| Literature DB >> 15040427 |
Abstract
The irreversibly sickled cell (ISC) is poorly deformable, dehydrated, of short life span, correlated to hemolysis, and a contributor to the pathophysiology of vaso-occlusive (VOC) episodes. The altered redox status and increased oxygen radical levels within high density sickle cells leads to oxidative damage and glutathiolation of cysteine residues. The formation of a disulfide bridge between Cys 284 and Cys 373 in ISC beta-actin leads to actin filaments which depolymerize poorly at 37 degrees C. Glutathiolation of cysteines within spectrin results in this key membrane skeletal protein losing it's E2/E3 ubiquitin-ligating/conjugating activity and therefore ability to self ubiquitinate. The resulting loss of ubiquitination in ISC alpha-spectrin repeats 20/21 causes a higher affinity ISC spectrin-4.1-actin ternary complex. Therefore, reversible oxidative damage to beta-actin and loss of ubiquitination of alpha-spectrin leads to an ISC membrane skeleton that disassembles poorly at 37 degrees C. The result is a membrane skeleton which is "locked" because it cannot disassemble or reassemble. N-acetylcysteine (NAC) is an antioxidant which raises intracellular reduced glutathione levels, and blocks the formation of ISCs in vitro. NAC, in a phase II human trial, caused a downward trend in ISCs, significantly decreased dense cells, and substantially decreased the rate of VOC episodes.Entities:
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Year: 2004 PMID: 15040427
Source DB: PubMed Journal: Cell Mol Biol (Noisy-le-grand) ISSN: 0145-5680 Impact factor: 1.770