Speaker
Description
The application of pulsed power technology is spreading to biotechnology and medical fields. Pulse electric fields yield various influences on cells. Endoplasmic reticulum (ER) stress which is due to accumulation of unfolded proteins has been considered as one of pathogenies such as diabetes and Alzheimer. Unfolded protein response (UPR) is a built-in avoiding function of ER stress and conduct reactions as promotion and pausing of folding. The activation of UPR by application of nsPEFs on cells was studied. Here, proper conditions to activate UPR were explored in experiments. Eukaryotic translation initiation factor 2 subunit α (eIF2α) is phosphorylated and translation of protein is inhibited when cells are stressed. Transportations of protein before folding to ER was accordingly inhibited and that process is UPR. In this experiment, phosphorylated eIF2α (P-eIF2α) was observed to check the induction of UPR. Electric fields pulses of 14ns in pulse width were applied on MEF and HeLa cells and expression of P-eIF2α was evaluated by western blotting. Relatively high electric fields pulses: over 100kV/cm were applied in this experiment. Thapsigargin was used for positive control. The P-eIF2α expression of high electric field pulse applied samples was significantly smaller than low electric field samples. Nevertheless, a tendency was seen that P-eIF2α expression increased with number of pulses. The detailed results will be presented on the conference.
