Significance Of Heat Shock Protein Research Articles

Clinicopathologic significance of heat shock protein 60 as a survival predictor in breast carcinoma.

While Heat Shock Protein 60 (HSP60) has been linked to human tumor, its clinic significance specifically in breast carcinoma is unclear. This investigation aims to retrospectively evaluate how HSP60 protein levels relate to survival outcomes among patients diagnosed with breast carcinoma. Evaluation of 206 patients diagnosed with breast carcinoma and receiving treatment from January 2012 to April 2018, carried out retrospectively. The protein level of HSP60 in breast carcinoma determined by immunohistochemical. The study provided evidence of a distinct upregulation of HSP60 expression in breast carcinoma tumor samples in contrast to adjacent normal tissue samples. Additionally, heightened HSP60 expression was linked to advanced T stage (P = 0.046), N stage (P = 0.034), tumor metastasis (P = 0.016), pathological grading (P = 0.012), and adjuvant therapy utilization (P = 0.004). Moreover, elevated levels of HSP60 proteins exhibited a significant inverse correlation with overall survival (OS) [hazard ratio (HR) 1.598, P = 0.018] and progression-free survival (PFS) (HR 1.600, P = 0.017) among breast carcinoma patients in univariate analyses. The results of multivariate analyses highlighted HSP60 may serve as an independent predictor for both OS and PFS in breast carcinoma patients (HR 1.525, P = 0.034; HR 1.528, P = 0.033, respectively). The involvement of HSP60 in breast carcinoma progression suggests its potential clinical relevance in treatment target validation and prognostic assessment of the disease.

Clinicopathologic Significance of Heat Shock Protein 60 as a Survival Predictor in Colorectal Cancer.

The role of heat shock protein 60 (HSP60), a mitochondrial chaperone, in tumor progression or its anti-tumor effects remains controversial. This study aimed to confirm the possibility of using HSP60 as a prognostic marker in patients with colorectal cancer (CRC), considering TNM classification for precise prediction. HSP60 expression increased with differentiation and p53 mutations in patients. However, compared to patients with high HSP60 expression, patients with low HSP60 expression had event-free survival and disease-specific survival hazard ratios (HRs) of 1.42 and 1.69, respectively. Moreover, when the survival rate was analyzed by combining TNM classification and HSP60 expression, the prognosis was poor, particularly when HSP60 expression was low in the late/advanced stage. This pattern was also observed with HSP family D member 1, HSPD1, the gene that encodes HSP60. Low HSPD1 expression was linked to lower overall survival and relapse-free survival rates, with HRs of 1.80 and 1.87, respectively. When TNM classification and HSPD1 expression were considered, CRC patients with low HSPD1 expression and advanced malignancy had a poorer prognosis than those with high HSPD1 expression. Thus, HSPD1/HSP60 can be a useful biomarker for a sophisticated survival prediction in late- and advanced-stage CRC, allowing the design of individualized treatment strategies.

A Review on the Involvement of Heat Shock Proteins (Extrinsic Chaperones) in Response to Stress Conditions in Aquatic Organisms.

Heat shock proteins (HSPs) encompass both extrinsic chaperones and stress proteins. These proteins, with molecular weights ranging from 14 to 120 kDa, are conserved across all living organisms and are expressed in response to stress. The upregulation of specific genes triggers the synthesis of HSPs, facilitated by the interaction between heat shock factors and gene promoter regions. Notably, HSPs function as chaperones or helper molecules in various cellular processes involving lipids and proteins, and their upregulation is not limited to heat-induced stress but also occurs in response to anoxia, acidosis, hypoxia, toxins, ischemia, protein breakdown, and microbial infection. HSPs play a vital role in regulating protein synthesis in cells. They assist in the folding and assembly of other cellular proteins, primarily through HSP families such as HSP70 and HSP90. Additionally, the process of the folding, translocation, and aggregation of proteins is governed by the dynamic partitioning facilitated by HSPs throughout the cell. Beyond their involvement in protein metabolism, HSPs also exert a significant influence on apoptosis, the immune system, and various characteristics of inflammation. The immunity of aquatic organisms, including shrimp, fish, and shellfish, relies heavily on the development of inflammation, as well as non-specific and specific immune responses to viral and bacterial infections. Recent advancements in aquatic research have demonstrated that the HSP levels in populations of fish, shrimp, and shellfish can be increased through non-traumatic means such as water or oral administration of HSP stimulants, exogenous HSPs, and heat induction. These methods have proven useful in reducing physical stress and trauma, while also facilitating sustainable husbandry practices such as vaccination and transportation, thereby offering health benefits. Hence, the present review discusses the importance of HSPs in different tissues in aquatic organisms (fish, shrimp), and their expression levels during pathogen invasion; this gives new insights into the significance of HSPs in invertebrates.

The significance of heat shock protein 27 in breast cancer: A signature to predict the outcome

Abstract Introduction: Heat shock protein (HSP) 27, if overexpressed in breast cancers, affects the disease outcome and sensitivity of tumors to chemotherapy and radiotherapy. There are limited studies on actual patients in India, so the present study was designed to contribute our experiences to the literature regarding HSP 27 expression and its significance in breast carcinoma. Materials and Methods: Thirty diagnosed cases of invasive duct carcinoma are evaluated for histopathology grade, stage, and expression of immune markers, namely, ER, PR, HER2, VEGF, and HSP 27, followed up to 2 years after primary management, especially if treated with Herceptin. The staining was evaluated, and data were analyzed using the χ2 and Fisher’s exact tests. Results: HSP 27 is expressed strongly in most ER- and PR-positive cases, but there is no correlation with Her2 and VEGF. The findings suggest more advanced disease, adverse outcomes, and lymph node metastasis. Moreover, these findings are directly related to strong HSP 27 expressions and shorter overall survival in the group of ER/PR-positive breast carcinoma cases, but this relation can be relied upon up to stage II disease. After that, in advance cases, HSP 27 loses its significance slowly and could not establish any link between HSP 27 and Herceptin resistance because of a short follow-up. Conclusion: HSP 27 proved a promising prognostic marker in ER/PR-positive breast carcinoma cases.

A Study of Heat Shock Protein 90 and Serum CCL21 Expression in Pregnant Women with Preeclampsia.

Objective The purpose of the study was to determine the significance of heat shock protein 90 (HSP 90) and serum chemokine ligand 21 (CCL-21) in pregnant women with preeclampsia (PE). Methods From June 2021 to June 2022, the study enrolled 100 women undergoing obstetric examinations and delivering in our hospital; 50 PE patients undergoing routine obstetric examinations and delivering during the same period were enrolled in the research group; according to the severity, they were divided into mild PE and severe PE groups, while 50 healthy pregnant women undergoing obstetric examinations and delivering in our hospital during the same period were enrolled in the control group. In a subsequent analysis, serum levels of CCL-21 and HSP90 were compared between the two groups, and the correlation among CCL-21, HSP 90, and PE severity was analyzed. Results An overall total of 50 patients with PE were enrolled in the study, which included 32 patients with mild PE and 18 patients with severe PE. Patients with severe PE had lower mean arterial pressure (MAP), HSP 90, and CCL21 index levels than those with mild PE; MAP, HSP 90, and CCL21 in the severe PE group were higher than those in the mild PE group, but the difference was not statistically significant; In the research group, MAP was weakly correlated with HSP90 concentration and CCL21 concentration, with correlation coefficients of 0.33 and 0.30, respectively, and the correlation analysis was significant. Conclusion Patients with PE showed significantly increased serum concentrations of HSP90 and CCL-21, but a significant difference did not exist between mild and severe PE. In addition, there was a weak relationship between HSP90 and CCL-21 concentrations in PE patients and MAP, suggesting that HSP90 and CCL-21 play an instrumental role in the pathogenesis of PE, although more studies are needed to clarify the exact mechanisms.

Relationship between HSP90 protein expression and overall survival and clinicopathological outcomes in gastric cancer patients

<br><b>Aim:</b> Gastric cancer is a highly prevalent public health problem with high morbidity and mortality. İts primary treatment is surgery. Recently, studies involving biological parameters and genetics in gastric cancer have been emerging but with many blind spots. Our study aims to investigate the clinicopathological and prognostic significance of heat shock proteins (HSP90) expression in patients with resectable gastric cancer.</br> <br><b>Methods:</b> Single-center retrospective clinical study conducted at the General Surgery Department of the local training and research hospital. Our study involves 54 patients who had curative surgery for gastric cancer between 2011 and 2014.</br> <br><b>Results:</b> Pathological specimens fixed in formalin and paraffin were re-evaluated with HSP90 staining and expression of HSP90 was evaluated. It was found that only 39 (72.2%) patients showed HSP90 expression. Seventeen (31.5%) of those showed mild, 13 (24.1%) had moderate, and 9 (10.5%) severe expression. HSP90 expression did not have a significant effect on survival in patients who underwent curative resection for gastric cancer, although statistically close. The effect of expression and intensity on overall survival was not statistically significant either.</br> <br><b>Conclusions:</b> There are various reports in literature on HSP90 expression in gastric cancer – some find it to be a prognostic factor, some not. There is a number of limitations of our study as we did not include metastatic tumors, the number of patients was low, the study involved only our patients and a single pathologist. This is the first study carried out in our population on this subject. Further studies could be done to evaluate this particular relationship in an effort to possibly identify novel treatments in gastric cancer.</br>

Expression and Clinical Significance of Heat Shock Protein 90 in Multiple Myeloma Patients

To investigate the expression of HSP90 in bone marrow samples of multiple myeloma (MM) patients and explore its clinical significance. Maxvision immunohistochemistry technique was used to detect the protein expression level of HSP90 76 MM patients and 29 normal healthy donors. The clinical characteristics of the patients were collected, and the correlation between the HSP90 expression and the clinical characteristics was analyzed. The count of MM patients with positive HSP90 protein was significantly higher than that of normal healthy donor, and there were no significant correlation between HSP90 expression and age, sex, hemoglobin (Hb), creatinine (CREA), blood calcium, lactate dehydrogenase (LDH), bone marrow plasma cell proportion and MM subtypes (P>0.05), but HSP90 expression was correlated with β2-microglobulin (β2-MG) and ISS stage (P<0.05). The survival time was lower in MM patients with high expression HSP90 as compared with low expression HSP90 MM patients. HSP90 protein was over-expressed in MM patients, and was correlated with β2-microglobulin, ISS stage and OS of MM patients.

Comparative In Silico Analysis of Randomly Selected Heat Shock Proteins in Caenorhabditis elegans and Photorhabdus temperata

Heat shock proteins (HSPs) such as HSP70A, HSP90 etc. (also known as Chaperons) play an important role in folding and unfolding of proteins, an assemblage of multiprotein complexes, transportation and sorting of proteins in subcellular compartments, cell cycle control, signaling pathways, protection against stress and programmed cell death. Studies have also linked heat shock proteins with a sudden rise in temperature, which can be related to anhydrobiosis in nematodes. Considering the significance of HSPs in nematodes and bacteria, the present study was designed for their in silico analysis in Caenorhabditis elegans and Photorhabdus temperata. The availability of a vast amount of sequence data generated through various bioinformatics tools, coupled with computational biology advancements, provides an ideal framework for silico gene expression and its analysis. A detailed in silico insight into these proteins include physicochemical properties, secondary structure prediction, homology modeling, and different models. The amino acid composition data were subjected to multivariate techniques, Pearson correlation, and phylogenetic analysis. In the present study, the authors characterized different HSPs according to different stability parameters and valid structures. A detailed in silico analysis of these proteins and prediction of their activity in different conditions can be very useful in both in vitro and in vivo experiments.

Clinicopathological Significance of Heat Shock Protein (HSP) 27 Expression in Gastric Cancer: A Updated Meta-Analysis.

Aim HSP27 is a protein chaperone protecting cell from heat shock, and upregulated HSP27 expression has been found in many different cancers. We conduct this update meta-analysis to evaluate the relationship between HSP27 expression and clinicopathological features. Methods We searched PubMed, Chinese CNKI, and WanFang databases to identify studies that assessed the association between clinicopathological feature and HSP27 expression in gastric cancer patients. Results We found overexpression of HSP27 was associated with incidence of gastric cancer (OR = 6.31, 95% CI = 1.10–36.15, P < 0.0001). However, there was no significant difference between HSP27 expression and gastric cancer differentiation, gender difference, lymph node metastasis, and distant metastasis. Conclusion Our meta-analysis study indicates that overexpression of HSP27 is associated with incidence of gastric cancer statistically.

Clinical and pathogenetic significance of heat shock protein in alopecia areata

Clinical and pathogenetic significance of heat shock protein in alopecia areata

High altitude hypoxia on brain ultrastructure of rats and Hsp70 expression changes

Objective: This study aims to investigate the biological significance of heat shock protein (HSP70) in adaptation to high altitude hypoxia.Methods: Ninety male SD rats were randomly divided into 10 groups: Acute plateau hypoxia group (group 5) and chronic high altitude hypoxia group (group 3), and control group (group 2).Changes in HSP gene and HSP protein expression in brain tissues of SD rats at different altitudes were determined by Western blot and conventional RT-PCR, while an optical and transmission electron microscope was used to observe the cell structure changes of animal brain tissues.Results: HSP70 expression rapidly increased at high altitudes in SD rats under high-altitude hypoxia environments, and HSP70 increased with altitude. Morphological and structural damage in SD rats in each group increased with altitude.Conclusion: The rapid synthesis of HSP70 in heat shock response is beneficial for maintaining the normal physiological function of cells during hypoxia stress, and the amount of HSP70 production is positively correlated with hypoxia tolerance ability.

The Significance of Heat Shock Protein 70 Expression in Benign Thyroid Nodules During Thermal Ablation

The Significance of Heat Shock Protein 70 Expression in Benign Thyroid Nodules During Thermal Ablation

Clinical, Prognostic and Therapeutic Significance of Heat Shock Proteins in Cancer.

Heat Shock Proteins (HSPs) constitute a group of proteins that play a crucial role in the process of protein folding. HSPs are also known to modulate a number of key apoptotic factors. High expression of these proteins is reported in an array of cancers, such as breast, prostate, colorectal, lung, ovarian, gastric, oral and esophageal cancer. Ample amount of investigations were carried out on a variety of cancers suggesting HSPs as a promising hallmark in cancers. Their expression profile in several tumors elucidates that they help in proliferation, invasion, metastasis and death of cancerous cells. Detection of the levels of heat shock proteins and their specific antibodies in the sera of diseased individuals can play an important role in cancer diagnosis. This review will present and summarize latest research being carried out on heat shock proteins. It will also highlight the clinical and prognostic features of HSP27, HSP60, HSP70, HSP90 and HSP110, and will discuss future implications of HSPs in the diagnosis and prognosis of cancer. Furthermore, the role of heat shock proteins as a therapeutic target in cancer will be discussed. In addition, the review article will report various studies, where HSPs have been targeted for their therapeutic potential. In summary, multiple experimental investigations have been successful in suggesting the role of heat shock protein as a clinical biomarker and therapeutic target in cancer. HSPs are associated with a number of cancer hallmarks such as cell proliferation, invasion and metastasis. Inhibition of HSPs has resulted in successful therapeutic outcome in cancer. It has served as a novel anti-cancer therapy for the treatment of several cancer forms. However, more experimental studies are required to elucidate the reliability and efficacy of heat shock proteins in combination with other conventional markers for cancer diagnosis and prognosis. Novel and effective interventions through HSP inhibition are expected to decrease the burden of cancer in the near future.

The protein-protein interaction network and clinical significance of heat-shock proteins in esophageal squamous cell carcinoma.

Heat-shock proteins (HSPs), one of the evolutionarily conserved protein families, are widely found in various organisms, and play important physiological functions. Nevertheless, HSPs have not been systematically analyzed in esophageal squamous cell carcinoma (ESCC). In this study, we applied the protein-protein interaction (PPI) network methodology to explore the characteristics of HSPs, and integrate their expression in ESCC. First, differentially expressed HSPs in ESCC were identified from our previous RNA-seq data. By constructing a specific PPI network, we found differentially expressed HSPs interacted with hundreds of neighboring proteins. Subcellular localization analyses demonstrated that HSPs and their interacting proteins distributed in multiple layers, from membrane to nucleus. Functional enrichment annotation analyses revealed known and potential functions for HSPs. KEGG pathway analyses identified four significant enrichment pathways. Moreover, three HSPs (DNAJC5B, HSPA1B, and HSPH1) could serve as promising targets for prognostic prediction in ESCC, suggesting these HSPs might play a significant role in the development of ESCC. These multiple bioinformatics analyses have provided a comprehensive view of the roles of heat-shock proteins in esophageal squamous cell carcinoma.

Clinical significance of heat shock proteins in gastric cancer following hyperthermia stress: Indications for hyperthermic intraperitoneal chemoperfusion therapy.

Heat shock proteins (HSPs) are important factors in the response of cancer cells to thermo- and chemotherapy. Transient hyperthermic intraperitoneal chemoperfusion (HIPEC) therapy results in the upregulation of HSP expression, which may compromise the efficacy of additional anticancer treatments. The aim of the present study was to monitor the kinetics of HSP expression in tumor cells and patients with gastric cancer following HIPEC. Thus, in vitro and in vivo experiments were conducted to investigate the expression of two HSP family members, HSP70 and HSP90. Cells from two gastric tumor strains were subjected to HIPEC-mimicking treatment, and HSPs expression was analyzed at specific time points up to 48 h. Serum HSP concentrations were analyzed in patients with gastric cancer who had previously received cytoreductive surgery plus HIPEC treatment. The in vitro experiments indicated a significant elevation of HSP90 expression in gastric adenocarcinoma cells following hyperthermic treatment. However, HSP70 expression increased from 4 h up to 20 h post-exposure and decreased to normal levels 36 h post-exposure. Analysis of HSPs in serum samples collected from 22 patients with gastric cancer confirmed that serum HSP90 and HSP70 levels increased following HIPEC therapy, peaking at 18 h and returning to normal 24 h post-exposure. It is therefore advisable to apply the second round of HIPEC or chemotherapy at least 24 h following the first treatment to minimize any potential thermoresistance and chemoresistance of tumor cells.

Clinical, prognostic, and therapeutic significance of heat shock protein 27 in bladder cancer.

Heat shock protein 27 (HSP27) is highly expressed in many cancers, and its prognostic and predictive value has been reported. HSP27 knockdown using siRNA or OGX-427 (an anti-sense oligonucleotide sequence targeting HSP27) is reported to have anti-cancer effects and to enhance chemosensitivity of cancer cells to chemotherapeutic agents. However, conflicting results have been reported regarding the clinical significance of HSP27 in bladder cancer (BC). Furthermore, long-term suppression of HSP27 has not been investigated in BC. In this study, we investigated the association between HSP27 expression and BC characteristics in 132 BC patient samples, as well as its prognostic value to determine the potential of HSP27 as a clinical biomarker. Additionally, we applied five different shRNAs targeting HSP27 in three invasive BC cell lines to analyze the long-term knockdown effects of HSP27. Our study revealed a significant association between HSP27 expression and adverse pathological characteristics such as high-stage and -grade BC. However, HSP27 expression was not associated with clinical outcomes such as tumor recurrence, progression, and patient survival. Interestingly, although our shRNAs had obvious knockdown effects on HSP27 in BC cells, we did not find consistent effects on apoptosis of BC cells or chemotherapeutic sensitivity of BC cells to cisplatin. Therefore, although HSP27 may be a predictor of adverse pathological characteristics in BC, its role as a prognostic biomarker and therapeutic target seems to be limited.

Nuclear heat shock protein 110 expression is associated with poor prognosis and hyperthermo-chemotherapy resistance in gastric cancer patients with peritoneal metastasis.

AIMTo investigate the significance of heat shock protein 110 (HSP110) in gastric cancer (GC) patients with peritoneal metastasis undergoing hyperthermo-chemotherapy.METHODSPrimary GC patients (n = 14) with peritoneal metastasis or positive peritoneal lavage cytology who underwent distal or total gastrectomy between April 2000 and December 2011 were enrolled in this study. The patients underwent postoperative intraperitoneal hyperthermo-chemotherapy using a Thermotron RF-8 heating device two weeks after surgery. We analyzed nuclear HSP110 expression in surgically resected tumors using immunohistochemistry. Additionally, the effect of HSP110 suppression on hyptherthermo-chemosensitivity was assessed in vitro in the MKN45 GC cell line using the HSP inhibitor KNK437.RESULTSHSP110 immnohistochemical staining in 14 GC patients showed that five (35.7%) samples belonged to the low expression group, and nine (64.3%) samples belonged to the high expression group. Progression-free survival was significantly shorter in the HSP110 high-expression group than in the low-expression group (P = 0.0313). However, no significant relationships were identified between HSP110 expression and the clinicopathological characteristics of patients. Furthermore, high HSP110 expression was not an independent prognostic factor in GC patients with peritoneal metastasis (P = 0.0625). HSP110 expression in MKN45 cells was suppressed by KNK437 at the hyperthermic temperature of 43 °C in vitro. Comparison of MKN45 cell proliferation in the presence and absence of KNK437 at 43 °C, revealed that proliferation was significantly decreased when HSP110 was inhibited by KNK437. Additionally, HSP110 suppression via HSP inhibitor treatment increased cellular sensitivity to hyperthermo-chemotherapy in vitro.CONCLUSIONThe expression of nuclear HSP110 in GC patients might be a new marker of chemosensitivity and a therapeutic target for patients who are tolerant to existing hyperthermo-chemotherapies.

Clinicopathological and prognostic significance of heat shock protein 27 (HSP27) expression in non-small cell lung cancer: a systematic review and meta-analysis.

Numbers of clinical and experimental investigations have provided increasing evidences to demonstrate that heat shock protein 27 (HSP27) is a qualified predictor for many cancers. However, no consensus has been reached on its clinicopathological and prognostic significance in patients with non-small cell lung cancer (NSCLC). Therefore, we performed this systematic meta-analysis to help addressing this issue. PubMed, EMBASE, the Web of Science and China National Knowledge Infrastructure were searched for full-text literatures met out eligibility criteria. We determined the odds ratio (OR) and hazard ratio (HR) as the appropriate summarized statistics for assessments of clinicopathological and prognostic roles of HSP27, respectively. Q-test and I2-statistic were used to evaluate the level of heterogeneity. Sensitivity analysis was conducted to examine the stability of overall estimates. Potential publication bias was detected by Begg’s test and Egger’s test. Finally, ten articles were identified to be included into our meta-analysis. The pooled analyses suggested that HSP27 expression was significantly associated with the unfavorable conditions for differentiation degree, lymphatic metastasis, clinical stage, squamous cell carcinoma and tumor size. However, HSP27 expression had no significant relationship to gender, age and smoking status. Meanwhile, pooled HRs indicated that HSP27 expression could be a predictor for a lower 5-year overall survival (OS) rate (HR: 1.832; 95 % CI 1.322–2.538; P < 0.001) but not for 1-year OS of NSCLC (HR: 0.885; 95 % CI 0.140–5.599; P = 0.896). In conclusion, our meta-analysis demonstrates that HSP27 expression may be a strong biomarker to predict both the poor clinicopathological and prognostic characteristics in patients with NSCLC.Electronic supplementary materialThe online version of this article (doi:10.1186/s40064-016-2827-8) contains supplementary material, which is available to authorized users.

Context- and time-dependent neurobiological and behavioral sensitization induced by a single morphine exposure in mice.

Drug-induced sensitization in the mesocorticolimbic systems is thought to play an important role in certain aspects of drug addiction, including the involvement of drug-associated cues and environments in mediating drug-seeking behaviors. Our previous studies have identified the significance of heat shock protein 70 (Hsp70) in the development of a single morphine exposure-induced behavioral sensitization. The present study expands upon these findings by investigating the effect of environment on the expression of behavioral sensitization induced by a single morphine exposure, and the potential involvement of Hsp70 protein levels in these effects. Mice were pretreated with a single morphine injection in test chambers (morphine-paired) or home cages (morphine-unpaired) on day 1 and challenged on day 2 or 8, in test chambers. Hsp70 expression in the nucleus accumbens (NAc) was analyzed after the challenge. The expression of single morphine exposure-induced behavioral sensitization was accompanied by a significant increase in Hsp70 expression in NAc. In contrast, the unpaired morphine-treated group failed to exhibit behavioral sensitization or higher Hsp70 expression. Additionally, by adding a habituation process prior to the challenge, we demonstrated that conditioned hyperactivity, which was not accompanied by an increased expression of Hsp70, is not essential for behavioral sensitization. Behavioral sensitization induced by a single morphine exposure in mice exhibits context and time dependency, with environmental context likely functioning via an inhibitory conditioning mechanism. Furthermore, alterations in Hsp70 expression in the NAc may represent a neurobiological sensitization mechanism mediating context- and time-dependent behavioral sensitization.

Heat Shock Proteins as Prognostic Markers of Cancer

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.