Rho inhibition decreases TNF-induced endothelial MAPK activation and monolayer permeability
Journal of Applied Physiology, ISSN: 8750-7587, Vol: 95, Issue: 5, Page: 1889-1895
2003
- 74Citations
- 22Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations74
- Citation Indexes74
- 74
- CrossRef61
- Captures22
- Readers22
- 22
Article Description
Our laboratory previously demonstrated that MAPK activation is an important signal during cytokine-induced endothelial permeability (Nwariaku FE, Liu Z, Terada L, Duffy S, Sarosi G, and Turnage R. Shock 18: 82-85, 2002). Because GTP-binding proteins have been implicated in MAPK activation, we now hypothesize that the GTP-binding protein Rho is a mediator of TNF-induced MAPK activation and increased endothelial permeability. Transmonolayer permeability was assessed in human lung microvascular cells by measuring transmonolayer electrical resistance. MAPK activity was assessed by using a phospho-specific immunoprecipitation kinase assay and by comparing Western blots for phospho-MAPK with total MAPK. MAPK inhibitors used were SB-202190 and PD-098059, whereas Clostridium botulinum C3 transferase was used as a Rho inactivator. Rho-associated coiled-coil kinase was inhibited with Y-27632. TNF increased pulmonary endothelial permeability in vitro and caused a rapid, sustained increase in endothelial p38 and extracellular signal-regulated kinase MAPK activity. Inhibition of p38 and extracellular signal-regulated kinase MAPK with SB-202190 and PD-098059, respectively, decreased TNF-induced endothelial permeability. C3 transferase attenuated TNF-induced MAPK activation and blocked TNF-induced endothelial permeability. Finally, inhibition of Rho-associated coiled-coil kinase with Y-27632 prevented both MAPK activation and TNF-induced decreases in transmonolayer resistance. Rho acts upstream of mitogen-activated protein kinases in mediating TNF-induced pulmonary endothelial leak.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0142180272&origin=inward; http://dx.doi.org/10.1152/japplphysiol.00225.2003; http://www.ncbi.nlm.nih.gov/pubmed/12844496; https://www.physiology.org/doi/10.1152/japplphysiol.00225.2003; http://www.physiology.org/doi/10.1152/japplphysiol.00225.2003; https://www.physiology.org/action/captchaChallenge?redirectUrl=https%3A%2F%2Fwww.physiology.org%2Fdoi%2Ffull%2F10.1152%2Fjapplphysiol.00225.2003
American Physiological Society
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