Proteasome inhibitors differentially affect heat shock protein response in cancer cells

2001 ◽  
Author(s):  
B. Ashok ◽  
E. Kim ◽  
A. Mittelman ◽  
R. Tiwari
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Proteasome Inhibitors ◽  
Protein Response

scholarly journals Recombinant heat shock protein 27 (HSP27/HSPB1) protects against cadmium-induced oxidative stress and toxicity in human cervical cancer cells

2017 ◽  
Vol 22 (3) ◽  
pp. 357-369 ◽  
Author(s):  
Daiana G. Alvarez-Olmedo ◽  
Veronica S. Biaggio ◽  
Geremy A. Koumbadinga ◽  
Nidia N. Gómez ◽  
Chunhua Shi ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cervical Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Heat Shock Protein 27 ◽  
Cervical Cancer Cells ◽  
Human Cervical Cancer Cells ◽  
Human Cervical Cancer

scholarly journals Enzyme-treated Asparagus Extract Down-regulates Heat Shock Protein 27 of Pancreatic Cancer Cells

In Vivo ◽  
2018 ◽  
Vol 32 (4) ◽  
pp. 759-763 ◽  
Author(s):  
TAKUYA SHIMADA ◽  
YUTA NANIMOTO ◽  
BYRON BARON ◽  
TAKAO KITAGAWA ◽  
KAZUHIRO TOKUDA ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Heat Shock Protein 27 ◽  
Pancreatic Cancer Cells

scholarly journals Heat Shock Protein Hsp72 Controls Oncogene-Induced Senescence Pathways in Cancer Cells

2008 ◽  
Vol 29 (2) ◽  
pp. 559-569 ◽  
Author(s):  
Vladimir L. Gabai ◽  
Julia A. Yaglom ◽  
Todd Waldman ◽  
Michael Y. Sherman
Keyword(s):  
Heat Shock ◽  
Epithelial Cells ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Pi3k Pathway ◽  
Phosphatidylinositol 3 Kinase ◽  
P53 Pathway ◽  
Extracellular Signal ◽  
Kinase Cascade ◽  
Dependent Pathway

ABSTRACT The heat shock protein Hsp72 is expressed at the elevated levels in various human tumors, and its levels often correlate with poor prognosis. Previously we reported that knockdown of Hsp72 in certain cancer cells, but not in untransformed breast epithelial cells, triggers senescence via p53-dependent and p53-independent mechanisms. Here we demonstrate that the p53-dependent pathway controlled by Hsp72 depends on the oncogenic form of phosphatidylinositol 3-kinase (PI3K). Indeed, upon expression of the oncogenic PI3K, epithelial cells began responding to Hsp72 depletion by activating the p53 pathway. Moreover, in cancer cell lines, activation of the p53 pathway caused by depletion of Hsp72 was dependent on oncogenes that activate the PI3K pathway. On the other hand, the p53-independent senescence pathway controlled by Hsp72 was associated with the Ras oncogene. In this pathway, extracellular signal-regulated kinases (ERKs) were critical for senescence, and Hsp72 controlled the ERK-activating kinase cascade at the level of Raf-1. Importantly, upon Ras expression, untransformed cells started responding to knockdown of Hsp72 by constitutive activation of ERKs, culminating in senescence. Therefore, Hsp72 is intimately involved in suppression of at least two separate senescence signaling pathways that are regulated by distinct oncogenes in transformed cells, which explains why cancer cells become “addicted” to this heat shock protein.

scholarly journals Paclitaxel-doxorubicin sequence is more effective in breast cancer cells with heat shock protein 27 overexpression

2008 ◽  
Vol 121 (20) ◽  
pp. 1975-1979 ◽  
Author(s):  
Peng SHI ◽  
Ming-ming WANG ◽  
Li-yu JIANG ◽  
Huan-tao LIU ◽  
Jing-zhong SUN
Keyword(s):  
Breast Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Heat Shock Protein 27
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