Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding
The pervasive weak electromagnetic fields (EMF) inundate the industrialized society, but the biological effects of EMF as weak as 10 µT have been scarcely analyzed. Heat shock proteins (HSPs) are molecular chaperones that mediate a sequential stress response. HSP70 and HSP90 provide cells under unde...
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| Format: | Article |
| Language: | English |
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Elsevier
2023-10-01
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| Series: | Ecotoxicology and Environmental Safety |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S0147651323009867 |
| _version_ | 1797676599456301056 |
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| author | Zhizhou Huang Mikako Ito Shaochuan Zhang Takuro Toda Jun-ichi Takeda Tomoo Ogi Kinji Ohno |
| author_facet | Zhizhou Huang Mikako Ito Shaochuan Zhang Takuro Toda Jun-ichi Takeda Tomoo Ogi Kinji Ohno |
| author_sort | Zhizhou Huang |
| collection | DOAJ |
| description | The pervasive weak electromagnetic fields (EMF) inundate the industrialized society, but the biological effects of EMF as weak as 10 µT have been scarcely analyzed. Heat shock proteins (HSPs) are molecular chaperones that mediate a sequential stress response. HSP70 and HSP90 provide cells under undesirable situations with either assisting covalent folding of proteins or degrading improperly folded proteins in an ATP-dependent manner. Here we examined the effect of extremely low-frequency (ELF)-EMF on AML12 and HEK293 cells. Although the protein expression levels of HSP70 and HSP90 were reduced after an exposure to ELF-EMF for 3 h, acetylations of HSP70 and HSP90 were increased, which was followed by an enhanced binding affinities of HSP70 and HSP90 for HSP70/HSP90-organizing protein (HOP/STIP1). After 3 h exposure to ELF-EMF, the amount of mitochondria was reduced but the ATP level and the maximal mitochondrial oxygen consumption were increased, which was followed by the reduced protein aggregates and the increased cell viability. Thus, ELF-EMF exposure for 3 h activated acetylation of HSPs to enhance protein folding, which was returned to the basal level at 12 h. The proteostatic effects of ELF-EMF will be able to be applied to treat pathological states in humans. |
| first_indexed | 2024-03-11T22:31:34Z |
| format | Article |
| id | doaj.art-1c02a5dbff1c4665ae89f11bc10d3249 |
| institution | Directory Open Access Journal |
| issn | 0147-6513 |
| language | English |
| last_indexed | 2024-03-11T22:31:34Z |
| publishDate | 2023-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Ecotoxicology and Environmental Safety |
| spelling | doaj.art-1c02a5dbff1c4665ae89f11bc10d32492023-09-23T05:10:12ZengElsevierEcotoxicology and Environmental Safety0147-65132023-10-01264115482Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein foldingZhizhou Huang0Mikako Ito1Shaochuan Zhang2Takuro Toda3Jun-ichi Takeda4Tomoo Ogi5Kinji Ohno6Division of Neurogenetics, Center for Neurological Diseases and Cancer, Nagoya University Graduate School of Medicine, Nagoya, JapanDivision of Neurogenetics, Center for Neurological Diseases and Cancer, Nagoya University Graduate School of Medicine, Nagoya, JapanDivision of Neurogenetics, Center for Neurological Diseases and Cancer, Nagoya University Graduate School of Medicine, Nagoya, JapanDivision of Neurogenetics, Center for Neurological Diseases and Cancer, Nagoya University Graduate School of Medicine, Nagoya, JapanDivision of Neurogenetics, Center for Neurological Diseases and Cancer, Nagoya University Graduate School of Medicine, Nagoya, JapanDepartment of Genetics, Research Institute of Environmental Medicine (RIeM), Nagoya University, Nagoya, JapanDivision of Neurogenetics, Center for Neurological Diseases and Cancer, Nagoya University Graduate School of Medicine, Nagoya, Japan; Correspondence to: Division of Neurogenetics, Center for Neurological Diseases and Cancer, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466–8550, Japan.The pervasive weak electromagnetic fields (EMF) inundate the industrialized society, but the biological effects of EMF as weak as 10 µT have been scarcely analyzed. Heat shock proteins (HSPs) are molecular chaperones that mediate a sequential stress response. HSP70 and HSP90 provide cells under undesirable situations with either assisting covalent folding of proteins or degrading improperly folded proteins in an ATP-dependent manner. Here we examined the effect of extremely low-frequency (ELF)-EMF on AML12 and HEK293 cells. Although the protein expression levels of HSP70 and HSP90 were reduced after an exposure to ELF-EMF for 3 h, acetylations of HSP70 and HSP90 were increased, which was followed by an enhanced binding affinities of HSP70 and HSP90 for HSP70/HSP90-organizing protein (HOP/STIP1). After 3 h exposure to ELF-EMF, the amount of mitochondria was reduced but the ATP level and the maximal mitochondrial oxygen consumption were increased, which was followed by the reduced protein aggregates and the increased cell viability. Thus, ELF-EMF exposure for 3 h activated acetylation of HSPs to enhance protein folding, which was returned to the basal level at 12 h. The proteostatic effects of ELF-EMF will be able to be applied to treat pathological states in humans.http://www.sciencedirect.com/science/article/pii/S0147651323009867ELF-EMFHSP70HSP90AcetylationHOP/STIP1Mitochondria |
| spellingShingle | Zhizhou Huang Mikako Ito Shaochuan Zhang Takuro Toda Jun-ichi Takeda Tomoo Ogi Kinji Ohno Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding Ecotoxicology and Environmental Safety ELF-EMF HSP70 HSP90 Acetylation HOP/STIP1 Mitochondria |
| title | Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding |
| title_full | Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding |
| title_fullStr | Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding |
| title_full_unstemmed | Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding |
| title_short | Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding |
| title_sort | extremely low frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding |
| topic | ELF-EMF HSP70 HSP90 Acetylation HOP/STIP1 Mitochondria |
| url | http://www.sciencedirect.com/science/article/pii/S0147651323009867 |
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