scholarly journals Allostery in the Hsp70 Chaperone Proteins

2012 ◽  
pp. 99-153 ◽  
Author(s):  
Erik R. P. Zuiderweg ◽  
Eric B. Bertelsen ◽  
Aikaterini Rousaki ◽  
Matthias P. Mayer ◽  
Jason E. Gestwicki ◽  
...  
Keyword(s):  
Chaperone Proteins ◽  
Hsp70 Chaperone

scholarly journals Structural basis of the allosteric trigger of the Hsp70 chaperone proteins.

2008 ◽  
Author(s):  
Akash Bhattacharya ◽  
Alexander Kurochkin ◽  
Grover Yip ◽  
Eric Bertelsen ◽  
Erik Zuiderweg
Keyword(s):  
Structural Basis ◽  
Chaperone Proteins ◽  
Hsp70 Chaperone

scholarly journals Expression Profile of Two HSP70 Chaperone Proteins in Response to Extreme Thermal Acclimation inXestia c-nigrum(Lepidoptera: Noctuidae)

2015 ◽  
Vol 98 (2) ◽  
pp. 506-515 ◽  
Author(s):  
Ling Wang ◽  
Shuai Yang ◽  
Lanlan Han ◽  
Kuijun Zhao ◽  
Lefu Ye
Keyword(s):  
Expression Profile ◽  
Thermal Acclimation ◽  
Chaperone Proteins ◽  
Hsp70 Chaperone ◽  
Lepidoptera Noctuidae

scholarly journals Disruption of the Complex between GAPDH and Hsp70 Sensitizes C6 Glioblastoma Cells to Hypoxic Stress

2021 ◽  
Vol 22 (4) ◽  
pp. 1520
Author(s):  
Marina A. Mikeladze ◽  
Elizaveta A. Dutysheva ◽  
Victor G. Kartsev ◽  
Boris A. Margulis ◽  
Irina V. Guzhova ◽  
...  
Keyword(s):  
Cell Death ◽  
Hypoxic Stress ◽  
C6 Cells ◽  
Tumor Resistance ◽  
Glioblastoma Cells ◽  
Enzyme Expression ◽  
Hsp70 Chaperone ◽  
Therapeutic Tools ◽  
Enzyme Molecules

Hypoxia, which commonly accompanies tumor growth, depending on its strength may cause the enhancement of tumorigenicity of cancer cells or their death. One of the proteins targeted by hypoxia is glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and we demonstrated here that hypoxia mimicked by treating C6 rat glioblastoma cells with cobalt chloride caused an up-regulation of the enzyme expression, while further elevation of hypoxic stress caused the enzyme aggregation concomitantly with cell death. Reduction or elevation of GAPDH performed with the aid of specific shRNAs resulted in the augmentation of the tumorigenicity of C6 cells or their sensitization to hypoxic stress. Another hypoxia-regulated protein, Hsp70 chaperone, was shown to prevent the aggregation of oxidized GAPDH and to reduce hypoxia-mediated cell death. In order to release the enzyme molecules from the chaperone, we employed its inhibitor, derivative of colchicine. The compound was found to substantially increase aggregation of GAPDH and to sensitize C6 cells to hypoxia both in vitro and in animals bearing tumors with distinct levels of the enzyme expression. In conclusion, blocking the chaperonic activity of Hsp70 and its interaction with GAPDH may become a promising strategy to overcome tumor resistance to multiple environmental stresses and enhance existing therapeutic tools.

scholarly journals Kinetic and structural parameters governing Fic-mediated adenylylation/AMPylation of the Hsp70 chaperone, BiP/GRP78

2021 ◽  
Author(s):  
Anwesha Sanyal ◽  
Erica A. Zbornik ◽  
Ben G. Watson ◽  
Charles Christoffer ◽  
Jia Ma ◽  
...  
Keyword(s):  
Structural Parameters ◽  
Hsp70 Chaperone

scholarly journals Prevention of High Glucose-Mediated EMT by Inhibition of Hsp70 Chaperone

2021 ◽  
Vol 22 (13) ◽  
pp. 6902
Author(s):  
Alina D. Nikotina ◽  
Snezhana A. Vladimirova ◽  
Elena Y. Komarova ◽  
Dmitry Alexeev ◽  
Sergey Efremov ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Transcription Factors ◽  
Cell Motility ◽  
Cancer Cells ◽  
High Glucose ◽  
Binding Capacity ◽  
Colon Cancer Cells ◽  
Mesenchymal Transition ◽  
Hsp70 Chaperone ◽  
Migration Capacity

Hyperglycemia may contribute to the progression of carcinomas by triggering epithelial-to-mesenchymal transition (EMT). Some proteostasis systems are involved in metastasis; in this paper, we sought to explore the mechanism of Hsp70 chaperone in EMT. We showed that knockdown of Hsp70 reduced cell migration capacity concomitantly with levels of mRNA of the Slug, Snail, and Twist markers of EMT, in colon cancer cells incubated in high glucose medium. Conversely, treatment of cells with Hsp70 inducer U-133 were found to elevate cell motility, along with the other EMT markers. To prove that inhibiting Hsp70 may reduce EMT efficiency, we treated cells with a CL-43 inhibitor of the HSF1 transcription factor, which lowered Hsp70 and HSF1 content in the control and induced EMT in carcinoma cells. Importantly, CL-43 reduced migration capacity, EMT-linked transcription factors, and increased content of epithelial marker E-cadherin in colon cancer cells of three lines, including one derived from a clinical sample. To prove that Hsp70 chaperone should be targeted when inhibiting the EMT pathway, we treated cancer cells with 2-phenylethynesulfonamide (PES) and demonstrated that the compound inhibited substrate-binding capacity of Hsp70. Furthermore, PES suppressed EMT features, cell motility, and expression of specific transcription factors. In conclusion, the Hsp70 chaperone machine efficiently protects mechanisms of the EMT, and the safe inhibitors of the chaperone are needed to hamper metastasis at its initial stage.

scholarly journals Hsp70 chaperone blocks α-synuclein oligomer formation via a novel engagement mechanism

2021 ◽  
Vol 296 ◽  
pp. 100613
Author(s):  
Jiahui Tao ◽  
Amandine Berthet ◽  
Y. Rose Citron ◽  
Paraskevi L. Tsiolaki ◽  
Robert Stanley ◽  
...  
Keyword(s):  
Oligomer Formation ◽  
Hsp70 Chaperone
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