Protein S-thiolation in cultured hepatocytes and human neutrophils

TL;DRAbstract

Protein S-thiolation was characterized in cultured hepatocytes treated with t-butyl hydroperoxide, menadione and phorbol diester-stimulated neutrophils. A similar group of soluble proteins was quickly S-thiolated in oxidant-treated hepatocytes and glutathione contributed at least 90% of the total protein-bound thiols. In hepatocytes treated with 0.5 mM t-butyl hydroperoxide, 0.2 mM menadione or 10[superscript]6 neutrophils, the maximum amount of protein-bound thiols was shown to be approximately 10%, 24% and 8% of cellular glutathione respectively bound to proteins. The most abundant S-thiolated 30 kDa protein in hepatocytes was identified as carbonic anhydrase III in all cases. In oxidant-treated cells carbonic anhydrase III contributed 30% of the total amount of protein-bound thiols. Two major S-thiolated proteins, (46 and 62 kDa) were observed in untreated hepatocytes and S-thiolation of these two proteins was not increased by the addition of oxidants to cells. The amount of protein

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