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Irreversibly sickled cell β‐actin: Defective filament formation
Author(s) -
Shartava Archil,
Korn William,
Shah Arvind K.,
Goodman Steven R.
Publication year - 1997
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/(sici)1096-8652(199706)55:2<97::aid-ajh8>3.0.co;2-y
Subject(s) - spectrin , actin , actina , actin remodeling , chemistry , biophysics , cytoskeleton , protein filament , cysteine , actin binding protein , microbiology and biotechnology , cell , biochemistry , actin cytoskeleton , biology , enzyme
It has been demonstrated that cysteine modification in irreversibly sickled cell β‐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 β‐actin polymerizes and depolymerizes more slowly than control β‐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 cysteine 264 and cysteine 373 in β‐actin. Am. J. Hematol. 55:97‐103, 1997. © 1997 Wiley‐Liss, Inc.