Irreversibly sickled cell beta-actin: defective filament formation.
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.
Mesh Terms:
Actins, Anemia, Sickle Cell, Humans, Microfilaments, Microscopy, Electron, Polymers, Protein Binding, Spectrin
Actins, Anemia, Sickle Cell, Humans, Microfilaments, Microscopy, Electron, Polymers, Protein Binding, Spectrin
Am. J. Hematol.
Date: Jun. 01, 1997
PubMed ID: 9209005
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