Transient suppression of gap junctional intercellular communication after exposure to 100-nanosecond pulsed electric fields
Language English Country Netherlands Media print-electronic
Document type Journal Article
PubMed
27439151
DOI
10.1016/j.bioelechem.2016.07.003
PII: S1567-5394(16)30087-1
Knihovny.cz E-resources
- Keywords
- Actin, Connexin 43, Cx43, GJIC, MAP kinase, nsPEF,
- MeSH
- Actins metabolism MeSH
- Enzyme Activation MeSH
- Cell Line MeSH
- Time Factors MeSH
- Electricity * MeSH
- Phosphorylation MeSH
- Connexin 43 genetics metabolism MeSH
- Rats MeSH
- Gap Junctions metabolism MeSH
- Cell Communication * MeSH
- Mitogen-Activated Protein Kinase 1 metabolism MeSH
- Mitogen-Activated Protein Kinase 3 metabolism MeSH
- p38 Mitogen-Activated Protein Kinases metabolism MeSH
- Zonula Occludens-1 Protein metabolism MeSH
- Gene Expression Regulation MeSH
- Cell Survival MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Actins MeSH
- Connexin 43 MeSH
- Mitogen-Activated Protein Kinase 1 MeSH
- Mitogen-Activated Protein Kinase 3 MeSH
- p38 Mitogen-Activated Protein Kinases MeSH
- Zonula Occludens-1 Protein MeSH
- Tjp1 protein, rat MeSH Browser
Gap junctional intercellular communication (GJIC) is an important mechanism that is involved and affected in many diseases and injuries. So far, the effect of nanosecond pulsed electric fields (nsPEFs) on the communication between cells was not investigated. An in vitro approach is presented with rat liver epithelial WB-F344 cells grown and exposed in a monolayer. In order to observe sub-lethal effects, cells were exposed to pulsed electric fields with a duration of 100ns and amplitudes between 10 and 20kV/cm. GJIC strongly decreased within 15min after treatment but recovered within 24h. Gene expression of Cx43 was significantly decreased and associated with a reduced total amount of Cx43 protein. In addition, MAP kinases p38 and Erk1/2, involved in Cx43 phosphorylation, were activated and Cx43 became hyperphosphorylated. Immunofluorescent staining of Cx43 displayed the disassembly of gap junctions. Further, a reorganization of the actin cytoskeleton was observed whereas tight junction protein ZO-1 was not significantly affected. All effects were field- and time-dependent and most pronounced within 30 to 60min after treatment. A better understanding of a possible manipulation of GJIC by nsPEFs might eventually offer a possibility to develop and improve treatments.
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