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1 Physiology Program, Harvard School of Public Health, Boston, MA, USA
2 Physics Department, Erlangen University, Erlangen, Germany
3 Unitat Biofisica i Bioenginyeria, Facultat Medicina, Universitat Barcelona - IDIBAPS, Barcelona, Spain
* To whom correspondence should be addressed. E-mail: mpuigdem{at}hsph.harvard.edu.
We probed elastic and loss moduli in the adherent human airway smooth muscle cell through a variety of receptor systems, each serving as a different molecular window on cytoskeletal dynamics. Coated magnetic microbeads were attached to the cell surface via coating-receptor binding. A panel of bead coatings was investigated: a peptide containing the sequence RGD, vitronectin, urokinase, activating antibody against 
1 integrin, non-activating antibody against 1 integrin, blocking antibody against 1 integrin, antibody against 3 integrin, and acetylated-low density lipoprotein. An oscillatory mechanical torque was applied to the bead and resulting lateral displacements were measured at baseline, after actin disruption by cytochalasin D, or after contractile activation by histamine. As expected, mechanical moduli depended strongly upon bead type and bead-coating, differing at the extremes by as much as two orders of magnitude. In every case, however, elastic and loss moduli increased with frequency, f, as a weak power law, fx-1. Moreover, with few exceptions data could be scaled such that suitably normalized elastic and frictional responses depended solely on the power law exponent x. Taken together, these data suggest that power law behavior represents a generic feature of underlying protein-protein dynamics.
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