淋巴细胞中热休克蛋白90基因表达双重调控机制的研究

Study on the Dual Regulation Mechanism of Human hsp90 Gene Expression in Lymphocyes Cell

体外正常生长的Ｊｕｒｋａｔ细胞中有高ｈｓｐ９０α，ｈｓｐ９０β和低ｈｓｐ７０基础性表达。ＰＨＡ和ＴＰＡ刺激对ｈｓｐ９０α和ｈｓｐ９０β呈迟缓型表达诱导，对ｈｓｐ７０无此种影响。４２℃热休克４０ｍｉｎ对三种ｈｓｐ表现为快速转录活化，但ｈｓｐ７０表达水平的增加明显高于两种ｈｓｐ９０。以富含ＨＳＥ核心序列的ＤＮＡ为探针研究细胞内ＨＳＦ与顺式作用元件的结合活性，发现正常培养或ＰＨＡ、ＴＰＡ刺激的Ｊｕｒｋａｔ细胞中的ＨＳＦ无ＨＳＥ结合活性，与之相反，热休克时ＨＳＦ与ＨＳＥ结合活性明显增加。以上研究结果提示，Ｔ淋巴细胞内ｈｓｐ９０表达存在双重调控机制。

he basal level expression of hsp in Jurkat T cells is very efficient for hsp90α and hsp90βgenes.PHA and TPA induce a slow response of hsp90α and hsp90β gene activation.Cells heatshocked at 42℃ for 40 mins show rapid induction for all of the detected hsps,in with the changeof hsp70 expression is much more notable than those of hsp90 genes.By using HSE-containingsequence as a probe,it is found that in normal growth or PHA,TPA stimulated Jurkat cells,noHSF binding is showed up;on the contrary,heat shock greatly increases HSF binding activity asdetected byEMSA.These results indicate the existence of a HSF-independent and a HSF depen-dent activation pathways in the dual control mechanism for hsp90 gene regulation.