HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Zaner, K. S. Search for Related Content PubMed PubMed Citation Articles by Zaner, K. S. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 261, Issue 17, 7615-7620, Jun, 1986

The effect of the 540-kilodalton actin cross-linking protein, actin- binding protein, on the mechanical properties of F-actin

KS Zaner

This study describes the effect of actin-binding protein derived from rabbit lung macrophages on the mechanical properties of F-actin. The dynamic storage modulus, G'(omega), and loss modulus, G"(omega) of F- actin, at concentrations from 1 to 4 mg/ml, in the absence or presence of actin-binding protein at molar ratios to actin of 1:1000 to 1:125, were measured at frequencies ranging from 3 X 10(-3) to 0.5 Hz. Actin- binding protein increased the dynamic moduli of F-actin, but this increase was much greater as either the actin-binding protein/actin ratio or the total protein concentration increased. Moreover, there was a convergence of the values of G' and G" at high frequencies for F- actin which became more prominent upon the addition of actin-binding protein. The value of the modulus obtained by an extrapolation of these data to actin concentrations similar to that found in the cell cortex was close to values which have been obtained by direct measurements. The addition of actin-binding protein to an F-actin solution enabled it to reach an equilibrium strain following the application of a stress, in contrast to pure F-actin. These data allow a more rigorous definition of the "sol" to "gel" transition and suggest that the cross- linking of actin filaments by actin-binding protein leads to the formation of a network structure whose underlying mechanism of mechanical behavior is short range intrafilament bending in contrast to the classical rubber network.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. Puig-de-Morales-Marinkovic, K. T. Turner, J. P. Butler, J. J. Fredberg, and S. Suresh Viscoelasticity of the human red blood cell Am J Physiol Cell Physiol, August 1, 2007; 293(2): C597 - C605. [Abstract] [Full Text] [PDF]

				M. F. Coughlin, M. Puig-de-Morales, P. Bursac, M. Mellema, E. Millet, and J. J. Fredberg Filamin-A and Rheological Properties of Cultured Melanoma Cells Biophys. J., March 15, 2006; 90(6): 2199 - 2205. [Abstract] [Full Text] [PDF]

				Y. Tseng, K. M. An, O. Esue, and D. Wirtz The Bimodal Role of Filamin in Controlling the Architecture and Mechanics of F-actin Networks J. Biol. Chem., January 16, 2004; 279(3): 1819 - 1826. [Abstract] [Full Text] [PDF]

				R. Kiefmann, K. Heckel, M. Dorger, S. Schenkat, M. Stoeckelhuber, J. Wesierska-Gadek, and A. E. Goetz Role of poly(ADP-ribose) synthetase in pulmonary leukocyte recruitment Am J Physiol Lung Cell Mol Physiol, November 1, 2003; 285(5): L996 - L1005. [Abstract] [Full Text] [PDF]

				D. Provance, A McDowall, M Marko, and K Luby-Phelps Cytoarchitecture of size-excluding compartments in living cells J. Cell Sci., January 10, 1993; 106(2): 565 - 577. [Abstract] [PDF]