Targeting Heat Shock Proteins 70/90 and Proteasome for Cancer Therapy

2011 ◽  
Vol 18 (27) ◽  
pp. 4250-4264 ◽  
Author(s):  
R. E. Wang
2006 ◽  
Vol 81 (1) ◽  
pp. 15-27 ◽  
Author(s):  
E. Schmitt ◽  
M. Gehrmann ◽  
M. Brunet ◽  
G. Multhoff ◽  
C. Garrido

2020 ◽  
Vol 21 (8) ◽  
pp. 751-760 ◽  
Author(s):  
Qiang Shan ◽  
Fengtao Ma ◽  
Jingya Wei ◽  
Hongyang Li ◽  
Hui Ma ◽  
...  

Heat shock proteins (HSPs) are molecular chaperones involved in a variety of life activities. HSPs function in the refolding of misfolded proteins, thereby contributing to the maintenance of cellular homeostasis. Heat shock factor (HSF) is activated in response to environmental stresses and binds to heat shock elements (HSEs), promoting HSP translation and thus the production of high levels of HSPs to prevent damage to the organism. Here, we summarize the role of molecular chaperones as anti-heat stress molecules and their involvement in immune responses and the modulation of apoptosis. In addition, we review the potential application of HSPs to cancer therapy, general medicine, and the treatment of heart disease.


Oncotarget ◽  
2011 ◽  
Vol 2 (6) ◽  
pp. 433-434 ◽  
Author(s):  
Elizabeth A. Repasky ◽  
John R. Subjeck

2020 ◽  
Vol 21 (18) ◽  
pp. 6611 ◽  
Author(s):  
Jixian Xiong ◽  
Yuting Li ◽  
Xiangyu Tan ◽  
Li Fu

Small heat shock proteins (sHSPs) are ubiquitous ATP-independent chaperones that play essential roles in response to cellular stresses and protein homeostasis. Investigations of sHSPs reveal that sHSPs are ubiquitously expressed in numerous types of tumors, and their expression is closely associated with cancer progression. sHSPs have been suggested to control a diverse range of cancer functions, including tumorigenesis, cell growth, apoptosis, metastasis, and chemoresistance, as well as regulation of cancer stem cell properties. Recent advances in the field indicate that some sHSPs have been validated as a powerful target in cancer therapy. In this review, we present and highlight current understanding, recent progress, and future challenges of sHSPs in cancer development and therapy.


2013 ◽  
Vol 30 (2) ◽  
Author(s):  
Sevil Oskay Halacli ◽  
Burcin Halacli ◽  
Kadri Altundag

Cells ◽  
2019 ◽  
Vol 9 (1) ◽  
pp. 60 ◽  
Author(s):  
Chul Won Yun ◽  
Hyung Joo Kim ◽  
Ji Ho Lim ◽  
Sang Hun Lee

Heat shock proteins (HSPs) constitute a large family of molecular chaperones classified by their molecular weights, and they include HSP27, HSP40, HSP60, HSP70, and HSP90. HSPs function in diverse physiological and protective processes to assist in maintaining cellular homeostasis. In particular, HSPs participate in protein folding and maturation processes under diverse stressors such as heat shock, hypoxia, and degradation. Notably, HSPs also play essential roles across cancers as they are implicated in a variety of cancer-related activities such as cell proliferation, metastasis, and anti-cancer drug resistance. In this review, we comprehensively discuss the functions of HSPs in association with cancer initiation, progression, and metastasis and anti-cancer therapy resistance. Moreover, the potential utilization of HSPs to enhance the effects of chemo-, radio-, and immunotherapy is explored. Taken together, HSPs have multiple clinical usages as biomarkers for cancer diagnosis and prognosis as well as the potential therapeutic targets for anti-cancer treatment.


Author(s):  
Katalin V. Lukacs ◽  
Olivier E. Pardo ◽  
M. Jo Colston ◽  
Duncan M. Geddes ◽  
Eric W F W Alton

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