Heat Shock Proteins Promote Cancer: It's a Protection Racket.

Heat shock proteins (HSP) are expressed at high levels in cancer and form a fostering environment that is essential for tumor development. Here, we review the recent data in this area, concentrating mainly on Hsp27, Hsp70, and Hsp90. The overriding role of HSPs in cancer is to stabilize the active functions of overexpressed and mutated cancer genes. Thus, elevated HSPs are required for many of the traits that underlie the morbidity of cancer, including increased growth, survival, and formation of secondary cancers. In addition, HSPs participate in the evolution of cancer treatment resistance. HSPs are also released from cancer cells and influence malignant properties by receptor-mediated signaling. Current data strongly support efforts to target HSPs in cancer treatment.

Calderwood SK ，Gong J 《TRENDS IN BIOCHEMICAL SCIENCES》

Modulatory effects of curcumin on heat shock proteins in cancer: A promising therapeutic approach.

Cancer metastasis represents a multistep process, including alteration of cell adhesion/motility in the microenvironment and sustained angiogenesis, which is essential for supporting cancer growth in tissues that are distant from the primary tumor. There is growing evidence suggesting that heat shock proteins (HSPs) (also known as heat stress proteins), which constitute a family of stress-inducible proteins, may be involved in the pathogenesis of cancer. Curcumin (diferuloylmethane) is a potent anti-inflammatory, antioxidant, antimicrobial, and antitumor agent. Curcumin has been shown to regulate different members of HSPs including HSP27, HSP40, HSP60, HSP70, and HSP90 in cancer. Here, we present extent findings suggesting that curcumin may act as a potential therapeutic agent for the treatment of cancer through its regulation of HSPs.

Forouzanfar F ，Barreto G ，Majeed M ，Sahebkar A ... -  《-》

Upregulation of heat shock protein 27 confers resistance to actinomycin D-induced apoptosis in cancer cells.

Actinomycin D (Act D) is a general transcriptional inhibitor that is approved for the treatment of sarcomas, and Wilms, germ cell and trophoblastic tumors. Little is known about the molecular mechanisms that dictate the sensitivity of cancer cells to Act D. In this study, we investigated the effects of Act D on heat shock proteins (HSPs) and the expression and roles of HSP27 in Act D-induced cancer cell apoptosis. We show that Act D upregulates HSP27 and HSP70 expression in cancer cells, whereas it inhibits HSP90 expression. The upregulation of HSP27 by Act D is not attributable to changes in HSP27 transcription or HSP27 synthesis. HSP27 knockdown leads to an increase in Act D-induced caspase 3 and caspase 7 cleavage, and sensitizes rhabdosarcoma cells and breast cancer cells to Act D-induced apoptosis. We conclude that upregulation of HSP27 represents an adaptive response that compromises the anticancer activity of Act D.

Ma W ，Teng Y ，Hua H ，Hou J ，Luo T ，Jiang Y ... -  《-》

Expression of heat shock proteins in medulloblastoma.

Alexiou GA ，Vartholomatos G ，Stefanaki K ，Patereli A ，Dova L ，Karamoutsios A ，Lallas G ，Sfakianos G ，Moschovi M ，Prodromou N ... -  《-》

Potential role of heat-shock proteins in giant cell tumors.

Chen JT ，Younusi A ，Cao L ，Tian Z ，Zhou YJ ，Song XH ... -  《-》