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. 2009 Feb 9:9:14.
doi: 10.1186/1471-230X-9-14.

Heat Shock Protein-27, -60 and -90 expression in gastric cancer: association with clinicopathological variables and patient survival

Constantinos Giaginis  1 , Stella S Daskalopoulou, Stephanie Vgenopoulou, Ioannis Sfiniadakis, Gregorios Kouraklis, Stamatios E Theocharis
Affiliations

Heat Shock Protein-27, -60 and -90 expression in gastric cancer: association with clinicopathological variables and patient survival

Constantinos Giaginis et al. BMC Gastroenterol. .

Abstract

Background: Heat shock proteins (HSPs) are ubiquitous, highly conserved proteins across all the species and play essential roles in maintaining protein stability within the cells under normal conditions, while preventing stress-induced cellular damage. HSPs were also overexpressed in various types of cancer, being associated with tumor cell proliferation, differentiation and apoptosis. The aim of the present study was to evaluate the clinical significance of HSP -27, -60, and -90 expression in gastric carcinoma.

Methods: HSP -27, -60, and -90 proteins expression was assessed immunohistochemically in tumoral samples of 66 gastric adenocarcinoma patients and was statistically analyzed in relation to various clinicopathological characteristics, tumor proliferative capacity and patients' survival.

Results: HSP-27, -60, -90 proteins were abundantly expressed in gastric adenocarcinoma cases examined. HSP-27 expression was significantly associated with tumor size (pT, P = 0.026), the presence of organ metastases (pM, P = 0.046) and pStage (P = 0.041), while HSP-27 staining intensity with nodal status (pN, P = 0.042). HSP-60 expression was significantly associated with patients' sex (P = 0.011), while HSP-60 staining intensity with patients' age (P = 0.027) and tumor histopathological grade (P = 0.031). HSP-90 expression was not associated with any of the clinicopathological parameters examined; however, HSP-90 staining intensity was significantly associated with tumor size (pT, P = 0.020). High HSP-90 expression was significantly associated with longer overall survival times in univariate analysis (log-rank test, P = 0.033), being also identified as an independent prognostic factor in multivariate analysis (P = 0.026).

Conclusion: HSP-27, -60, and -90 were associated with certain clinicopathological parameters which are crucial for the management of gastric adenocarcinoma patient. HSP-90 expression may also be an independent prognostic indicator in gastric adenocarcinoma patients.

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Figures

Figure 1
Figure 1
Representative cases of HSPs protein expression in tumor cells of gastric adenocarcinoma: A. HSP-27 B. HSP-60. C. HSP-90 (original magnification ×200).
Figure 2
Figure 2
Kaplan-Meier survival analysis stratified according to HSP-90 expression in patients with gastric cancer. A. All cases. B. Subgroup of pN0 cases. C. Subgroup of G1/G2 cases. D. Subgroup of pM0 cases. (Red dashed line, high HSP-90 expression; Blue continuous line, low HSP-90 expression).
See this image and copyright information in PMC

References

    1. Tang D, Khaleque AA, Jones ER, Theriault JR, Li C, Wong WH, Stevenson MA, Calderwood SK. Expression of heat shock proteins and HSP messenger ribonucleic acid ih human prostate carcinoma in vitro and in tumors in vivo. Cell Stress Chaperones. 2005;10:46–59. - PMC - PubMed
    1. Hendrick JP, Hartl FU. Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem. 1993;62:349–384. - PubMed
    1. Calderwood SK, Khaleque MA, Sawyer DB, Ciocca DR. Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem Sci. 2006;31:164–172. - PubMed
    1. Soti C, Nagy E, Giricz Z, Vigh L, Csermely P, Ferdinandy. Heat shock proteins as emerging therapeutic targets. Br J Pharmacol. 2005;146:769–780. - PMC - PubMed
    1. Kiang JG, Tsokos GC. Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. Pharmacol Ther. 1998;80:183–201. - PubMed

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