Mild Electrical Stimulation Increases Ubiquitinated Proteins and Hsp72 in A549 Cells via Attenuation of Proteasomal Degradation

To explore the cellular effects of mild electrical stimulation (MES), we treated A549 cells with low-intensity direct current at 5 V applied for 10 min. MES did not induce cell cytotoxicity or the unfolded protein response (UPR). Interestingly, the expression of ubiquitinated proteins and heat shock...

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Main Authors: Saori Morino (Author), Mary Ann Suico (Author), Tatsuya Kondo (Author), Erika Sekimoto (Author), Shuichiro Yano (Author), Tomoko Matsuda (Author), Takashi Matsuno (Author), Tsuyoshi Shuto (Author), Eiichi Araki (Author), Hirofumi Kai (Author)
Format: Book
Published: Elsevier, 2008-01-01T00:00:00Z.
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Summary:To explore the cellular effects of mild electrical stimulation (MES), we treated A549 cells with low-intensity direct current at 5 V applied for 10 min. MES did not induce cell cytotoxicity or the unfolded protein response (UPR). Interestingly, the expression of ubiquitinated proteins and heat shock protein (Hsp)72 was increased but not that of other Hsps. MES attenuated the degradation of Hsp72, which is a substrate of the proteasome-ubiquitin system. These results, along with the observed increase in expression of ubiquitinated proteins, imply that MES may affect the proteasome system, which regulates the fate of many proteins. Keywords:: mild electrical stimulation, proteasomal degradation, ubiquitinated protein
Item Description:1347-8613
10.1254/jphs.08180SC