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@ARTICLE{Chan:281432,
      author       = {Chan, Chii J. and Ekpenyong, Andrew E. and Golfier, S. and
                      Li, Wenhong and Chalut, Kevin J. and Otto, Oliver and
                      Elgeti, Jens and Guck, Jochen and Lautenschlager, Franziska},
      title        = {{M}yosin {II} {A}ctivity {S}oftens {C}ells in {S}uspension},
      journal      = {Biophysical journal},
      volume       = {108},
      number       = {8},
      issn         = {0006-3495},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {FZJ-2016-01125},
      pages        = {1856-1869},
      year         = {2015},
      abstract     = {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.},
      cin          = {IAS-2 / ICS-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IAS-2-20090406 / I:(DE-Juel1)ICS-2-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000353344400005},
      pubmed       = {pmid:25902426},
      doi          = {10.1016/j.bpj.2015.03.009},
      url          = {https://juser.fz-juelich.de/record/281432},
}