Myosin II Activity Softens Cells in Suspension

The cellular cytoskeleton is crucial for many cellular functions such as cell motility and wound healing, as well as other processes that require shape change or force generation. Actin is one cytoskeleton component that regulates cell mechanics. Important properties driving this regulation include...

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Bibliographic Details
Published in:Biophysical journal 2015-04, Vol.108 (8), p.1856-1869
Main Authors: Chan, Chii J., Ekpenyong, Andrew E., Golfier, Stefan, Li, Wenhong, Chalut, Kevin J., Otto, Oliver, Elgeti, Jens, Guck, Jochen, Lautenschläger, Franziska
Format: Article
Language:English
Subjects:
3T3 Cells
Actin Cytoskeleton - chemistry
Actin Cytoskeleton - metabolism
Animals
Cell Adhesion
Cell Biophysics
Cell division
Cell Membrane - metabolism
Cell Membrane - ultrastructure
Cells
Cytoskeleton
Elasticity
HeLa Cells
Humans
Mice
Microfluidics
Motility
Myosin Type II - chemistry
Myosin Type II - metabolism
Wound healing
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Summary:The cellular cytoskeleton is crucial for many cellular functions such as cell motility and wound healing, as well as other processes that require shape change or force generation. Actin is one cytoskeleton component that regulates cell mechanics. Important properties driving this regulation include the amount of actin, its level of cross-linking, and its coordination with the activity of specific molecular motors like myosin. While studies investigating the contribution of myosin activity to cell mechanics have been performed on cells attached to a substrate, we investigated mechanical properties of cells in suspension. To do this, we used multiple probes for cell mechanics including a microfluidic optical stretcher, a microfluidic microcirculation mimetic, and real-time deformability cytometry. We found that nonadherent blood cells, cells arrested in mitosis, and naturally adherent cells brought into suspension, stiffen and become more solidlike upon myosin inhibition across multiple timescales (milliseconds to minutes). Our results hold across several pharmacological and genetic perturbations targeting myosin. Our findings suggest that myosin II activity contributes to increased whole-cell compliance and fluidity. This finding is contrary to what has been reported for cells attached to a substrate, which stiffen via active myosin driven prestress. Our results establish the importance of myosin II as an active component in modulating suspended cell mechanics, with a functional role distinctly different from that for substrate-adhered cells.
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2015.03.009