Live cell tracking of symmetry break in actin cytoskeleton triggered by abrupt changes in micromechanical environments
Source abstract
Abstract
With the aid of stimulus-responsive hydrogel substrates composed of ABA triblock copolymer micelles, we monitored the morphological dynamics of myoblast (C2C12) cells in response to an abrupt change in the substrate elasticity by live cell imaging. The remodeling of actin cytoskeletons could be monitored by means of transient transfection with LifeAct-GFP. Dynamic changes in the orientational order of actin filaments were characterized by an order parameter, which enables one to generalize the mechanically induced actin cytoskeletons as a break of symmetry. The critical role that acto-myosin complexes play in the morphological transition was verified by the treatment of cells with myosin II inhibitor (blebbistatin) and the fluorescence localization of focal adhesion contacts. Such dynamically tunable hydrogels can be utilized as in vitro cellular micro-environments that can exert time-dependent stimuli to mechanically regulate target cells.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Cellular Mechanics and Interactions · 3D Printing in Biomedical Research · Microtubule and mitosis dynamics
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Physical Chemistry of Biosystems
Institute of Physical Chemistry
University of Heidelberg
D69120 Heidelberg
Germany
Institute for Integrated Cell-Material Sciences (WPI iCeMS)
Kyoto University
Kyoto 606-8501
Japan
Department of Chemistry
Saitama University
Saitama 338-8570
Dainton Building
University of Sheffield
Sheffield
UK
Biocompatibles UK Ltd
Camberley
Funding
Japan Society for the Promotion of Science · Ministry of Education, Culture, Sports, Science, and Technology · Deutsche Forschungsgemeinschaft
References (29)
Show source-provided references
1. Vogel · Nat. Rev. Mol. Cell Biol. · 2006 · 7 · 26510.1038/nrm1890 ↗
2. Discher · Science · 2005 · 310 · 113910.1126/science.1116995 ↗
3. Engler · Biophys. J. · 2004 · 86 · 61710.1016/S0006-3495(04)74140-5 ↗
4. Kidoaki · J. Biotechnol. · 2008 · 133 · 22510.1016/j.jbiotec.2007.08.015 ↗
5. Wen · Nat. Mater. · 2014 · 13 · 97910.1038/nmat4051 ↗
6. Georges · Biophys. J. · 2006 · 90 · 301210.1529/biophysj.105.073114 ↗
7. Lo · Biophys. J. · 2000 · 79 · 14410.1016/S0006-3495(00)76279-5 ↗
8. Gray · J. Biomed. Mater. Res., Part A · 2003 · 66A · 60510.1002/jbm.a.10585 ↗
9. Pelham · Proc. Natl. Acad. Sci. U. S. A. · 1997 · 94 · 1366110.1073/pnas.94.25.13661 ↗
10. Winer · Tissue Eng., Part A · 2008 · 15 · 14710.1089/ten.tea.2007.0388 ↗
11. Engler · Cell · 2006 · 126 · 67710.1016/j.cell.2006.06.044 ↗
12. Simmons · Bone · 2004 · 35 · 56210.1016/j.bone.2004.02.027 ↗
13. Wolf · J. Cell Biol. · 2003 · 160 · 26710.1083/jcb.200209006 ↗
14. Burdick · Nat. Commun. · 2012 · 3 · 126910.1038/ncomms2271 ↗
15. Shu · Biomacromolecules · 2002 · 3 · 130410.1021/bm025603c ↗
16. Hörning · Biophys. J. · 2012 · 102 · 37910.1016/j.bpj.2011.12.018 ↗
17. Shu · J. Biomed. Mater. Res., Part A · 2006 · 79A · 90210.1002/jbm.a.30831 ↗
18. Yoshikawa · J. Am. Chem. Soc. · 2011 · 133 · 136710.1021/ja1060615 ↗
19. Zemel · Nat. Phys. · 2010 · 6 · 46810.1038/nphys1613 ↗
20. Yoshikawa · J. Phys. Chem. B · 2013 · 117 · 408110.1021/jp4008224 ↗
21. Ma · Biomacromolecules · 2003 · 4 · 86410.1021/bm034118u ↗
22. Madsen · Biomacromolecules · 2008 · 9 · 226510.1021/bm8005006 ↗
23. A. W. Adamson , Physical Chemistry of Surfaces, Wiley, 1990
24. Otsu · IEEE Trans. Syst. Man Cybern. · 1979 · 9 · 6210.1109/TSMC.1979.4310076 ↗
25. Simson · Biophys. J. · 1998 · 74 · 51410.1016/S0006-3495(98)77808-7 ↗
26. R. Bruinsma , in Proceedings of the NATO Advanced Institute of Physics and Biomaterials, NATO Advanced Study Institute Series B: Physics, Kluwer, London, 1995
27. Gönnenwein · Biophys. J. · 2003 · 48 · 64610.1016/S0006-3495(03)74508-1 ↗
28. Kovács · J. Biol. Chem. · 2004 · 279 · 3555710.1074/jbc.M405319200 ↗
29. Allingham · Nat. Struct. Mol. Biol. · 2005 · 12 · 37810.1038/nsmb908 ↗