論文 - 詳細
| RRC ID | 82124 |
|---|---|
| 著者 | Aklima J, Onchaiya S, Saotome T, Velmurugan P, Motoichi T, Naima J, Kuroda Y, Ohta Y. |
| タイトル | Direct Analysis of Mitochondrial Damage Caused by Misfolded/Destabilized Proteins. |
| ジャーナル | Int J Mol Sci |
| Abstract |
Protein quality control is essential for cellular homeostasis. In this study, we examined the effect of improperly folded proteins that do not form amyloid fibrils on mitochondria, which play important roles in ATP production and cell death. First, we prepared domain 3 of the dengue envelope protein in wild type and four mutants with widely different biophysical properties in misfolded/aggregated or destabilized states. The effects of the different proteins were detected using fluorescence microscopy and Western blotting, which revealed that three of the five proteins disrupted both inner and outer membrane integrity, while the other two proteins, including the wild type, did not. Next, we examined the common characteristics of the proteins that displayed toxicity against mitochondria by measuring oligomer size, molten globule-like properties, and thermal stability. The common feature of all three toxic proteins was thermal instability. Therefore, our data strongly suggest that thermally unstable proteins generated in the cytosol can cause cellular damage by coming into direct contact with mitochondria. More importantly, we revealed that this damage is not amyloid-specific. |
| 巻・号 | 23(17) |
| 公開日 | 2022-8-31 |
| DOI | 10.3390/ijms23179881 |
| PII | ijms23179881 |
| PMID | 36077279 |
| PMC | PMC9456338 |
| MeSH | Amyloid* / metabolism Amyloidosis* / metabolism Cytosol / metabolism Homeostasis Humans Mitochondria / metabolism Mitochondrial Proteins / genetics Mitochondrial Proteins / metabolism |
| IF | 4.556 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 1 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| ヒト・動物細胞 | HeLa(RCB0007) |