scholarly journals UDP glucuronosyltransferase 1A expression levels determine the response of colorectal cancer cells to the heat shock protein 90 inhibitor ganetespib

2014 ◽  
Vol 5 (9) ◽  
pp. e1411-e1411 ◽  
Author(s):  
H Landmann ◽  
D A Proia ◽  
S He ◽  
L S Ogawa ◽  
F Kramer ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Heat Shock Protein 90 ◽  
Expression Levels ◽  
Colorectal Cancer Cells ◽  
Udp Glucuronosyltransferase

Heat shock protein 27 is associated with irinotecan resistance in human colorectal cancer cells

FEBS Letters ◽  
2007 ◽  
Vol 581 (8) ◽  
pp. 1649-1656 ◽  
Author(s):  
Dae Hwa Choi ◽  
Jin Sook Ha ◽  
Won Hyuck Lee ◽  
Jeong Kee Song ◽  
Gyu Yeol Kim ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Heat Shock Protein 27 ◽  
Human Colorectal Cancer ◽  
Colorectal Cancer Cells ◽  
Human Colorectal Cancer Cells

scholarly journals Heat shock protein 90 is involved in the regulation of HMGA2-driven growth and epithelial-to-mesenchymal transition of colorectal cancer cells

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e1683 ◽  
Author(s):  
Chun-Yu Kao ◽  
Pei-Ming Yang ◽  
Ming-Heng Wu ◽  
Chi-Chen Huang ◽  
Yi-Chao Lee ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Expression ◽  
Cancer Cells ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitors ◽  
Hsp90 Inhibition ◽  
Mesenchymal Transition ◽  
Hmga2 Protein

High Mobility Group AT-hook 2 (HMGA2) is a nonhistone chromatin-binding protein which acts as a transcriptional regulating factor involved in gene transcription. In particular, overexpression of HMGA2 has been demonstrated to associate with neoplastic transformation and tumor progression in Colorectal Cancer (CRC). Thus, HMGA2 is a potential therapeutic target in cancer therapy. Heat Shock Protein 90 (Hsp90) is a chaperone protein required for the stability and function for a number of proteins that promote the growth, mobility, and survival of cancer cells. Moreover, it has shown strong positive connections were observed between Hsp90 inhibitors and CRC, which indicated their potential for use in CRC treatment by using combination of data mining and experimental designs. However, little is known about the effect of Hsp90 inhibition on HMGA2 protein expression in CRC. In this study, we tested the hypothesis that Hsp90 may regulate HMGA2 expression and investigated the relationship between Hsp90 and HMGA2 signaling. The use of the second-generation Hsp90 inhibitor, NVP-AUY922, considerably knocked down HMGA2 expression, and the effects of Hsp90 and HMGA2 knockdown were similar. In addition, Hsp90 knockdown abrogates colocalization of Hsp90 and HMGA2 in CRC cells. Moreover, the suppression of HMGA2 protein expression in response to NVP-AUY922 treatment resulted in ubiquitination and subsequent proteasome-dependant degradation of HMGA2. Furthermore, RNAi-mediated silencing of HMGA2 reduced the survival of CRC cells and increased the sensitivity of these cells to chemotherapy. Finally, we found that the NVP-AUY922-dependent mitigation of HMGA2 signaling occurred also through indirect reactivation of the tumor suppressor microRNA (miRNA), let-7a, or the inhibition of ERK-regulated HMGA2 involved in regulating the growth of CRC cells. Collectively, our studies identify the crucial role for the Hsp90-HMGA2 interaction in maintaining CRC cell survival and migration. These findings have significant implications for inhibition HMGA2-dependent tumorigenesis by clinically available Hsp90 inhibitors.

scholarly journals Inhibition of heat shock protein 27 phosphorylation promotes sensitivity to 5-fluorouracil in colorectal cancer cells

2014 ◽  
Vol 8 (6) ◽  
pp. 2496-2500 ◽  
Author(s):  
ATSUSHI MATSUNAGA ◽  
YOSHIYUKI ISHII ◽  
MASASHI TSURUTA ◽  
KOJI OKABAYASHI ◽  
HIROTOSHI HASEGAWA ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Heat Shock Protein 27 ◽  
Colorectal Cancer Cells

scholarly journals Cetuximab promotes SN38 sensitivity via suppression of heat shock protein 27 in colorectal cancer cells with wild-type RAS

2017 ◽  
Vol 38 (2) ◽  
pp. 926-932 ◽  
Author(s):  
Takashi Ishida ◽  
Yoshiyuki Ishii ◽  
Masashi Tsuruta ◽  
Koji Okabayashi ◽  
Shingo Akimoto ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Heat Shock Protein 27 ◽  
Wild Type ◽  
Colorectal Cancer Cells
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