HSP27, 70 and 90, anti-apoptotic proteins, in clinical cancer therapy

Wang, Xiaoxia; Chen, Meijuan; Zhou, Jing; Xu, Zhonghua

doi:10.3892/ijo.2014.2399

Cited by 232 publications

(165 citation statements)

References 125 publications

(152 reference statements)

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“…HSF assembles into a trimeric form that is exhibits DNA-binding activity, phosphorylates and then translocates into the nucleus. In the nucleus, HSF binds to HSEs and activates transcription of Hsp genes, e.g., Hsp 27, 70 and 90, to synthesize new Hsps [29][30][31]. In our results, the cells under heat stress conditions showed a statistically significant increase in expression of Hsps 27, 70 and 90 compared with control cells.…”

Section: Expression Of Heat Shock Proteinssupporting

confidence: 53%

Expression of Heat Shock Proteins in Human Fibroblast Cells under Magnetic Resonant Coupling Wireless Power Transfer

2015

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Since 2007, resonant coupling wireless power transfer (WPT) technology has been attracting attention and has been widely researched for practical use. Moreover, dosimetric evaluation has also been discussed to evaluate the potential health risks of the electromagnetic field from this WPT technology based on the International Commission on Non-Ionizing Radiation Protection (ICNIRP) guidelines. However, there has not been much experimental evaluation of the potential health risks of this WPT technology. In this study, to evaluate whether magnetic resonant coupling WPT induces cellular stress, we focused on heat shock proteins (Hsps) and determined the expression level of Hsps 27, 70 and 90 in WI38VA13 subcloned 2RA human fibroblast cells using a western blotting method. The expression level of Hsps under conditions of magnetic resonant coupling WPT for 24 h was not significantly different compared with control cells, although the expression level of Hsps for cells exposed to heat stress conditions was significantly increased. These results suggested that exposure to magnetic resonant coupling WPT did not cause detectable cell stress.

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Section: Expression Of Heat Shock Proteinssupporting

confidence: 53%

Expression of Heat Shock Proteins in Human Fibroblast Cells under Magnetic Resonant Coupling Wireless Power Transfer

2015

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“…HSPs are known to be key factors in the heat shock response and have been identified to be implicated in the etiology of breast cancer (7). The cellular levels of HSP27 are significantly increased in breast cancer cells compared with surrounding healthy tissues.…”

Section: Discussionmentioning

confidence: 99%

“…Heat shock proteins (HSPs) are a large family of proteins that function as molecular chaperones under physiological conditions (7). The ability of radiofrequency ablation to induce the expression of HSPs, including HSP70, in small animal models suggests that HSPs may be involved in rescuing damaged cells in close proximity to the ablation zone and, therefore, limiting the therapeutic effects (8,9).…”

Section: Introductionmentioning

confidence: 99%

Heat shock protein 27 promotes cell proliferation through activator protein-1 in lung cancer

Zhang

Huang

et al. 2015

Oncology Letters

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Abstract. Heat shock protein 27 (HSP27) is an important regulator involved in the development of lung cancer. However, limited evidence exists concerning the underlying molecular mechanisms of its action. The results of the present study revealed that HSP27 was highly expressed in the lung cancer tissues of mice. In an in vitro model, the overexpression of HSP27 promoted cell proliferation, while HSP27 knockdown inhibited cell proliferation. HSP27 promoted cell proliferation in vitro by directly upregulating the expression of HSP27 target genes, which required the activation of the activator protein-1 (AP-1) signaling pathway. This was evaluated by the phosphorylation status of an important pathway component, c-Jun in lung cancer tissue and cells. These results suggested that HSP27 has a promotional role in lung cancer, and therefore indicated a novel mechanism involving lung cancer cell proliferation, which may underlie poor responses to therapy. Therefore, HSP27 may be a suitable therapeutic target for the treatment of lung cancer. IntroductionLung cancer is the leading cause of cancer-associated mortality worldwide, with non-small cell lung cancer (NSCLC) accounting for ~85% of all mortalities associated with lung cancer. The overall five-year survival rate for patients remains poor (1-3). The poor prognoses of lung cancer patients primarily result from early relapse, metastasis and unsuccessful responses to treatment strategies, including surgery, chemotherapy and radiotherapy (4-6). In addition, the lack of effective prognostic biomarkers that are able to predict treatment response and prognosis affects treatment regimens and patient outcomes.Heat shock proteins (HSPs) are a large family of proteins that function as molecular chaperones under physiological conditions (7). The ability of radiofrequency ablation to induce the expression of HSPs, including HSP70, in small animal models suggests that HSPs may be involved in rescuing damaged cells in close proximity to the ablation zone and, therefore, limiting the therapeutic effects (8,9). In addition, HSPs have been identified to promote carcinogenesis by inhibiting apoptosis (10-14) and enhancing resistance to treatment (15,16). However, it has been established that HSPs function differently in different tumors (10,15).HSP27 is a 27-kDa protein that regulates apoptosis by interacting with key components of apoptotic signaling pathways, particularly those involved in the activation of caspases. Increasing evidence has indicated that HSP27 may play an important role in cancer (17). The expression of HSP27 has been associated with poor prognoses in ovarian (18), breast (10,19), gastric (20) and prostate cancers (21), as well as in osteoscarcomas (14). In addition, HSP27 has been reported to be associated with poor prognoses in patients with lung cancer (22). However, whether the expression of HSP27 has a prognostic role in lung cancer remains controversial. Zimmermann et al (22) reported that the level of serum HSP27 was positively correlated with advanced lung...

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“…Thus, treatment strategies based on HSP inhibition are recognized as an important approach to deplete oncoproteins and attack oncogenic signal pathways required for cancer development and progression (13). HSP27 is an important small HSP and is induced in response to varieties of cellular stresses, such as exposure to mitogens, growth factors, hormones, inflammatory cytokines, and anticancer treatment (14). It has been reported that HSP27 was elevated in some human cancer types, such as breast cancer and prostate cancer, and aberrant HSP27 expression correlates with tumor growth, metastasis, as well as therapy resistance (15,16).…”

Section: Discussionmentioning

confidence: 99%

HSP27-Mediated Extracellular and Intracellular Signaling Pathways Synergistically Confer Chemoresistance in Squamous Cell Carcinoma of Tongue

Zheng

Zhang

Líu

et al. 2018

Clinical Cancer Research

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Purpose: Squamous cell carcinoma of tongue (SCCT) is the most common type of oral cavity carcinoma. Chemoresistance in SCCT is common, and the underlying mechanism remains largely unknown. We aimed to identify key molecules and signaling pathways mediating chemoresistance in SCCT. Experimental Design: Using a proteomic approach, we found that the HSP27 was a potential mediator for chemoresistance in SCCT cells. To further validate this role of HSP27, we performed various mechanistic studies using in vitro and in vivo models as well as serum and tissue samples from SCCT patients. Results: The HSP27 protein level was significantly increased in the multidrug-resistant SCCT cells and cell culture medium. Both HSP27 knockdown and anti-HSP27 antibody treatment reversed chemoresistance. Inversely, both HSP27 overexpression and recombinant human HSP27 protein treatment enhanced chemoresistance. Moreover, chemotherapy significantly induced HSP27 protein expression in both SCCT cells and their culture medium, as well as in tumor tissues and serum of SCCT patients. HSP27 overexpression predicts a poor outcome for SCCT patients receiving chemotherapy. Mechanically, extracellular HSP27 binds to TLR5 and then activates NF-κB signaling to maintain SCCT cell survival. TLR5 knockdown or restored IκBα protein level disrupts extracellular HSP27-induced NF-κB transactivation and chemoresistance. Moreover, intracellular HSP27 binds to BAX and BIM to repress their translocation to mitochondrion and subsequent cytochrome C release upon chemotherapy, resulting in inhibition of the mitochondrial apoptotic pathway. Conclusions: HSP27 plays a pivotal role in chemoresistance of SCCT cells via a synergistic extracellular and intracellular signaling. HSP27 may represent a potential biomarker and therapeutic target for precision SCCT treatment. Clin Cancer Res; 24(5); 1163–75. ©2017 AACR.

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HSP27, 70 and 90, anti-apoptotic proteins, in clinical cancer therapy

Cited by 232 publications

References 125 publications

Expression of Heat Shock Proteins in Human Fibroblast Cells under Magnetic Resonant Coupling Wireless Power Transfer

Expression of Heat Shock Proteins in Human Fibroblast Cells under Magnetic Resonant Coupling Wireless Power Transfer

Heat shock protein 27 promotes cell proliferation through activator protein-1 in lung cancer

HSP27-Mediated Extracellular and Intracellular Signaling Pathways Synergistically Confer Chemoresistance in Squamous Cell Carcinoma of Tongue

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