Anthrax infection inhibits the AKT signaling involved in the E-cadherin-mediated adhesion of lung epithelial cells
Abstract
The effect of anthrax infection on phosphoprotein signaling was studied in human small airway lung epithelial cells exposed to B. anthracis spores of the plasmidless dSterne strain in comparison with the Sterne strain containing the toxigenic plasmid (pXO1). The differential regulation of phosphorylation was found in the mitogen-activated protein kinase cascade (ERK, p38, and P90RSK), the PI3K cascade (AKT, GSK-3α/β), and downstream in the case of the proapoptotic BAD and the transcription factor STAT3. Both strains stimulate phosphorylation of CREB and inhibit phosphorylation of 4E-BP1 required for activation of cap-dependent translation. Downregulation of the survival AKT phosphorylation by the Sterne strain inhibits the process of Ca2+-dependent homophilic interaction of E-cadherin (EC) upon formation or repair of cell–cell contacts. Both lethal and edema toxins produced by the Sterne strain inhibit the AKT phosphorylation induced during the EC-mediated signaling. Activity of ERK1/2 and p38 inhibitors indicates that inhibition of AKT phosphorylation takes place through the ERK1/2-PI3K crosstalk. In Sterne spore-challenged mice, a specific inhibitor of PI3K/AKT, wortmannin, accelerates the lethal outcome, and reduction of AKT phosphorylation in the circulating blood cells coincides with the death of animals. We conclude that the PI3K/AKT pathway controlling the integrity of epithelium plays an important survivalmore »
- Authors:
-
- George Mason Univ., Fairfax, VA (United States). National Center for Biodefense and Infectious Diseases
- George Mason Univ., Fairfax, VA (United States). Center for Applied Proteomics and Molecular Medicine
- Publication Date:
- Research Org.:
- George Mason Univ., Fairfax, VA (United States)
- Sponsoring Org.:
- USDOE; USDOD
- OSTI Identifier:
- 1625901
- Grant/Contract Number:
- FC52-04NA25455; DAMD17-03-C-0122
- Resource Type:
- Accepted Manuscript
- Journal Name:
- FEMS Immunology & Medical Microbiology
- Additional Journal Information:
- Journal Volume: 56; Journal Issue: 2; Journal ID: ISSN 0928-8244
- Publisher:
- Elsevier
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 60 APPLIED LIFE SCIENCES; 59 BASIC BIOLOGICAL SCIENCES; immunology; infectious diseases; microbiology; reverse-phase microarray; cell signaling; epithelial cells; AKT; cell–cell adherence
Citation Formats
Popova, Taissia, Espina, Virginia, Bailey, Charles, Liotta, Lance, Petricoin, Emanuel, and Popov, Serguei. Anthrax infection inhibits the AKT signaling involved in the E-cadherin-mediated adhesion of lung epithelial cells. United States: N. p., 2009.
Web. doi:10.1111/j.1574-695x.2009.00558.x.
Popova, Taissia, Espina, Virginia, Bailey, Charles, Liotta, Lance, Petricoin, Emanuel, & Popov, Serguei. Anthrax infection inhibits the AKT signaling involved in the E-cadherin-mediated adhesion of lung epithelial cells. United States. https://doi.org/10.1111/j.1574-695x.2009.00558.x
Popova, Taissia, Espina, Virginia, Bailey, Charles, Liotta, Lance, Petricoin, Emanuel, and Popov, Serguei. Wed .
"Anthrax infection inhibits the AKT signaling involved in the E-cadherin-mediated adhesion of lung epithelial cells". United States. https://doi.org/10.1111/j.1574-695x.2009.00558.x. https://www.osti.gov/servlets/purl/1625901.
@article{osti_1625901,
title = {Anthrax infection inhibits the AKT signaling involved in the E-cadherin-mediated adhesion of lung epithelial cells},
author = {Popova, Taissia and Espina, Virginia and Bailey, Charles and Liotta, Lance and Petricoin, Emanuel and Popov, Serguei},
abstractNote = {The effect of anthrax infection on phosphoprotein signaling was studied in human small airway lung epithelial cells exposed to B. anthracis spores of the plasmidless dSterne strain in comparison with the Sterne strain containing the toxigenic plasmid (pXO1). The differential regulation of phosphorylation was found in the mitogen-activated protein kinase cascade (ERK, p38, and P90RSK), the PI3K cascade (AKT, GSK-3α/β), and downstream in the case of the proapoptotic BAD and the transcription factor STAT3. Both strains stimulate phosphorylation of CREB and inhibit phosphorylation of 4E-BP1 required for activation of cap-dependent translation. Downregulation of the survival AKT phosphorylation by the Sterne strain inhibits the process of Ca2+-dependent homophilic interaction of E-cadherin (EC) upon formation or repair of cell–cell contacts. Both lethal and edema toxins produced by the Sterne strain inhibit the AKT phosphorylation induced during the EC-mediated signaling. Activity of ERK1/2 and p38 inhibitors indicates that inhibition of AKT phosphorylation takes place through the ERK1/2-PI3K crosstalk. In Sterne spore-challenged mice, a specific inhibitor of PI3K/AKT, wortmannin, accelerates the lethal outcome, and reduction of AKT phosphorylation in the circulating blood cells coincides with the death of animals. We conclude that the PI3K/AKT pathway controlling the integrity of epithelium plays an important survival role in anthrax infection.},
doi = {10.1111/j.1574-695x.2009.00558.x},
journal = {FEMS Immunology & Medical Microbiology},
number = 2,
volume = 56,
place = {United States},
year = {Wed Jul 01 00:00:00 EDT 2009},
month = {Wed Jul 01 00:00:00 EDT 2009}
}
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