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Comparison of glucocorticoid receptors in two rat hepatoma cell lines with different sensitivities to glucocorticoids and antiglucocorticoids.

Two independently derived rat hepatoma cell lines, HTC and Fu5-5, differ in their sensitivities to both glucocorticoids and antiglucocorticoids, despite virtually identical number and affinity of glucocorticoid receptors. The present study further examined both receptors for differences that could account for the nonidentical responses of the two cell lines. HTC and Fu5-5 cell receptors that were covalently labeled with [3H] dexamethasone 21-mesylate ([3H]DM) had the same mol wt of about 97,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the same isoelectric point of about 6.4 by nonequilibrium pH gradient electrophoresis. Limited proteolysis of receptor-[3H]DM complexes with three different proteases generated identical protease-specific digestion patterns regardless of the cellular origin of the receptors. Receptor-[3H]dexamethasone complexes prepared from either Fu5-5 or HTC cells bound calf thymus DNA with the same affinity in vitro. In intact cells, the intracellular distribution of receptor-dexamethasone or receptor-DM complexes at equilibrium was almost identical in the two cell lines. Thus, we detected no differences in the size, sequence, or net charge of Fu5-5 or HTC cell receptors; additionally, there were no significant differences in steroid uptake, receptor binding, or activation, translocation, and nuclear binding of receptor-steroid complexes. However, the DM labeling efficiency, calculated as the percentage of total receptors covalently labeled by DM, was higher in HTC cells (65.9 +/- 12.9%; n = 5) than in Fu5-5 cells (39.3 +/- 7.7%; n = 5). The labeling efficiency of DM correlated inversely with its ability to induce tyrosine aminotransferase activity, suggesting that DM forms noncovalent, as well as covalent, complexes in vivo which mediate the glucocorticoid and antiglucocorticoid activities of DM, respectively. Further research is required to identify the factor(s) that influences DM labeling efficiency, thereby affecting the amount of DM agonist activity and, possibly, the sensitivity of the cells to glucocorticoids.