共查询到19条相似文献,搜索用时 109 毫秒
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热休克转录因子1的抗炎症作用 总被引:2,自引:1,他引:1
热休克转录因子1(heat shock factor 1, HSF1)是调节细胞保护性应激蛋白--热休克蛋白表达的主要转录因子,可被热应激、氧化应激等多种理化因素激活.近年研究表明,HSF1具有抗炎症作用:HSF1可抑制TNFα、IL-1β、M-CSF等致炎因子表达,促进IL-10等抗炎因子表达,并降低NF-κB、AP-1等致炎转录因子的活性.HSF1上调热休克蛋白和抑制炎症的双重活性,提示其很可能是联系应激反应和炎症反应的重要因子. 相似文献
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为探讨热休克因子1(heatshockfactor 1,HSF1)活化和过表达对内毒素(endotoxin ,ET)所致粒细胞集落刺激因子(granulocyte colonystimulatingfactor,G CSF)基因表达的影响,采用大肠杆菌内毒素即脂多糖(lipopolysaccharide ,LPS)处理RAW2 6 4 7巨噬细胞,并通过热休克预处理诱导HSF1活化,采用Western印迹检测HSP70的表达观察HSF1的活化情况,RT PCR检测热休克反应(heatshockresponse ,HSR)对G CSFmRNA表达的影响;构建HSF1的pcDNA3 1真核表达质粒,采用脂质体转染法建立HSF1过表达RAW 2 6 4 7巨噬细胞株,用免疫细胞化学和Western印迹观察HSF1的表达,RT- PCR及Northern印迹进一步研究HSF1对G CSF基因表达的可能影响.发现LPS诱导巨噬细胞中G- CSFmRNA表达增多,并随时间的延长,表达量逐渐增加;与单纯内毒素处理组相比,热休克预处理后,LPS诱导的巨噬细胞G- CSFmRNA的表达明显被抑制;建立的稳定表达HSF1的RAW 2 6 4 7细胞株中有HSF1蛋白的核移位;HSF1过表达可明显抑制LPS诱导的RAW2 6 4 7巨噬细胞G -CSFmRNA的表达.上述结果表明热休克预处理能抑制LPS诱导的巨噬细胞G- CSFmRNA的表达;HSF1过表达可抑制内毒素诱导的巨噬细胞G CSFmRNA的表达. 相似文献
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热休克蛋白27(Heat shock protein 27,HSP27)是一种具有多重功能的小热休克蛋白,它在一些病毒的生命周期中也发挥着重要作用。为研究HSP27对流感病毒感染的调节作用,首先在原核及真核细胞中克隆并表达了人源的HSP27蛋白,并验证了HSP27和A型流感病毒NS1蛋白能够相互结合。通过荧光素酶检测试验发现,HSP27可以抑制病毒感染细胞中β干扰素(IFN-β)的表达,但不依赖于其自身的磷酸化状态,而且HSP27与NS1共同对于IFN-β的表达具有叠加抑制效果。进一步的结果表明HSP27可能通过RIG-I样RNA解旋酶(RLH)途径中MDA5因子抑制IFN-β的表达。研究表明,HSP27在被感染细胞的天然免疫中发挥一定作用,有助于进一步阐明宿主因子对于流感病毒感染的调节机理。 相似文献
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目的:研究热休克蛋白27(heat shock protein 27,HSP27)与热休克因子l(heat shock factor 1,HSFl)在子痫前期孕妇胎盘中的表达情况.方法:选择2011年6月-2012年6月在南京医科大学第一附属医院产科住院分娩的子痫前期患者21例(子痫前期组),以同期分娩的正常孕妇21例(正常妊娠组)作为对照组,采用实时定量聚合酶链反应(RT-PCR)、免疫组化(Immunohistochemistry)、蛋白印迹法(Western Blotting)检测两组孕妇胎盘HSP27mRNA和蛋白的表达以及HSF1蛋白表达水平,分析其是否存在组间差异.结果:子痫前期组胎盘中HSP27mRNA表达(3.28±0.34)高于正常妊娠组(1.87±0.22)和蛋白的表达明显增高,HSF1蛋白表达增高,差异具有统计学意义;HSF1与HSP27呈正相关关系(r=0.73,P<0.05).结论:胎盘中HSF1是HSP27表达的主要调控因子. 相似文献
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Jordan T.F. Young Julie Gauley John J. Heikkila 《Comparative biochemistry and physiology. Part A, Molecular & integrative physiology》2009,153(4):417-424
In this study, we examined the effect of concurrent low concentrations of sodium arsenite and mild heat shock temperatures on hsp30 and hsp70 gene expression in Xenopus A6 kidney epithelial cells. RNA blot hybridization and immunoblot analysis revealed that exposure of A6 cells to 1–10 µM sodium arsenite at a mild heat shock temperature of 30 °C enhanced hsp30 and hsp70 gene expression to a much greater extent than found with either stress individually. In cells treated simultaneously with 10 µM sodium arsenite and different heat shock temperatures, enhanced accumulation of HSP30 and HSP70 protein was first detected at 26 °C with larger responses at 28 and 30 °C. HSF1 activity was involved in combined stress-induced hsp gene expression since the HSF1 activation inhibitor, KNK437, inhibited HSP30 and HSP70 accumulation. Immunocytochemical analysis revealed that HSP30 was present in a granular pattern primarily in the cytoplasm in cells treated simultaneously with both stresses. Finally, prior exposure of A6 cells to concurrent sodium arsenite (10 µM) and heat shock (30 °C) treatment conferred thermotolerance since it protected them against a subsequent thermal challenge (37 °C). Acquired thermotolerance was not observed with cells treated with the two mild stresses individually. 相似文献
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Proteome analysis of human umbilical endothelial cells was performed to identify proteins that are modified during vascular endothelial cell growth factor (VEGF)-induced transition from the quiescent into the proliferating-migrative phenotype. Subtractive analysis of two-dimensional gel patterns of human endothelial cells, before and after stimulation with VEGF(165), revealed differences in 85 protein spots. All proteins were identified by peptide sequencing and peptide mass fingerprinting using an electrospray spectrometer. The proteins identified were members of specific families including Ca(2+)-binding proteins, fatty-acid binding proteins, structural proteins, and chaperones. Remarkably, there was a massive activation of cellular machinery for both protein synthesis and protein degradation. Thus, among up-regulated proteins there were members of all groups of heat shock proteins (HSPs; HSP 27, HSP 60, HSP 70p5, HSP 70p8, HSP 90, and HSP 96) and some other proteins showing either chaperone activity or which participate in assembly of multimolecular structures (TCP-1, desmoplakins, junction plakoglobin, GRP 94, thioredoxin related protein, and peptidylprolyl isomerase). The increased expression of HSPs was confirmed at the mRNA level at different stages of treatment with VEGF. Similarly, components of the proteolytic machinery for the degradation of misfolded proteins (ER-60, cathepsin D, proteasome subunits, and protease inhibitor 6) were also up-regulated. On the other hand, changes in the expression of structural proteins (T-plastin, vimentin, alpha tubulin, actin, and myosin) could account, at least in part, for the different morphologies displayed by migrating endothelial cells. In summary, our data show that VEGF levels similar to those during physiological stresses induce a number of genes and multiple endogenous pathways seem to be engaged in restoring cellular homeostasis. To ensure cell survival, the molecular chaperones (the heat shock family of stress proteins) are highly up-regulated providing protein-folding machinery to repair or degrade misfolded proteins. 相似文献
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《Bioorganic & medicinal chemistry letters》2014,24(2):661-666
When a cell encounters external stressors, such as lack of nutrients, elevated temperatures, changes in pH or other stressful environments, a key set of evolutionarily conserved proteins, the heat shock proteins (hsps), become overexpressed. Hsps are classified into six major families with the hsp90 family being the best understood; an increase in cell stress leads to increased levels of hsp90, which leads to cellular protection. A hallmark of hsp90 inhibitors is that they induce a cell rescue mechanism, the heat shock response. We define the unique molecular profile of a compound (SM145) that regulates hormone receptor protein levels through hsp90 inhibition without inducing the heat shock response. Modulation of the binding event between heat shock protein 90 and the immunophilins/homologs using SM145, leads to a decrease in hormone receptor protein levels. Unlike N-terminal hsp90 inhibitors, this hsp90 inhibitor does not induce a heat shock response. This work is proof of principle that controlling hormone receptor expression can occur by inhibiting hsp90 without inducing pro-survival protein heat shock protein 70 (hsp70) or other proteins associated with the heat shock response. Innovatively, we show that blocking the heat shock response, in addition to hsp90, is key to regulating hsp90-associated pathways. 相似文献