scholarly journals Heat Shock Protein gp96 Interacts with Protein Phosphatase 5 and Controls Toll-like Receptor 2 (TLR2)-mediated Activation of Extracellular Signal-regulated Kinase (ERK) 1/2 in Post-hypoxic Kidney Cells

2009 ◽  
Vol 284 (18) ◽  
pp. 12541-12549 ◽  
Author(s):  
Sanae Ben Mkaddem ◽  
Catherine Werts ◽  
Jean-Michel Goujon ◽  
Marcelle Bens ◽  
Eric Pedruzzi ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Phosphatase ◽  
Kidney Cells ◽  
Toll Like Receptor ◽  
Protein Phosphatase 5 ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Heat Shock Protein Gp96 ◽  
Toll Like Receptor 2

scholarly journals The Endoplasmic Reticulum-resident Heat Shock Protein Gp96 Activates Dendritic Cells via the Toll-like Receptor 2/4 Pathway

2002 ◽  
Vol 277 (23) ◽  
pp. 20847-20853 ◽  
Author(s):  
Ramunas M. Vabulas ◽  
Sibylla Braedel ◽  
Norbert Hilf ◽  
Harpreet Singh-Jasuja ◽  
Sylvia Herter ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Dendritic Cells ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Toll Like Receptor ◽  
Heat Shock Protein Gp96 ◽  
Toll Like Receptor 2

scholarly journals The Molecular Chaperone Heat Shock Protein 70 Controls Liver Cancer Initiation and Progression by Regulating Adaptive DNA Damage and Mitogen-Activated Protein Kinase/Extracellular Signal-Regulated Kinase Signaling Pathways

2019 ◽  
Vol 39 (9) ◽  
Author(s):  
Wonkyoung Cho ◽  
Xiongjie Jin ◽  
Junfeng Pang ◽  
Yan Wang ◽  
Nahid F. Mivechi ◽  
...  
Keyword(s):  
Dna Damage ◽  
Heat Shock ◽  
Protein Kinase ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Cell Transformation ◽  
Mitogen Activated Protein Kinase ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Mitogen Activated Protein

ABSTRACT Delineating the mechanisms that drive hepatic injury and hepatocellular carcinoma (HCC) progression is critical for development of novel treatments for recurrent and advanced HCC but also for the development of diagnostic and preventive strategies. Heat shock protein 70 (HSP70) acts in concert with several cochaperones and nucleotide exchange factors and plays an essential role in protein quality control that increases survival by protecting cells against environmental stressors. Specifically, the HSP70-mediated response has been implicated in the pathogenesis of cancer, but the specific mechanisms by which HSP70 may support malignant cell transformation remains to be fully elucidated. Here, we show that genetic ablation of HSP70 markedly impairs HCC initiation and progression by distinct but overlapping pathways. This includes the potentiation of the carcinogen-induced DNA damage response, at the tumor initiation stage, to increase the p53-dependent surveillance response leading to the cell cycle exit or death of genomically damaged differentiated pericentral hepatocytes, and this may also prevent their conversion into more proliferating HCC progenitor cells. Subsequently, activation of a mitogen-activated protein kinase/extracellular signal-regulated kinase (MAPK/ERK) negative feedback pathway diminishes oncogenic signals, thereby attenuating premalignant cell transformation and tumor progression. Modulation of HSP70 function may be a strategy for interfering with oncogenic signals driving liver cell transformation and tumor progression, thus providing an opportunity for human cancer control.

The Significance of Heat-Shock Protein GP96 and its Receptors' CD91 and Toll-Like Receptor 4 Expression at the Maternal Foetal Interface

2013 ◽  
Vol 70 (1) ◽  
pp. 10-23 ◽  
Author(s):  
Tamara Gulic ◽  
Gordana Laskarin ◽  
Arnela Redzovic ◽  
Senija Eminović ◽  
Herman Haller ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Toll Like Receptor ◽  
Toll Like Receptor 4 ◽  
Heat Shock Protein Gp96
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