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RNA Interference-based Investigation of the Function of Heat Shock Protein 27 during Corneal Epithelial Wound Healing
Published on: September 27, 2016
Protective role of HSP27 against UVC-induced cell death in human cells
Chieko Wano1, Kazuko Kita, Shunji Takahashi
1Department of Environmental Biochemistry, Graduate School of Medicine, Chiba University, Chiba 260-8670, Japan.
Abstract:
It is an intriguing problem whether heat shock proteins (HSPs) play a protective role in UVC-induced cell death in human cells, and the problem has not been solved. To search for the HSPs involved in UVC resistance, gene expression profiles using cDNA array were compared between UVC-sensitive human RSa cells and their UVC-resistant variant AP(r)-1 cells. The expression levels of heat shock protein 27 (HSP27) were lower in RSa cells than in AP(r)-1 cells. RSa cells transfected with sense HSP27 cDNA showed slightly lower sensitivity to UVC-induced cell death than the control cells transfected with a vector alone and much lower sensitivity than RSa cells transfected with the antisense HSP27 cDNA. Furthermore, the removal capacities of the two major types of UVC-damaged DNA (thymine dimers and (6-4)photoproducts) in the cells with the up-regulation of HSP27 were moderately elevated compared with those in the control cells, while those in the cells with down-regulation were remarkably suppressed. These results suggest that HSP27 is involved in the UVC-resistance of human cells, at least those tested, possibly via functioning in nucleotide excision repair.
Insights
Heat shock protein 27 (HSP27) protects human cells against UVC damage. Upregulating HSP27 enhances DNA repair and UVC resistance, while downregulating it suppresses these effects.
Area of Science:
- Molecular Biology
- Cell Biology
- Genetics
Background:
- The role of heat shock proteins (HSPs) in UVC-induced cell death in human cells remains unclear.
- Investigating HSPs involved in UVC resistance is crucial for understanding cellular protection mechanisms.
Purpose of the Study:
- To identify heat shock proteins (HSPs) that contribute to UVC resistance in human cells.
- To elucidate the specific role of heat shock protein 27 (HSP27) in cellular response to UVC radiation.
Main Methods:
- Comparative gene expression profiling using cDNA arrays between UVC-sensitive (RSa) and UVC-resistant (AP(r)-1) human cells.
- Transfection of RSa cells with sense and antisense HSP27 cDNA to modulate HSP27 expression.
- Assessment of UVC-induced cell death sensitivity and DNA repair capacities (thymine dimers and (6-4)photoproducts removal).
Main Results:
- Heat shock protein 27 (HSP27) expression was lower in UVC-sensitive RSa cells compared to UVC-resistant AP(r)-1 cells.
- RSa cells transfected with sense HSP27 cDNA exhibited reduced UVC sensitivity, while antisense transfection increased sensitivity.
- Upregulation of HSP27 moderately enhanced the removal of UVC-damaged DNA, whereas downregulation significantly suppressed it.
Conclusions:
- Heat shock protein 27 (HSP27) plays a significant role in UVC resistance in the tested human cells.
- HSP27 may confer UVC resistance by enhancing nucleotide excision repair, a key DNA repair pathway.
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