The induction mechanism of the molecular chaperone HSP70 in the gastric mucosa by Geranylgeranylacetone (HSP-inducer)
The induction mechanism of the molecular chaperone HSP70 in the gastric mucosa by Geranylgeranylacetone (HSP-inducer)
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DOI：
10.1016/j.bbrc.2006.12.031
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发表时间：
2007-02-09
影响因子：
3.1
通讯作者：
Itoh, Hideaki
中科院分区：
文献类型：
--
作者：
Otaka, Michiro;Yamamoto, Soh;Itoh, Hideaki
为了阐明香叶基香叶基丙酮（GGA）诱导热休克蛋白70表达的机制，我们利用GGA亲和柱研究了GGA特异性结合蛋白。在存在或不存在GGA的情况下，评估HSP 70的伴侣活性和HSP 70与热休克因子1（HSF 1）的结合亲和力的改变。并分析了HSP 70与GGA的结合结构域。一个70 kDa的蛋白质洗脱的10 mM GGA从GGA亲和柱是相同的组成型表达的HSP 70的免疫印迹。HSP 70的GGA结合结构域位于蛋白质的C端，为肽结合结构域（HSP 70 C）。GGA可抑制HSP 70和重组HSP 70 C的分子伴侣活性。此外，在GGA存在下观察到HSP 70从HSF-1上解离。GGA优先结合到与HSF-1结合的HSP 70的C-末端。HSP 70解离后，游离的HSF-1可获得与HSE（HSP 70的启动子区）结合的能力。(c)2006爱思唯尔公司All rights reserved.
To elucidate the induction mechanism of HSP70 by geranylgeranylacetone (GGA), we investigated GGA specific binding proteins using a GGA-affinity column. Alteration of chaperone activity of HSP70 and binding affinity of HSP70 to heat shock factor-1 (HSF1) was evaluated in the presence or absence of GGA. The binding domain of HSP70 to GGA was also analyzed. A 70-kDa protein eluted by 10 mM GGA from the GGA-affinity column was identical to constitutively expressed HSP70 on immunoblotting. GGA-binding domain of HSP70 was C-terminal of the protein as peptide-binding domain (HSP70C). The chaperone activity of HSP70 and recombinant HSP70C was suppressed by GGA. Furthermore, dissociation of the HSP70 from HSF-I was observed in the presence of GGA. GGA preferentially binds to the C-terminal of HSP70 which binds to HSF-1. After dissociation of HSP70, free HSF-1 could acquire the ability to bind to HSE (the promoter region of HSP70) gene. (c) 2006 Elsevier Inc. All rights reserved.