Reducing agents mitigate protein synthesis inhibition mediated by vanadate and vanadyl compounds in reticulocyte lysates

Archives of Biochemistry and Biophysics
T KrishnamoorthyKolluru V A Ramaiah

Abstract

Recently, we synthesized and characterized vanadyl saccharides to evaluate the effects of various vanadate and vanadyl complexes, which differ in their oxidation states on various biomacromolecules and cellular activities (1, 2). Here, we report that both vanadate (+V oxidation state) and different vanadyl species (+IV oxidation state) such as vanadyl D-glucose, vanadyl diascorbate, and vanadyl sulfate, impair the formation of polysomes and inhibit the initiation of protein synthesis in hemin-supplemented rabbit reticulocyte lysates. Vanadate inhibits protein synthesis more severely than vanadyl species and is consistent with the idea that vanadate is reduced to vanadyl state intracellularly. The inhibition of protein synthesis caused by low concentrations (10-20 microM) of vanadate and vanadyl species is effectively mitigated by reducing agents such as dithiothreitol, reduced glutathione (GSH), or reduced pyridine dinucleotide. A significant decrease in the protein synthesis inhibition in vanadate-treated lysates by GSH suggests that the mechanism of protein synthesis inhibition by vanadate is different than the action of other oxidants such as heavy metal ions and oxidized glutathione. This suggestion is also consistent with ...Continue Reading

References

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