Correlation of Heat Shock Protein 70 Expression with Estrogen Receptor Levels in Invasive Human Breast Cancer

Takahashi, Shuji; Mikami, Toshihiko; Watanabe, Yoshiki; Okazaki, Masanori; Osuga, Yutaka; Okazaki, Atsushi; Satō, Takashi; Asaishi, Kazuaki; Hirata, Koichi; Narimatsu, Eimei; Mori, Makoto; Sato, Noriyuki; Kikuchi, Kokichi

doi:10.1093/ajcp/101.4.519

Cited by 39 publications

(31 citation statements)

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“…Abundant data have been published on the increased expression of HSP70 in several tumors, such as breast cancer (Takahashi et al 1994;Lazaris et al 1997;Vargas-Roig et al 1997), ovarian cancer (Elpek et al 2003), carcinoma of the uterine cervix (Kaur and Ralhan 1995;Park et al 1999), lung cancer (Zhong et al 2003), prostate cancer (Abe et al 2004;Cornford et al 2000), and other types of cancer (reviewed in Ciocca and Calderwood (2005)) . Colorectal tumors also exhibit increased HSP70 expression (Hwang et al 2003;Dundas et al 2005;Pfister et al 2007).…”

Section: Discussionmentioning

confidence: 99%

Serum level of soluble 70-kD heat shock protein is associated with high mortality in patients with colorectal cancer without distant metastasis

Kocsis

Madaras

Tóth

et al. 2010

Cell Stress and Chaperones

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Many findings indicate that measuring the serum concentration of soluble 70-kD heat shock protein (soluble HSP70) may provide important information in cardiovascular, inflammatory, and pregnancy-related diseases; however, only scarce data are available in cancer. Therefore, using a commercial ELISA kit, we measured soluble HSP70 concentration in the sera of 179 patients with colorectal cancer. We investigated the relationship between soluble HSP70 concentration and mortality, during 33.0 (24.4-44.0)months long follow-up. High (>1.65 pg/ml, median concentration) soluble HSP70 level was a significant (hazard ratio: 1.88 (1.20-2.96, p=0.005) predictor of mortality during the follow-up period. When we compared the soluble HSP70 levels in patients with non-resected primary tumors as compared to those who were recruited into the study 4-6 weeks after the tumor resection they were found to be significantly (p=0.020) higher in the former group. Since the patients with non-resected primary tumors had also distant metastasis and died early, we limited the further analysis to 142 patients with no distant metastasis at the beginning of the follow-up. This association remained significant even after multiple Cox-regression analysis had been performed to adjust the data for age and sex (p=0.028); age, sex, and TNM-T stage (p=0.041); age, sex, and TNM-N stage (p=0.021); age, sex, and histological grade (p=0.023); or age, sex, and tumor localization (p=0.029). Further analysis showed that the significant association between high HSP70 levels and poor survival is in the strongest in the group of <70-year-old female patients (HR: 5.52 (2.02-15.15), p=0.001), as well as in those who were in a less advanced stage of the disease at baseline. These novel findings indicate that the serum level of soluble HSP70 might prove a useful, stage-independent prognostic marker in colorectal cancer without distant metastasis.

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Section: Discussionmentioning

confidence: 99%

Serum level of soluble 70-kD heat shock protein is associated with high mortality in patients with colorectal cancer without distant metastasis

Kocsis

Madaras

Tóth

et al. 2010

Cell Stress and Chaperones

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“…As an example, HSP90 stabilizes Akt and oncogenic forms of mutant epidermal growth factor receptor, both of which contribute to the growth of a variety of cancers including gliomas (13)(14)(15). HSP70, in a complex with HSP90 and HSP40, also serves to regulate the function and turnover of the estrogen receptor, increasing its activation and driving estrogen-dependent cellular responses (16,17). HSP70 and HSP90 are also critically involved in the DNA-binding properties and stability of p53, and by stabilizing mutant p53, contribute to its role in transformation (18,19).…”

Section: Introductionmentioning

confidence: 99%

Heat Shock Protein 90α Recruits FLIPS to the Death-Inducing Signaling Complex and Contributes to TRAIL Resistance in Human Glioma

Panner

Murray²,

Berger³

et al. 2007

Cancer Research

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Heat shock protein 90 (HSP90) is a molecular chaperone that contributes to the proper folding and stability of target proteins. Because HSP90 has been suggested to interact with FLIP S , the key regulator of tumor necrosis factor-A-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in glioma cells, we examined the role HSP90 played in controlling TRAIL response. HSP90A was found to associate with FLIP S in resting cells in a manner dependent on the ATPbinding NH 2 -terminal domain of HSP90A. Following TRAIL exposure, HSP90A and the client FLIP S protein were recruited to the death-inducing signaling complex (DISC). Short interfering RNA-mediated suppression of HSP90A did not alter the total cellular levels of FLIP S , but rather inhibited the recruitment of FLIP S and other antiapoptotic proteins such as RIP and FLIP L to the DISC, and sensitized otherwise resistant glioma cells to TRAIL-induced apoptosis. These results show that HSP90A, by localizing FLIP S to the DISC, plays a key role in the resistance of tumor cells to TRAIL, and perhaps other proapoptotic agents. The results also define a novel means of apoptotic control by a HSP90A that may in turn help explain the global antiapoptotic effects of this protein. [Cancer Res 2007;67(19):9482-9]

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“…A strict correlation between HSP70 levels and increased oestrogen receptors has also been detected [53]. Significant increases in HSP27 and HSP70 in its inducible form have also been observed in canine mammary tumour, particularly in the more invasive neoplastic cells, therefore these proteins (and HSP90) play a meaningful role in the multiple processes leading to malignant transformation and tumour progression in the canine mammary gland [12].…”

Section: Diagnostic and Prognostic Implications Of Hsp Expression In mentioning

confidence: 88%

“…Clinical-pathological studies have shown that the inducible form of the HSP70 family (HSP72) is associated with poor differentiation and the presence of mutated p53 in breast cancers [53], and its nuclear staining pattern has been reported to be correlated to tumour size [54]. A strict correlation between HSP70 levels and increased oestrogen receptors has also been detected [53].…”

Section: Diagnostic and Prognostic Implications Of Hsp Expression In mentioning

confidence: 99%

The Role of Heat Shock Proteins in Mammary Neoplasms: A Brief Review

Salda¹,

Romanucci²

2012

JCT

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Research into heat shock proteins (HSPs) for the clinical management of tumours has intensified as new evidence shows they can be used as biomarkers in carcinogenesis and are related to poor prognosis in some cancer types. Members of small HSP, HSP70 and HSP90 families have been studied extensively in breast cancer. This article reviews current understanding of the role of HSP and HSF-1 (Heat shock factor 1) expression in human breast cancer and looks at its potential diagnostic, prognostic and therapeutic value. The exciting progress that has been made using HSP 90 inhibitors in breast cancer treatment is examined and the results of preliminary studies on the expression of stress proteins in the animal model canine mammary tumours are also presented.

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Correlation of Heat Shock Protein 70 Expression with Estrogen Receptor Levels in Invasive Human Breast Cancer

Cited by 39 publications

References 0 publications

Serum level of soluble 70-kD heat shock protein is associated with high mortality in patients with colorectal cancer without distant metastasis

Serum level of soluble 70-kD heat shock protein is associated with high mortality in patients with colorectal cancer without distant metastasis

Heat Shock Protein 90α Recruits FLIPS to the Death-Inducing Signaling Complex and Contributes to TRAIL Resistance in Human Glioma

The Role of Heat Shock Proteins in Mammary Neoplasms: A Brief Review

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