Impaired induction of heat shock protein implicated in decreased thermotolerance in a temperature-sensitive multinucleated cell line

1998 ◽  
Vol 437 (1) ◽  
pp. 15-20 ◽  
Author(s):  
Y. Cao ◽  
Takaaki Matsumoto ◽  
Katsuaki Motomura ◽  
Akira Ohtsuru ◽  
Shunichi Yamashita ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cell Line ◽  
Temperature Sensitive ◽  
Multinucleated Cell

Canine heat shock protein 27 promotes proliferation, migration, and doxorubicin resistance in the canine cell line DTK-F

2015 ◽  
Vol 205 (2) ◽  
pp. 254-262 ◽  
Author(s):  
An-Ci Lin ◽  
Cheng-Wei Liao ◽  
Sui-Wen Lin ◽  
Chien-Yi Huang ◽  
Chian-Jiun Liou ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cell Line ◽  
Heat Shock Protein 27 ◽  
Doxorubicin Resistance

The role of heat shock protein 70 in the thermoresistance of prostate cancer cell line spheroids

FEBS Letters ◽  
2004 ◽  
Vol 561 (1-3) ◽  
pp. 144-148 ◽  
Author(s):  
Samideh Khoei ◽  
Bahram Goliaei ◽  
Ali Neshasteh-Riz ◽  
Abdolkhalegh Deizadji
Keyword(s):  
Prostate Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cell Line ◽  
Cancer Cell ◽  
Heat Shock Protein 70 ◽  
Prostate Cancer Cell ◽  
Cancer Cell Line ◽  
Prostate Cancer Cell Line

scholarly journals In Vivo Chaperone Activity of Heat Shock Protein 70 and Thermotolerance

1999 ◽  
Vol 19 (3) ◽  
pp. 2069-2079 ◽  
Author(s):  
Ellen A. A. Nollen ◽  
Jeanette F. Brunsting ◽  
Han Roelofsen ◽  
Lee A. Weber ◽  
Harm H. Kampinga
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Resistance ◽  
Cell Line ◽  
Heat Shock Protein 70 ◽  
Chaperone Activity ◽  
Luciferase Reporter ◽  
Reporter Protein ◽  
Regulated Gene Expression

ABSTRACT Heat shock protein 70 (Hsp70) is thought to play a critical role in the thermotolerance of mammalian cells, presumably due to its chaperone activity. We examined the chaperone activity and cellular heat resistance of a clonal cell line in which overexpression of Hsp70 was transiently induced by means of the tetracycline-regulated gene expression system. This single-cell-line approach circumvents problems associated with clonal variation and indirect effects resulting from constitutive overexpression of Hsp70. The in vivo chaperone function of Hsp70 was quantitatively investigated by using firefly luciferase as a reporter protein. Chaperone activity was found to strictly correlate to the level of Hsp70 expression. In addition, we observed an Hsp70 concentration dependent increase in the cellular heat resistance. In order to study the contribution of the Hsp70 chaperone activity, heat resistance of cells that expressed tetracycline-regulated Hsp70 was compared to thermotolerant cells expressing the same level of Hsp70 plus all of the other heat shock proteins. Overexpression of Hsp70 alone was sufficient to induce a similar recovery of cytoplasmic luciferase activity, as does expression of all Hsps in thermotolerant cells. However, when the luciferase reporter protein was directed to the nucleus, expression of Hsp70 alone was not sufficient to yield the level of recovery observed in thermotolerant cells. In addition, cells expressing the same level of Hsp70 found in heat-induced thermotolerant cells containing additional Hsps showed increased resistance to thermal killing but were more sensitive than thermotolerant cells. These results suggest that the inducible form of Hsp70 contributes to the stress-tolerant state by increasing the chaperone activity in the cytoplasm. However, its expression alone is apparently insufficient for protection of other subcellular compartments to yield clonal heat resistance to the level observed in thermotolerant cells.

scholarly journals STI571 (Glivec) inhibits the interaction between c-KIT and heat shock protein 90 of the gastrointestinal stromal tumor cell line, GIST-T1

2005 ◽  
Vol 96 (2) ◽  
pp. 116-119 ◽  
Author(s):  
Hajime Nakatani ◽  
Michiya Kobayashi ◽  
Toufeng Jin ◽  
Takahiro Taguchi ◽  
Takeki Sugimoto ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Tumor Cell ◽  
Gastrointestinal Stromal Tumor ◽  
Cell Line ◽  
Tumor Cell Line ◽  
Heat Shock Protein 90 ◽  
Stromal Tumor
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