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. 1999 Apr;76(4):2208–2215. doi: 10.1016/S0006-3495(99)77376-5

Thiol oxidation of actin produces dimers that enhance the elasticity of the F-actin network.

J X Tang 1, P A Janmey 1, T P Stossel 1, T Ito 1
PMCID: PMC1300193  PMID: 10096915

Abstract

Slow oxidation of sulfhydryls, forming covalently linked actin dimers and higher oligomers, accounts for increases in the shear elasticity of purified actin observed after aging. Disulfide-bonded actin dimers are incorporated into F-actin during polymerization and generate cross-links between actin filaments. The large gel strength of oxidized actin (>100 Pa for 1 mg/ml) in the absence of cross-linking proteins falls to within the theoretically predicted order of magnitude for uncross-linked actin filament networks (1 Pa) with the addition of sufficient concentrations of reducing agents such as 5 mM dithiothreitol or 10 mM beta-mercaptoethanol. As little as 1 gelsolin/1000 actin subunits also lowers the high storage modulus of oxidized actin. The effects of gelsolin may be both to increase filament number as it severs F-actin and to cover the barbed end of an actin filament, which otherwise might cross-link to the side of another filament via an actin dimer. These new findings may explain why previous studies of actin rheology report a wide range of values when purified actin is polymerized without added regulatory proteins.

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Selected References

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