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Gap junctional intercellular communication and cellular response to heat stress.
Nobuyuki Hamada1, Seiji Kodama, Keiji Suzuki
1Division of Radiation Biology, Department of Radiology and Radiation Biology, Graduate School of Biomedical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan.
Carcinogenesis
|August 16, 2003
Summary
Gap junctional intercellular communication (GJIC) protects human cells from heat stress. Disrupting GJIC with lindane or heat shock increases cell death by impairing heat shock protein 72 nuclear translocation and connexin 43 phosphorylation.
Area of Science:
- Cell Biology
- Molecular Biology
- Biophysics
Background:
- Gap junctional intercellular communication (GJIC) is vital for tissue homeostasis and tumor suppression.
- GJIC plays a role in cellular stress responses to radiation and oxidative stress.
- The role of GJIC in heat stress response remains largely unknown.
Purpose of the Study:
- To investigate the contribution of GJIC to cellular heat stress response.
- To determine if GJIC disruption affects heat sensitivity in human cells.
- To examine the impact of heat shock on GJIC and connexin protein phosphorylation.
Main Methods:
- Utilized lindane to inhibit GJIC in normal human cells and assessed heat sensitivity.
- Monitored nuclear translocation of heat shock protein 72 (HSP72).
- Exposed cells to heat shock and analyzed GJIC function and Cx43 phosphorylation.
Main Results:
- Lindane treatment potentiated heat-induced cell killing at 43°C by inhibiting HSP72 nuclear translocation.
- Heat shock induced Cx43 phosphorylation in a time- and temperature-dependent manner.
- Heat shock disrupted GJIC, which was associated with increased Cx43 phosphorylation.
Conclusions:
- GJIC contributes to cellular protection against heat stress.
- Heat shock-induced Cx43 phosphorylation abrogates GJIC, exacerbating hyperthermic lethality.
- Loss of GJIC function may worsen outcomes in heat-stressed conditions, potentially impacting carcinogenesis.