Abstract

The effect of sodium molybdate on the stability and activation of the glucocorticoid receptor from chick and rat thymus were investigated. Molybdate, at a concentration range of 1–10 mM, blocked denaturation of the cytosol receptor by elevated (25 and 37°C) temperatures. This effect could be observed only with the aggregated (low-salt) form of the receptor. Molybdate also inhibited transformation of the receptor-hormone complex to the DNA-binding state which occurs either with incubation at 25°C or with salt treatment. The inhibitory effect of molybdate could be observed only on the non-activated receptor; nuclear- and DNA-binding of the activated receptor was not significantly changed by molybdate. Both effects were concentration-dependent. Molybdate had no effect on the activation of the partially purified glucocorticoid receptor. Molybdate effect was also examined using intact lymphocytes. Sodium molybdate had no effect either on the steroid binding of whole cells or on the nuclear transfer of the hormone-receptor complex. While the mechanism of molybdate action remains unknown the results of experiments on purified receptor suggest that molybdate does not act directly on the receptor molecule; rather through some cytosol factor(s). However, these effects could only be seen in cell-free experiments, and not during the conditions of the living cell.

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