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Substrate stiffness regulates temporary NF-kappa B activation via actomyosin contractions
| Title: | Substrate stiffness regulates temporary NF-kappa B activation via actomyosin contractions |
| Authors: | Ishihara, Seiichiro Browse this author | | Yasuda, Motoaki Browse this author →KAKEN DB | | Mizutani, Takeomi Browse this author →KAKEN DB | | Kawabata, Kazushige Browse this author →KAKEN DB | | Haga, Hisashi Browse this author →KAKEN DB |
| Keywords: | Actomyosin | | Lung adenocarcinoma cell | | NF-kappa B | | Mechanotransduction | | Substrate stiffness |
| Issue Date: | 15-Nov-2013 |
| Publisher: | Elsevier inc |
| Journal Title: | Experimental cell research |
| Volume: | 319 |
| Issue: | 19 |
| Start Page: | 2916 |
| End Page: | 2927 |
| Publisher DOI: | 10.1016/j.yexcr.2013.09.018 |
| PMID: | 24113574 |
| Abstract: | Physical properties of the extracellular matrix (ECM) can control cellular phenotypes via mechanotransduction, which is the process of translation of mechanical stresses into biochemical signals. While current research is clarifying the relationship between mechanotransduction and cytoskeleton or adhesion complexes, the contribution of transcription factors to mechanotransduction is not well understood. The results of this study revealed that the transcription factor NF-kappa B, a major regulator for immunoreaction and cancer progression, is responsive to substrate stiffness. NF-kappa B activation was temporarily induced in H1299 lung adenocarcinoma cells grown on a stiff substrate but not in cells grown on a soft substrate. Although the activation of NF-kappa B was independent of the activity of integrin beta 1, an ECM-binding protein, the activation was dependent on actomyosin contractions induced by phosphorylation of myosin regulatory light chain (MRLC). Additionally, the inhibition of MRLC phosphorylation by Rho kinase inhibitor Y27632 reduced the activity of NF-kappa B. We also observed substrate-specific morphology of the cells, with cells grown on the soft substrate appearing more rounded and cells grown on the stiff substrate appearing more spread out. Inhibiting NF-kappa B activation caused a reversal of these morphologies on both substrates. These results suggest that substrate stiffness regulates NF-kappa B activity via actomyosin contractions, resulting in morphological changes. (C) 2013 Elsevier Inc. All rights reserved. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/57311 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 芳賀 永
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