摘要
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.
出处
《基础医学与临床》
CSCD
1995年第6期23-27,共5页
Basic and Clinical Medicine
基金
国家自然科学基金
卫生部重点课题基金
