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A Posttranslational Modification of/3-Actin Contributes to the Slow Dissociation of the Spectrin-Protein 4.1-Actin Complex of Irreversibly Sickled Cells

By Rick Gussio, Linda A. Casoria-scott, Arvind K. Shah, Christine A. Heuerman and Steven R. Goodman*ll


Abstract. Irreversibly sickled cells (ISCs) remain sickled even under conditions where they are well oxygenated and hemoglobin is depolymerized. In our studies we demonstrate that triton extracted ISC core skeletons containing only spectrin, protein 4.1, and actin also retain their sickled shape; while reversibly sickled cell (RSC) skeletons remodel to a round or biconcave shape. We also demonstrate that these triton extracted ISC core skeletons dissociate more slowly upon incubation at 37°C than do RSC or control (AA) core skeletons. This observation may supply the basis for the inability of the ISC core skeleton to remodel its shape. Using an in vitro ternary complex dissocia-T HE molecular events which occur within red blood cells (RBCs) ' from homozygous sickle cell (SS) patients, and to their extracellular environment, leading to the painful sickle cell crisis, organ damage, and mortality have been of great interest to the clinical and scientific communit

Year: 2013
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