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HSP70 in TGF-β signal transduction role

Author: LiYiHao
Tutor: KangXianJiang；WangQiang
School: Hebei University
Course: Aquatic organisms
Keywords: TGF-β HSP70 Smad2 Epithelial cells into mesenchymal cells into EMT
CLC: Q75
Type: Master's thesis
Year: 2011
Downloads: 41
Quote: 0
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Abstract


Nodal / TGF-β signaling pathway is TGF-β superfamily members, in vertebrate embryonic development, tissue differentiation, maintenance of homeostasis, and apoptosis, migration, diseases and other physiological and pathological processes plays a vital effect. As a Nodal / TGF-β signaling pathway is an important component, Smad2 synergy with many proteins and transcription factor binding regulation Nodal / TGF-β signaling pathway, thus affecting downstream target gene expression. And the interaction of these proteins directly affect Smad2 TGF-β signal transduction and regulation processes. In order to identify some new Smad2 binding factor, this paper GST-Smad2 fusion protein as bait, using GST pull down assay technologies separation of its potential binding proteins. Using mass spectrometry protein components found MDM2 binding protein MTBP and heat shock protein HSP70. Protein immunoprecipitation results show, HSP70 can not only interacts with zebrafish Smad2, you can also combine with human Smad2, and in vitro translation of the two proteins also exist interactions. Luciferase reporter gene experiments found that overexpression of HSP70 for Smad2-mediated TGF-β signaling pathway has a significant inhibitory effect, while HSP70 and HSP70 siRNA inhibitors can increase signal transduction were proved right Smad2 mediated HSP70 the presence of TGF-β signaling negative regulation. A further study found, HSP70 in TGF-β stimulation of expression in the cytoplasm before and after using the sustained activation of TGF-βI receptor activation pathway, HSP70 and Smad2 combination has not been significantly affected. However, overexpression of HSP70 endogenous HEK293 cells can lead to phosphorylation of Smad2 significantly reduced, and more importantly, the present study also found that HSP70 may block TGF-β-induced stimulation of the nucleus during Smad2. Binding assays epithelial cells to mesenchymal cell transformation experiments and found that the overexpression of HSP70 can hinder TGF-β-induced epithelial to mesenchymal cell transformation, this result also speaks of HSP70 on TGF-β signaling negative regulation role, but also that this regulation will negatively affect some and TGF-β signaling of important physiological processes. TGF-β signaling in the early stage of tumor cell proliferation inhibiting effect. In tumor tissue, HSP70 expression level than normal tissue. This discovery of HSP70 on TGF-β signaling pathway inhibition and molecular mechanisms, which may be understood mechanism of tumorigenesis has important reference.

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