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  • Title: Irreversibly sickled cell beta-actin: defective filament formation.
    Author: Shartava A, Korn W, Shah AK, Goodman SR.
    Journal: Am J Hematol; 1997 Jun; 55(2):97-103. PubMed ID: 9209005.
    Abstract:
    It has been demonstrated that cysteine modification in irreversibly sickled cell beta-actin slows down the remodeling of membrane skeletons [Shartava et al.: J Cell Biol 128:805-812, 1995]. This slow remodeling can be due to alterations in spectrin-actin binding and/or actin-actin interactions in irreversibly sickled cell (ISC) membrane skeletons. In these studies we demonstrate that ISC actin binds spectrin normally. However, ISC beta-actin polymerizes and depolymerizes more slowly than control beta-actin, and forms unusual aggregates when placed under polymerizing conditions. Electron microscopic analysis of actin polymers indicated that ISC actin generates a large amount of aggregates which we conclude are due to the structural modification caused by the disulfide bridge between cysteine284 and cysteine373 in beta-actin.
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