Gudas J M, Karenlampi S O, Hankinson O
J Cell Physiol. 1986 Sep;128(3):441-8. doi: 10.1002/jcp.1041280313.
The subcellular distribution of the Ah receptor from the mouse hepatoma line, Hepa-1, was investigated following cytochalasin B treatment and cell enucleation. Probing the resultant cytoplast and nucleoplast fractions with radiolabelled tetrachlorodibenzo-p-dioxin (TCDD) revealed the presence of a specifically bound peak of receptor only in the cytoplast fraction. However, the quantity of receptor recovered in these experiments was only 10-12% of the expected value. We therefore undertook an investigation to determine the fate of the Ah receptor in the presence of cytochalasin B. Incubation of Hepa-1 cells with this compound resulted in a rapid loss or inactivation of cytosolic binding activity with a concomitant decrease in the amount of receptor partitioned into the nucleus at all time periods examined. Control experiments indicated that cytochalasin B did not compete with TCDD for binding to the Ah receptor and furthermore, that its mechanism of action could not be attributed to a non-specific effect on all cytosolic proteins. The results obtained are discussed in relation to the proposed models for induction by the estrogen and glucocorticoid binding receptors.
在用细胞松弛素B处理和细胞去核后，对小鼠肝癌细胞系Hepa-1中的芳烃受体（Ah受体）进行了亚细胞分布研究。用放射性标记的四氯二苯并-对-二恶英（TCDD）探测所得的胞质体和核质体组分，结果显示仅在胞质体组分中存在受体特异性结合峰。然而，这些实验中回收的受体量仅为预期值的10% - 12%。因此，我们进行了一项研究以确定在细胞松弛素B存在的情况下Ah受体的去向。用该化合物孵育Hepa-1细胞导致胞质结合活性迅速丧失或失活，同时在所有检测时间段内进入细胞核的受体量均减少。对照实验表明，细胞松弛素B不会与TCDD竞争结合Ah受体，此外，其作用机制不能归因于对所有胞质蛋白的非特异性影响。结合雌激素和糖皮质激素结合受体诱导的模型对所得结果进行了讨论。
