ArticleCellular and molecular bioengineering2014
Mathematical modeling of the dynamic mechanical behavior of neighboring sarcomeres in actin stress fibers.
Article in Cellular and molecular bioengineering, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Mechanical deformation and death of circulating tumor cells in the bloodstream.Cancer metastasis reviews · 2024Review
- Titin-mediated thick filament activation stabilizes myofibrils on the descending limb of their force-length relationship.Journal of sport and health science · 2018Article
- A biomechanical perspective on stress fiber structure and function.Biochimica et biophysica acta · 2015Review
- Cardiomyocyte subdomain contractility arising from microenvironmental stiffness and topography.Biomechanics and modeling in mechanobiology · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Actin stress fibers (SFs) in live cells consist of series of dynamic individual sarcomeric units. Within a group of consecutive SF sarcomeres, individual sarcomeres can spontaneously shorten or lengthen without changing the overall length of this group, but the underlying mechanism is unclear. We used a computational model to test our hypothesis that this dynamic behavior is inherent to the heterogeneous mechanical properties of the sarcomeres and the cytoplasmic viscosity. Each sarcomere was modeled as a discrete element consisting of an elastic spring, a viscous dashpot and an active contractile unit all connected in parallel, and experiences forces as a result of actin filament elastic stiffness, myosin II contractility, internal viscoelasticity, or cytoplasmic drag. When all four types of forces are considered, the simulated dynamic behavior closely resembles the experimental observations, which include a low-frequency fluctuation in individual sarcomere length and compensatory lengthening and shortening of adjacent sarcomeres. Our results suggest that heterogeneous stiffness and viscoelasticity of actin fibers, heterogeneous myosin II contractility, and the cytoplasmic drag are sufficient to cause spontaneous fluctuations in SF sarcomere length. Our results shed new light to the dynamic behavior of SF and help design experiments to further our understanding of SF dynamics.
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