Characterization of Corticosterone‐Induced Protein Synthesis in Hippocampal Slices
Characterization of Corticosterone‐Induced Protein Synthesis in Hippocampal Slices
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DOI：
10.1111/j.1471-4159.1980.tb03696.x
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发表时间：
1980-09
影响因子：
4.7
通讯作者：
A. M. Etgen;Michelle Martin;Russell Gilbert;G. Lynch
中科院分区：
文献类型：
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作者：
A. M. Etgen;Michelle Martin;Russell Gilbert;G. Lynch
皮质酮显著增加[3 H]亮氨酸掺入从成年雄性白化病大鼠制备的体外海马切片分离的特异性胞质溶胶蛋白。本研究表明，在与糖皮质激素加蛋白质合成抑制剂（1 mm-放线菌酮）共孵育的切片中，未观察到氨基酸掺入的增强，表明激素在海马中起作用以增加从头蛋白质合成。进一步的实验表明，在将切片暴露于皮质酮30分钟后，首先可检测到类固醇诱导的蛋白质合成（+ 5.7%）;与对照组相比，孵育1或2小时的切片均显示受影响蛋白质的合成增加12%。为了确定糖皮质激素对蛋白质代谢的改变是否是受体介导的，还将海马切片与10 nm孕酮一起孵育，孕酮是一种已知竞争皮质酮结合其胞质受体的类固醇。单独的孕酮不会将细胞质受体转移到细胞核，不会改变海马蛋白质代谢，并有效地阻断了皮质酮对54 K蛋白的诱导。这些研究提供的证据表明，在大鼠海马中，皮质酮与高亲和力类固醇受体相互作用，以调节特定蛋白质的合成。
: Corticosterone significantly increases the incorporation of [3H]leucine into specific cytosol protein(s) isolated from in vitro hippocampal slices prepared from adult male albino rats. The present study showed that in slices coincubated with glucocorticoid plus a protein synthesis inhibitor (1 mm‐cycloheximide), no such enhancement of amino acid incorporation was observed, suggesting that the hormone acts in the hippocampus to increase de novo protein synthesis. Further experiments demonstrated that the steroid‐induced protein synthesis was first detectable (+ 5.7%) following a 30‐min exposure of slices to corticosterone; slices incubated for 1 or 2 h both showed a 12% increase in synthesis of the affected protein(s) when compared with controls. In an attempt to determine whether the glucocorticoid alteration of protein metabolism was receptor‐mediated, hippocampal slices were also incubated with 10 nm‐progesterone, a steroid known to compete for corticosterone binding to its cytosol receptor. Progesterone alone, which does not translocate cytoplasmic receptors to the nucleus, did not alter hippocampal protein metabolism and effectively blocked the induction by corticosterone of the 54K protein(s). These studies provide evidence that in the rat hippocampus corticosterone interacts with high‐affinity steroid receptors to regulate the synthesis of specific protein(s).