Protein phosphatase 2A inhibition and subsequent cytoskeleton reorganization contributes to cell migration caused by microcystin-LR in human laryngeal epithelial cells (Hep-2)

2016 ◽  
Vol 32 (3) ◽  
pp. 890-903 ◽  
Author(s):  
Beilei Wang ◽  
Jinghui Liu ◽  
Pu Huang ◽  
Kailun Xu ◽  
Hanying Wang ◽  
...  
Keyword(s):  
Cell Migration ◽  
Epithelial Cells ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Cytoskeleton Reorganization ◽  
Phosphatase 2A

scholarly journals Protein phosphatase 2A–mediated flotillin-1 dephosphorylation up-regulates endothelial cell migration and angiogenesis regulation

2019 ◽  
Vol 294 (52) ◽  
pp. 20196-20206 ◽  
Author(s):  
Zsófia Thalwieser ◽  
Nikolett Király ◽  
Márton Fonódi ◽  
Csilla Csortos ◽  
Anita Boratkó
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Endothelial Cell Migration ◽  
Phosphatase 2A

scholarly journals Activating protein phosphatase 2A (PP2A) enhances tristetraprolin (TTP) anti-inflammatory function in A549 lung epithelial cells

2016 ◽  
Vol 28 (4) ◽  
pp. 325-334 ◽  
Author(s):  
Md. Mostafizur Rahman ◽  
Nowshin N. Rumzhum ◽  
Philip M. Hansbro ◽  
Jonathan C. Morris ◽  
Andrew R. Clark ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Lung Epithelial Cells ◽  
Lung Epithelial ◽  
Phosphatase 2A ◽  
Anti Inflammatory ◽  
A549 Lung

scholarly journals Loss of myeloid-specific protein phosphatase 2A enhances lung injury and fibrosis and results in IL-10-dependent sensitization of epithelial cell apoptosis

2019 ◽  
Vol 316 (6) ◽  
pp. L1035-L1048 ◽  
Author(s):  
Lei Sun ◽  
Elissa M. Hult ◽  
Timothy T. Cornell ◽  
Kevin K. Kim ◽  
Thomas P. Shanley ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Lung Injury ◽  
Protein Phosphatase ◽  
Cell Apoptosis ◽  
Cell Function ◽  
Protein Phosphatase 2A ◽  
Cytokine Signaling ◽  
Epithelial Cell Apoptosis ◽  
Phosphatase 2A

Protein phosphatase 2A (PP2A), a ubiquitously expressed Ser/Thr phosphatase is an important regulator of cytokine signaling and cell function. We previously showed that myeloid-specific deletion of PP2A (LysMcrePP2A−/−) increased mortality in a murine peritoneal sepsis model. In the current study, we assessed the role of myeloid PP2A in regulation of lung injury induced by lipopolysaccharide (LPS) or bleomycin delivered intratracheally. LysMcrePP2A−/− mice experienced increased lung injury in response to both LPS and bleomycin. LysMcrePP2A−/− mice developed more exuberant fibrosis in response to bleomycin, elevated cytokine responses, and chronic myeloid inflammation. Bone marrow-derived macrophages (BMDMs) from LysMcrePP2A−/− mice showed exaggerated inflammatory cytokine release under conditions of both M1 and M2 activation. Notably, secretion of IL-10 was elevated under all stimulation conditions, including activation of BMDMs by multiple Toll-like receptor ligands. Supernatants collected from LPS-stimulated LysMcrePP2A−/− BMDMs induced epithelial cell apoptosis in vitro but this effect was mitigated when IL-10 was also depleted from the BMDMs by crossing LysMcrePP2A−/− mice with systemic IL-10−/− mice (LysMcrePP2A−/− × IL-10−/−) or when IL-10 was neutralized. Despite these findings, IL-10 did not directly induce epithelial cell apoptosis but sensitized epithelial cells to other mediators from the BMDMs. Taken together our results demonstrate that myeloid PP2A regulates production of multiple cytokines but that its effect is most pronounced on IL-10 production. Furthermore, IL-10 sensitizes epithelial cells to apoptosis in response to myeloid-derived mediators, which likely contributes to the pathogenesis of lung injury and fibrosis in this model.

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