Presence of antibody against the inducible Hsp71 in patients with acute heat-induced illness
Tangchun WuSheng ChenChengfeng XiaoWang Chang-laiQin PanZizheng WangMin XieZhicheng MaoYang WuRobert M. Tanguay
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Pathogenesis
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The family of HSP60 belongs to heat shock proteins with highly species conservatism and some important biologic functions. It can help other proteins for their assembling, folding and translocating, and plays a role in protecting cells against injuries and other types of stress. In addition, HSP60 is frequently recognized by the immune system as predominant antigens during infections and the progression of certain autoimmune diseases and might provide a novel strategy for the development of immunotherapeutics. This review focuses on distribution, molecular chaperone mechanism, function and gene expression regulation of HSP60. [
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Heat shock proteins (HSPs) are highly conserved molecular chaperones with divergent roles in various cellular processes. The HSPs are classified according to their molecular size as HSP27, HSP40, HSP60, HSP70, and HSP90. The HSPs prevent nonspecific cellular aggregation of proteins by maintaining their native folding energetics. The disruption of this vital cellular process, driven by the aberrant expression of HSPs, is implicated in the progression of several different carcinomas. Many HSPs are also actively involved in promoting the proliferation and differentiation of tumor cells, contributing to their metastatic phenotype. Upregulation of these HSPs is associated with the poor outcome of anticancer therapy in clinical settings. On the other hand, these highly expressed HSPs may be exploited as viable immunotherapeutic targets for different types of cancers. This review discusses recent advances and perspectives on the research of HSP-based cancer immunotherapy.
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Abstract : Heat illnesses range in severity form mild (heat rash, heat syncope, cramps) to serious (heat exhaustion, heat injury, heat stroke). Although heat illness can occur in anyone, an increased risk is associated with a variety of environmental factors, personal characteristics, health conditions, and medications. The risk of serious heat illness can be markedly reduced by implementing a variety of countermeasures, including becoming acclimated to the heat, managing heat stress exposure, and maintaining hydration. Athletes, coaches, training staff, and medical personnel should be vigilant for signs and symptoms of heat related illnesses. If warning signs are acted upon and body cooling rapidly administered, serious heat illness can be avoided. If heat stroke is suspected, rapid body cooling by immersion or soaking in cold water or ice water should be initiated.
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Cardiovascular disease (CVD) is a leading cause of morbidity and mortality worldwide. There is growing evidence that molecular chaperones, many of which are heat shock proteins HSPs, are involved in CVD pathogenesis. In this review we focus on HSP60, the human mitochondrial chaperone that also displays extramitochondrial and extracellular functions. HSP60 is typically cytoprotective but a number of stress conditions determine its conversion to a potentially toxic molecule for cells and tissues. We present illustrative examples of specific subtypes of CVD where HSP60 is implicated in the initiation and/or progression of disease. The data not only indicate a pathogenic role for HSP60 but also its potential as a biomarker with applications for diagnosis, assessing prognosis and response to treatment, as well as for preventing and treating CVD. Keywords: Chaperonin, heat shock protein 60, cardiomyocytes, heart failure, cardiovascular disease, atherosclerosis, apoptosis, microRNAs (miRs), diabetes, Atrial fibrillation
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A high percentage of oesophageal adenocarcinomas show an aggressive clinical behaviour with a significant resistance to chemotherapy. Heat-shock proteins (HSPs) and glucose-regulated proteins (GRPs) are molecular chaperones that play an important role in tumour biology. Recently, novel therapeutic approaches targeting HSP90/GRP94 have been introduced for treating cancer. We performed a comprehensive investigation of HSP and GRP expression including HSP27, phosphorylated (p)-HSP27(Ser15), p-HSP27(Ser78), p-HSP27(Ser82), HSP60, HSP70, HSP90, GRP78 and GRP94 in 92 primary resected oesophageal adenocarcinomas by using reverse phase protein arrays (RPPA), immunohistochemistry (IHC) and real-time quantitative RT-PCR (qPCR). Results were correlated with pathologic features and survival. HSP/GRP protein and mRNA expression was detected in all tumours at various levels. Unsupervised hierarchical clustering showed two distinct groups of tumours with specific protein expression patterns: The hallmark of the first group was a high expression of p-HSP27(Ser15, Ser78, Ser82) and low expression of GRP78, GRP94 and HSP60. The second group showed the inverse pattern with low p-HSP27 and high GRP78, GRP94 and HSP60 expression. The clinical outcome for patients from the first group was significantly improved compared to patients from the second group, both in univariate analysis (p = 0.015) and multivariate analysis (p = 0.029). Interestingly, these two groups could not be distinguished by immunohistochemistry or qPCR analysis. In summary, two distinct and prognostic relevant HSP/GRP protein expression patterns in adenocarcinomas of the oesophagus were detected by RPPA. Our approach may be helpful for identifying candidates for specific HSP/GRP-targeted therapies.
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Our recent studies have been focused on the expression and cytoprotective function of heat shock proteins (HSPs) mediated by their function as a molecular chaperone in digestive organs. We have reported that HSP72 (72-kDa heat shock protein, stress-inducible HSP70) has crucial function in the gastric mucosa, colonic mucosa and the liver. In the pancreas, we proved that HSP60 (60-kDa heat shock protein, chaperonin homolog) has cytoprotective function. These evidences lead us to develop effective “chaperone-inducing therapy” including drugs, chemicals and gene therapies which might effective for disease therapy enhancing not only cytoprotective ability but also tissue restoration. In this review, we introduce our previous data.
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This review systematically examines the literature and data on the prognostic significance of heat shock proteins (heat shock protein - Hsp) Hsp27, Hsp60, Hsp70, Hsp90 in various cancers. Our analysis of the literature showed that the existing data are contradictory with regard to the prognostic significance of Hsp. This result may be due to biological differences of the carcinomas studied and methodological differences in the assessment of heat shock proteins. Heat shock proteins play a significant role in the development of cancer, as they are highly expressed and thus allow tumor cells to escape apoptotic death. Therefore, the inhibition of Hsps is currently an attractive potential therapeutic approach against cancer. Keywords: Cancer, heat shock proteins, Hsp27, Hsp60, Hsp70, Hsp90, prognostic markers.
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