論文 - 詳細
| RRC ID | 68806 |
|---|---|
| 著者 | Nagahama M, Kobayashi K, Takehara M. |
| タイトル | Cathepsin Release from Lysosomes Promotes Endocytosis of Clostridium perfringens Iota-Toxin. |
| ジャーナル | Toxins (Basel) |
| Abstract |
Iota-toxin from Clostridium perfringens type E is a binary toxin composed of two independent proteins: actin-ADP-ribosylating enzyme component, iota-a (Ia), and binding component, iota-b (Ib). Ib binds to target cell receptors and mediates the internalization of Ia into the cytoplasm. Extracellular lysosomal enzyme acid sphingomyelinase (ASMase) was previously shown to facilitate the internalization of iota-toxin. In this study, we investigated how lysosomal cathepsin promotes the internalization of iota-toxin into target cells. Cysteine protease inhibitor E64 prevented the cytotoxicity caused by iota-toxin, but aspartate protease inhibitor pepstatin-A and serine protease inhibitor AEBSF did not. Knockdown of lysosomal cysteine protease cathepsins B and L decreased the toxin-induced cytotoxicity. E64 suppressed the Ib-induced ASMase activity in extracellular fluid, showing that the proteases play a role in ASMase activation. These results indicate that cathepsin B and L facilitate entry of iota-toxin via activation of ASMase. |
| 巻・号 | 13(10) |
| 公開日 | 2021-10-12 |
| DOI | 10.3390/toxins13100721 |
| PII | toxins13100721 |
| PMID | 34679014 |
| PMC | PMC8537257 |
| MeSH | ADP Ribose Transferases / pharmacology* Animals Bacterial Toxins / pharmacology* Cathepsin B / metabolism Cathepsin L / metabolism Clostridium perfringens Cysteine Proteinase Inhibitors / metabolism Dogs Endocytosis / drug effects* Lysosomes / metabolism Madin Darby Canine Kidney Cells Sphingomyelin Phosphodiesterase / metabolism* |
| IF | 3.531 |
| 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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| 各媒体での言及数の合計 | 0 |
| リソース情報 | |
| ヒト・動物細胞 | MDCK(RCB0995) |