2012年5月
Cofilin is required for organization of sarcomeric actin filaments in chicken skeletal muscle cells
CYTOSKELETON
- ,
- ,
- 巻
- 69
- 号
- 5
- 開始ページ
- 290
- 終了ページ
- 302
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1002/cm.21025
- 出版者・発行元
- WILEY
Cofilin is an actin regulatory protein that plays a critical role in actin filament dynamics in a variety of cells. We have previously demonstrated that excess cofilin in skeletal muscle cells leads to disruption of actin filaments, followed by actin-cofilin rod formation in the cytoplasm. In this study, to further clarify the role of cofilin in actin assembly during myofibrillogenesis, cofilin expression was suppressed in cultured chicken skeletal muscle cells. First, we confirmed that turnover of cofilin in myotubes was much higher than that of actin, and that the cofilin level could be decreased drastically within 2 days when cofilin de novo synthesis was suppressed. Next, cofilin expression in individual myotubes was suppressed by introducing antisense morpholino oligonucleotides into the cells by microinjection. Cofilin depletion at the early phase of myofibrillogenesis caused abnormal actin aggregates in myotubes and impaired actin organization into cross-striated myofibril structures. However, when cofilin expression was suppressed in developed myotubes, actin localization in striated myofibrils was scarcely affected. These results indicate that cofilin plays a critical role in the regulation of actin assembly at the early process of myofibrillogenesis. (C) 2012 Wiley Periodicals, Inc
- リンク情報
- ID情報
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- DOI : 10.1002/cm.21025
- ISSN : 1949-3584
- eISSN : 1949-3592
- Web of Science ID : WOS:000304083300003