Pp2a mediated ampk inhibition promotes hsp70 expression in heat shock response
文献类型：期刊论文
| 作者 | Wang, Ting1; Yu, Qiujing; Chen, Juan; Deng, Bo; Qian, Lihua; Le, Yingying |
| 刊名 | Plos one
 |
| 出版日期 | 2010-10-01 |
| 卷号 | 5期号:10页码:6 |
| ISSN号 | 1932-6203 |
| DOI | 10.1371/journal.pone.0013096 |
| 通讯作者 | Wang, ting() |
| 英文摘要 | Background: under stress, amp-activated protein kinase (ampk) plays a central role in energy balance, and the heat shock response is a protective mechanism for cell survival. the relationship between ampk activity and heat shock protein (hsp) expression under stress is unclear. methodology/principal findings: we found that heat stress induced dephosphorylation of ampk alpha subunit (ampk alpha) in various cell types from human and rodent. in hepg2 cells, the dephosphorylation of ampk alpha under heat stress in turn caused dephosphorylation of acetyl-coa carboxylase and upregulation of phosphoenolpyruvate carboxykinase, two downstream targets of ampk, confirming the inhibition of ampk activity by heat stress. treatment of hepg2 cells with phosphatase 2a (pp2a) inhibitor okadaic acid or inhibition of pp2a expression by rna interference efficiently reversed heat stress-induced ampka dephosphorylation, suggesting that heat stress inhibited ampk through activation of pp2a. heat stress-and other hsp inducer (cdcl(2), celastrol, mg132)-induced hsp70 expression could be inhibited by aicar, an ampk specific activator. inhibition of ampka expression by rna interference reversed the inhibitory effect of aicar on hsp70 expression under heat stress. these results indicate that ampk inhibition under stress contribute to hsp70 expression. mechanistic studies showed that activation of ampk by aicar had no effect on heat stress-induced hsf1 nuclear translocation, phosphorylation and binding with heat response element in the promoter region of hsp70 gene, but significantly decreased hsp70 mrna stability. conclusions/significance: these results demonstrate that during heat shock response, pp2a mediated ampk inhibition upregulates hsp70 expression at least partially through stabilizing its mrna, which suggests a novel mechanism for hsp induction under stress. |
| WOS关键词 | ACTIVATED PROTEIN-KINASE ; PANCREATIC BETA-CELLS ; OKADAIC ACID ; CERAMIDE ; DEPHOSPHORYLATION ; APOPTOSIS ; GLUCOSE ; ALPHA ; 2A ; PHOSPHORYLATION |
| WOS研究方向 | Science & Technology - Other Topics |
| WOS类目 | Multidisciplinary Sciences |
| 语种 | 英语 |
| WOS记录号 | WOS:000282359300006 |
| 出版者 | PUBLIC LIBRARY SCIENCE |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2406349 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Wang, Ting |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Nutr Sci, Key Lab Nutr & Metab, Shanghai, Peoples R China 2.Chinese Acad Sci, Grad Sch, Shanghai, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wang, Ting,Yu, Qiujing,Chen, Juan,et al. Pp2a mediated ampk inhibition promotes hsp70 expression in heat shock response[J]. Plos one,2010,5(10):6. |
| APA | Wang, Ting,Yu, Qiujing,Chen, Juan,Deng, Bo,Qian, Lihua,&Le, Yingying.(2010).Pp2a mediated ampk inhibition promotes hsp70 expression in heat shock response.Plos one,5(10),6. |
| MLA | Wang, Ting,et al."Pp2a mediated ampk inhibition promotes hsp70 expression in heat shock response".Plos one 5.10(2010):6. |
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来源：中国科学院大学
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