein kinase occurs upstream via G(q/11)-dependent transactivation of the epidermal growth factor receptor. We have further characterized the effects of PMT on the downstream mitogenic response and cell cycle progression in Swiss 3T3 and Vero cells. PMT treatment caused dramatic morphological changes in both cell lines. In Vero cells, limited multinucleation, nuclear fragmentation, and disruption of cytokinesis were also observed; however, a strong mitogenic response occurred only with Swiss 3T3 cells. Significantly, this mitogenic response was not sustained. Cell cycle analysis revealed that after the initial mitogenic response to PMT, both cell types subsequently arrested primarily in G(1) and became unresponsive to further PMT treatment. In Swiss 3T3 cells, PMT induced up-regulation of c-Myc; cyclins D1, D2, D3, and E; p21; PCNA; and the Rb proteins, p107 and p130. In Vero cells, PMT failed to up-regulate PCNA and cyclins D3 and E. We also found that the initial PMT-mediated up-regulation of several of these signaling proteins was not sustained, supporting the subsequent cell cycle arrest. The consequences of PMT entry thus depend on the differential regulation of signaling pathways within different cell types.

Indexed as

Bacterial ProteinsPasteurella multocida3T3 CellsAnimalsAntineoplastic AgentsBacterial ToxinsCell Cycle ProteinsChlorocebus aethiopsCytoskeletonMiceMitogensRecombinant ProteinsSignal TransductionVero CellsAntineoplastic AgentsBacterial ProteinsBacterial ToxinsCell Cycle ProteinsMitogensPasteurella multocida toxinRecombinant Proteins

Identifiers

PMID10899852
PMCPMC98366
OpenAlexW2159350304

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.