Pyridoxal-5-phosphate affects glucocorticoid receptors in intact lymphocytes similarly as in cell-free systems

Pyridoxal-5-phosphate markedly decreased the heat-stability of the unbound thymus cytosol receptor as well as that of the receptor-[3H]-triamcinolone acetonide complex in cell-free systems. Treatment with pyridoxal phosphate also decreased DNA-binding of the complex, being present either before or after heat- and salt-activation. 5 mM pyridoxal phosphate was required for 50% inhibition of DNA-binding. Pyridoxine, at similar concentrations, had no inhibitory effect. Pre-incubation of intact thymocytes with 10 mM pyridoxine caused also a marked decrease in the binding of [3H]-triamcinolone acetonide by the cells. Treating the cells with liposomes containing 1-100 mM pyridoxal phosphate caused an increase in intracellular pyridoxal phosphate concentration by about 0.1-10 microM and a decrease in [3H]-triamcinolone acetonide binding of the cells by about 50%. The results suggest that 1. pyridoxal phosphate acts not only on the activated but also on the unbound and non-activated forms of glucocorticoid receptor in cell-free systems; 2. pyridoxal phosphate has a similar effect in the intracellular millieu and thus, 3. pyridoxal phosphate might act as a physiologic regulator of the steroid hormone action.