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Originally published as Biophys J. BioFAST on December 21, 2004.
doi:10.1529/biophysj.104.045328
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Biophysical Journal 88:1859-1874 (2005)
© 2005 The Biophysical Society

Red Blood Cell Membrane Fluctuations and Shape Controlled by ATP-Induced Cytoskeletal Defects

N. S. Gov * and S. A. Safran {dagger}

* Department of Materials and Interfaces, and {dagger} Department of Chemical Physics, The Weizmann Institute of Science, Rehovot, Israel

Correspondence: Address reprint requests to Dr. Nir S. Gov, Weizmann Institute of Science, Dept. of Chemical Physics, P.O.B. 26, Rehovot 76100, Israel. Tel.: 972-8-934-3323; E-mail: nirgov{at}wisemail.weizmann.ac.il.

We show theoretically how adenosine 5'-triphosphate (ATP)-induced dynamic dissociations of spectrin filaments (from each other and from the membrane) in the cytoskeleton network of red blood cells (RBC) can explain in a unified manner both the measured fluctuation amplitude as well as the observed shape transformations as a function of intracellular ATP concentration. Static defects can be induced by external stresses such as those present when RBCs pass through small capillaries. We suggest that the partially freed actin at these defect sites may explain the activation of the CFTR membrane-bound protein and the subsequent release of ATP by RBCs subjected to deformations. Our theoretical predictions can be tested by experiments that measure the correlation between variations in the binding of actin to spectrin, the activity of CFTR, and the amount of ATP released.




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