Irreversibly sickled cell β-actin

Defective filament formation

Archil Shartava, William Korn, Arvind K. Shah, Steven Goodman

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

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 Bio 128:805812, 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 ere due to the structural modification caused by the disulfide bridge between cysteine284 and cysteine373 in β-actin.

Original languageEnglish (US)
Pages (from-to)97-103
Number of pages7
JournalAmerican Journal of Hematology
Volume55
Issue number2
DOIs
StatePublished - Jun 1 1997
Externally publishedYes

Fingerprint

Actin Cytoskeleton
Actins
Spectrin
Skeleton
Disulfides
Cysteine
Polymers
Cell Membrane
Electrons
Membranes

All Science Journal Classification (ASJC) codes

  • Hematology

Cite this

Irreversibly sickled cell β-actin : Defective filament formation. / Shartava, Archil; Korn, William; Shah, Arvind K.; Goodman, Steven.

In: American Journal of Hematology, Vol. 55, No. 2, 01.06.1997, p. 97-103.

Research output: Contribution to journalArticle

Shartava, Archil ; Korn, William ; Shah, Arvind K. ; Goodman, Steven. / Irreversibly sickled cell β-actin : Defective filament formation. In: American Journal of Hematology. 1997 ; Vol. 55, No. 2. pp. 97-103.
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