title: Red blood cell membrane fluctuations and shape controlled by ATP-induced cytoskeletal defects.
abstract: 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.
authors.affiliation: Department of Materials and Interfaces, The Weizmann Institute of Science, Rehovot 76100, Israel. nirgov@wisemail.weizmann.ac.il
authors.forename: N S
authors.initials: NS
authors.lastname: Gov
authors.forename: S A
authors.initials: SA
authors.lastname: Safran
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002478:Cells, Cultured; D003198:Computer Simulation; D003599:Cytoskeleton / Q000737:chemistry / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008560:Membrane Fluidity / Q000502:physiology*; D008954:Models, Biological; D008956:Models, Chemical; D011485:Protein Binding; D013314:Stress, Mechanical
chemical_list: D000255:Adenosine Triphosphate