ArticleProceedings of the National Academy of Sciences of the United States of America1990
Liquid crystal domains and thixotropy of filamentous actin suspensions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Form and function in biological filaments: a physicist's review.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025Review
- What do we know about growth of vessel elements of secondary xylem in woody plants?Biological reviews of the Cambridge Philosophical Society · 2021Review
- Emergent complexity of the cytoskeleton: from single filaments to tissue.Advances in physics · 2013Review
- Two-dimensional periodic texture of actin filaments formed upon drying.Biophysics (Nagoya-shi, Japan) · 2011Article
- Real-time monitoring of cell elasticity reveals oscillating myosin activity.Biophysical journal · 2010Article
- Apparent thixotropic properties of saline/glycerol drops with biotinylated antibodies on streptavidin-coated glass slides: implications for bacterial capture on antibody microarrays.Sensors (Basel, Switzerland) · 2009Article
- The interplay between viscoelastic and thermodynamic properties determines the birefringence of F-actin gels.Biophysical journal · 2005Article
- Mechanical behavior in living cells consistent with the tensegrity model.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Cryoatomic force microscopy of filamentous actin.Biophysical journal · 2000Article
- Tracer diffusion through F-actin: effect of filament length and cross-linking.Biophysical journal · 1996Article
- The bundling of actin with polyethylene glycol 8000 in the presence and absence of gelsolin.Biophysical journal · 1996Article
- Theoretical estimates of mechanical properties of the endothelial cell cytoskeleton.Biophysical journal · 1996Article
- Transformation of actin-encapsulating liposomes induced by cytochalasin D.Biophysical journal · 1994Article
- Local measurements of viscoelastic moduli of entangled actin networks using an oscillating magnetic bead micro-rheometer.Biophysical journal · 1994Article
- A 27,000-D core of the Dictyostelium 34,000-D protein retains Ca(2+)-regulated actin cross-linking but lacks bundling activity.The Journal of cell biology · 1993Article
- Quantitation of liquid-crystalline ordering in F-actin solutions.Biophysical journal · 1992Article
- Viscoelastic properties of vimentin compared with other filamentous biopolymer networks.The Journal of cell biology · 1991Article
- Growth cone behavior and production of traction force.The Journal of cell biology · 1990Article
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5 authors.
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Abstract
The thixotropic properties of filamentous actin suspensions were examined by a step-function shearing protocol. Samples of purified filamentous actin were sheared at 0.2 sec-1 in a cone and plate rheometer. We noted a sharp stress overshoot upon the initiation of shear, indicative of a gel state, and a nearly instantaneous drop to zero stress upon cessation of shear. Stress-overshoot recovery was almost complete after 5 min of "rest" before samples were again sheared at 0.2 sec-1. Overshoot recovery increased linearly with the square root of rest time, suggesting that gel-state recovery is diffusion limited. Actin suspensions subjected to oscillatory shearing at frequencies from 0.003 to 30 radians/sec confirmed the existence of a 5-min time scale in the gel, similar to that for stress-overshoot recovery. Flow of filamentous actin was visualized by polarized light observations. Actin from 6 mg/ml to 20 mg/ml showed the "polycrystalline" texture of birefringence typical for liquid crystal structure. At shear rates less than 1 sec-1, flow occurred by the relative movement of irregular, roughly ellipsoidal actin domains 40-140 microns long; the appearance was similar to moving ice floes. At shear rates greater than 1 sec-1, domains decreased in size, possibly by frictional interactions among domains. Eventually domains flow in a "river" of actin aligned by the flow. Our observations confirm our previous domain-friction model for actin rheology. The similarities between the unusual flow properties of actin and cytoplasm argue that cytoplasm also may flow as domains.
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