Abstract
For cytoplasmic glucocorticoid–receptor complexes to enter and accumulate in the nucleus a temperature-dependent event, ‘activation’ is required1–4. Activation can be achieved in vitro by increased ionic strength3–6, dilution or gel filtration7 and is manifested by an increased affinity of steroid–receptor complex for DNA3,5,7,8 and an altered elution profile from ion-exchange resins9–11. Munck and Foley have shown12 that activated complexes isolated from thymocytes elute from DEAE-cellulose in a manner identical to complexes activated in vitro. We report here that DEAE-cellulose chromatography of steroid–receptor complexes from CEM-C7, a cloned human leukaemic T-cell line sensitive to the cytolytic action of glucocorticoids13–15, and its steroid-resistant subclone 4R4 demonstrated that steroid receptors of clone 4R4 cannot form stable activated complexes. This defines a new defect in receptor action, activation lability (r+act1), which is unlike either the r−, r+nt−, or r+nti phenotypes previously described for mouse lymphoid variants16–19.
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Schmidt, T., Harmon, J. & Thompson, E. ‘Activation-labile’ glucocorticoid–receptor complexes of a steroid-resistant variant of CEM-C7 human lymphoid cells. Nature 286, 507–510 (1980). https://doi.org/10.1038/286507a0
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DOI: https://doi.org/10.1038/286507a0
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