Abstract
BackgroundHeat 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.MethodsHSP -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.ResultsHSP-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).ConclusionHSP-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.
Highlights
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
Tumors staging was assessed using the 5th edition of the Tumor, Node, Metastasis (TNM) system according to the Union Internationale Contra la Cancrum (UICC) and the American Joint Committee on Cancer (AJCC) [23]; they were classified asT1 (n = 9, 14%), T2 (n = 22, 33%), T3 (n = 29, 44%) and T4 (2 = 6, 9%)
HSP-27, -60, -90 proteins were abundantly expressed in gastric adenocarcinoma cases examined, presenting mainly a cytoplasmic and occasionally membraneous pattern of staining
Summary
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. Heat shock proteins (HSPs) are ubiquitous, highly conserved proteins across all species, which are strongly induced by heat shock and diverse environmental and physiopathological stresses [1,2]. HSPs constitute the products of several distinct genes commonly designated according to their mass [1,2,3]. Their principal function as molecular chaperones results in the maintenance of stability and delivery of other peptides, which are crucial for the protection of cellular integrity in normal and malignant cell growth. HSF forms a homotrimeric structure in the cytosol and translocate to the nucleus, binding to heat shock elements (HSEs) in order for the transactivation of heat shock-inducible genes to be elicited [4,5,6]
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