PURPOSE: To investigate if the use of the infrared warm compression device often used in clinical settings induced heat shock proteins. METHODS: Subjects were heat-treated with an infrared warm compression device for 20 minutes. We examined the temperature of the upper eyelid and cornea before and after heat treatment and images were obtained by Digital Infrared Thermal Imaging System. After 6 hours of heat treatment, conjunctival epithelial cells were obtained by gently pressing nitrocellulose paper on the conjunctival surface for 3 to 5 seconds Immunocytochemical staining analysis was performed on the obtained samples. Tear samples were obtained prior to heat treatment and Western blot was performed to observe the expression patterns of heat shock proteins 27, 47, 70, and 90. RESULTS: By Western blot and immunocytochemical analysis, heat shock proteins 70 and 27 were significantly increased in the heat-treated samples. However, no difference was observed for heat shock proteins 47 and 90 before and after heat treatment, according to the immunocytochemical analysis. On Western blot, heat shock protein 47 was slightly increased by heat treatment but heat shock protein 90 did not show a significant difference after heat treatment. CONCLUSIONS: It was observed that the infrared warm compression device significantly increased the induction of heat shock proteins 27 and 70, and that 47 was also slightly induced. This result suggests that the device developed herein could be used as a new therapeutic modality for the reduction of inflammatory cell injury through the induction of heat shock proteins.
Blotting, Western ; Collodion ; Cornea ; Epithelial Cells ; Eyelids ; Heat-Shock Proteins* ; Hot Temperature* ; HSP27 Heat-Shock Proteins ; HSP47 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins

OBJECTIVETo investigate the expression and significance of HSP27, HSP60, HSP70 and HSP90 alpha in esophageal squamous cell carcinoma (ESCC) and tissues along the incision margin (TIM).

METHODSThe presence and the level of expression of HSP27, HSP60, HSP70 and HSP90 alpha were determined in 168 specimens from ESCC and 42 from tissues along TIM by EnVision immunohistochemistry and Western blotting, to compare their positive staining rates and explore the correlation between their expressions and clinicopathologic features in ESCC.

RESULTSThe positive staining rates of HSP27, HSP60, HSP70 and HSP90 alpha in ESCC and TIM were 62.0% and 42.1%, 92.7% and 63.2%, 57.9% and 22.2%, and 33.7% and 18.5%, respectively. There was very significant difference between the expression of HSP60 and HSP70 in ESCC and TIM (P < 0.01), but not significant about HSP27 and HSP90 alpha (P > 0.05). The positive staining rate of HSP27 declined with the lower grade of differentiation of ESCC (P < 0.05).

CONCLUSIONThe present findings suggest that the expression of HSPs of different molecular weight in ESCC and TIM is a common event. The level of expressions of HSP60 and HSP70 are higher than those in TIM. HSP60 and HSP70 expression correlated with the biological behavior of ESCC. The expression of HSP27 was positively correlated to the grade of differentiation of ESCC. Overexpression of HSP27 may be associated to the differentiation of squamous cell carcinoma.

Blotting, Western ; Carcinoma, Squamous Cell ; metabolism ; pathology ; Cell Differentiation ; Chaperonin 60 ; metabolism ; Chi-Square Distribution ; Esophageal Neoplasms ; metabolism ; pathology ; Esophagus ; chemistry ; pathology ; HSP27 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; metabolism ; HSP90 Heat-Shock Proteins ; metabolism ; Heat-Shock Proteins ; metabolism ; Humans ; Immunohistochemistry ; Lymphatic Metastasis ; Neoplasm Invasiveness ; Neoplasm Proteins ; metabolism

OBJECTIVETo establish a RT-PCR system for detecting mRNA expression level of 4 hsp genes in human cells.

METHODSRT-PCR system was established with gene cloning, gene recombination, in vitro transcription and RT-PCR techniques; The detection of expression level of 4 hsp genes in SW13 cell was carried out with this system.

RESULTSIn SW13 cell, hsp70 and hsp90 alpha were typical heat shock induced genes, while hsp60 and hsp90 beta were efficiently expressed and further induced by heat-shock to various extent.

CONCLUSIONSIn our hands novel RT-PCR system can be used to detect mRNA expression level of 4 human hsp genes.

Chaperonin 60 ; biosynthesis ; genetics ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; biosynthesis ; genetics ; HSP90 Heat-Shock Proteins ; biosynthesis ; genetics ; Heat-Shock Proteins ; biosynthesis ; genetics ; Humans ; Leukemia, T-Cell ; metabolism ; pathology ; RNA, Messenger ; biosynthesis ; genetics ; Reverse Transcriptase Polymerase Chain Reaction ; Tumor Cells, Cultured

PURPOSE: The purposes of study were to assess the expression patterns of heat shock protein (HSP) after glutamine and glutamine with non- lethal heat shock treatment, to evaluate the protective effects of heat shock protein from apoptosis in cultured human corneal epithelial cell. METHODS: The cultured human corneal epithelial cells were divided into two group. One group was treated with 0, 10, 20, 30, 40, 50 mM of glutamine and the other group was exposed to 43 degrees C (heat shock) for 30 minutes with same concentration of glutamine. After glutamine and heat treatment, the expression patterns of Hsp 27, 70 were examined by western blot and immunohistochemistry. Apoptosis was induced with 80uM of etoposide. The viability (cell protection rate of heat shock protein) against apoptosis after etoposide treatment was measured by 3-[4, 5-dimethylthiazol-2-yl]-2, 5-diphenyltetrazolium bromide (MTT) assay. RESULTS: Expression of Heat shock protein 70 was not significantly effected in only glutamine treatment, but was remarkably increased in heat shock with glutamine treatment group. The increased cell number (viability= antiapoptotic effect of heat shock protein)of glutamine with heat shock group after etoposide treatment suggested that Hsp 70 appeared to be a major role in protection of Human corneal epithelial cell from apoptosis. The expression of Heat shock protein 27 was not effected in only glutamine and heat with glutamine treatment group. CONCLUSIONS: These data suggest that induced heat shock protein protect etoposide-generated apoptosis in human corneal epithelial cell.
Apoptosis ; Blotting, Western ; Cell Count ; Epithelial Cells* ; Etoposide ; Glutamine ; Heat-Shock Proteins* ; Hot Temperature* ; HSP27 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; Humans* ; Immunohistochemistry ; Shock

PURPOSE: Heat shock proteins (HSPs) are highly conserved molecular chaperones. There are various studies that assess the prognostic value of HSPs in patients with esophageal cancer, but the conclusion remains controversial. This is the first meta-analysis study aiming to summarize the evidence on the suitability of HSPs to predict patients' survival. MATERIALS AND METHODS: Searching PubMed, Web of science and Medline until May 31, 2014, data were compared for overall survival in patients with down-regulated HSPs level with those with up-regulated level. We conducted a meta-analysis of 9 studies (801 patients) that correlated HSPs levels with overall survival. Data were synthesized with hazard ratios (HRs). RESULTS: The estimated risk of death was 2.93-fold greater in HSP27 negative patients than HSP27 positive patients [95% confidence interval (CI), 1.12-7.62]. When limited to esophageal squamous cell carcinoma (ESCC), the risk of death in HSP27 negative patients seemed more significant (HR, 3.90; 95% CI, 2.35-6.49). Decreased expression of HSP70 was also associated with worse survival in esophageal cancer (HR, 2.83; 95% CI, 1.90-4.23) and, when limited to ESCC, HR was 3.21 (95% CI, 1.94-5.30). Data collected, however, were not sufficient to determine the prognostic value of HSP90 in patients with ESCC nor esophageal adenocarcinomas (EADC). CONCLUSION: In this meta-analysis, reduced HSP27 and HSP70 expressions were associated with poor survival in patients with esophageal cancer, especially esophageal squamous cell carcinoma.
Adenocarcinoma/*diagnosis/*metabolism/mortality ; Carcinoma, Squamous Cell/diagnosis/*metabolism/therapy ; Esophageal Neoplasms/*diagnosis/*metabolism/mortality/therapy ; Gene Expression Regulation, Neoplastic ; HSP27 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; HSP90 Heat-Shock Proteins ; Heat-Shock Proteins/*metabolism ; Humans ; Male ; Neoplasm Proteins ; Prognosis ; Survival ; Treatment Outcome

Adult ; Female ; HSP27 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; biosynthesis ; blood ; HSP90 Heat-Shock Proteins ; biosynthesis ; blood ; Heat-Shock Proteins ; biosynthesis ; blood ; Hepatitis B Core Antigens ; blood ; Hepatitis B, Chronic ; metabolism ; pathology ; Humans ; Liver ; metabolism ; pathology ; Male ; Middle Aged ; Neoplasm Proteins ; biosynthesis ; blood

Proteins in DNAJ/K families are ubiquitous, from prokaryotes to eukaryotes, and function as molecular chaperones. For systematic phylogenomics of the DNAJ/K families, we developed the Eukaryotic DNAJ/K Database (EDD). A total of 12,908 DNAJs and 4,886 DNAKs were identified from 339 eukaryotic genomes in the EDD. Kingdom-wide comparison of DNAJ/K families provides new insights on the evolutionary relationship within these families. Empowered by 'class', 'cluster', and 'taxonomy' browsers and the 'favorite' function, the EDD provides a versatile platform for comparative genomic analyses of DNAJ/K families.
Eukaryota ; Genome ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; Humans ; Molecular Chaperones ; Proteins

OBJECTIVE: To analyze HSP70/HSP27 protein expression in the nasopharyngeal carcinoma (NPC) primary tissues and the residual lesion, and to explore its predictive value. METHODS: Immunohistochemical experiment was performed to detect the expression of HSP70 and HSP27 in 58 NPC primary tissues: 28 were in the experimental group with the local residual lesion and 30 in the control group without recurring and metastasis within 5 years by conventional radiotherapy. RESULTS: The positive expression of HSP70 and HSP27 in the experimental group was 92.9%(26/28) and 53.6%(15/28), while that in the control group was 53.3%(16/30) and 53.3%(16/30),respectively. There was significant difference in the 2 groups. The common positive expression of HSP70 and HSP27 between the 2 groups had significant difference, 50.0% (14/28) in the experimental group and 16.7% (5/30) in the control group, respectively. There was no significant difference in the negative ratio of HSP70 and HSP27 common expression between the 2 groups, 3.6% (1/28) in the experimental group and 10.0% (3/30) in the control group, respectively. CONCLUSION HSP70 may have an important role in the radioresistance of NPC, and may predict the residual lesion after radiotherapy.
Adult ; Aged ; Carcinoma, Squamous Cell ; metabolism ; radiotherapy ; Female ; HSP27 Heat-Shock Proteins ; metabolism ; HSP70 Heat-Shock Proteins ; metabolism ; Humans ; Male ; Middle Aged ; Nasopharyngeal Neoplasms ; metabolism ; radiotherapy ; Young Adult

OBJECTIVETo study the expression and the possible role of JWA protein in oxidative stress-induced damage of MCF-7 cells, especially the relationship between JWA and heat shock proteins (HSPs).

METHODSMCF-7 cells were exposed to different concentration of H(2)O(2) (0.01,0.10, 1.00 mmol/L) for different time (10, 30, 60 and 180 min) respectively. DNA damage was detected by using DNA gel electrophoresis. The MTT assay was used to analyze the effect of H(2)O(2) on the cytotoxicity and relative cell proliferation ratio of the cells. The expressions of JWA, HSP70, HSP27 and HSF1 were determined by Western-blot.

RESULTSThe inhibitory effect on MCF-7 cells viability induced by H(2)O(2) was shown a dose-and time-dependent manner and MCF-7 cells proliferation, and was almost completely inhibited by the exposure of H(2)O(2) at 1.00 mmol/L for 180 min. Hydrogen peroxide treatment of MCF-7 cells caused oxidative stress which up-regulated the expressions of JWA, HSP70 and heat shock factor 1 (HSF1) in a dose-dependent manner, and the expression pattern of JWA was very similar to those of HSP70 and HSF1 but not to HSP27.

CONCLUSIONJWA might enhance intracellular defenses against H(2)O(2)-induced oxidative damage in human breast carcinoma cells. JWA is determined functioning as an effective environmental responsive protein and as a parallel molecule of HSP70 actively participates in the signal pathways of oxidative damage which might be regulated by HSF1.

Cell Line, Tumor ; DNA Damage ; drug effects ; DNA-Binding Proteins ; biosynthesis ; Dose-Response Relationship, Drug ; Female ; HSP27 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; biosynthesis ; Heat Shock Transcription Factors ; Heat-Shock Proteins ; biosynthesis ; Humans ; Hydrogen Peroxide ; adverse effects ; Intracellular Signaling Peptides and Proteins ; Neoplasm Proteins ; biosynthesis ; Oxidative Stress ; drug effects ; Transcription Factors ; biosynthesis ; Up-Regulation

OBJECTIVETo explore the relationship between the expression of heat shock protein 90, 60 and 27 (HSP90, HSP60 and HSP27) and genetic damage in peripheral blood of workers exposed to coke oven emissions.

METHODS288 coke oven workers in a steel factory were divided into the high-dose group and the low-dose group on the basis of environment monitoring result and work place. There were 172 men in high-dose group (workers who worked at the oven top and oven side) and 116 men in low-dose group (workers who worked at the oven bottom and others who were engaged to aided work). 38 workers unexposed occupationally to carcinogenic substances were selected as the control group, who were employed in medical therapy unit nearby 2 kilometers from the steel factory. Their general information, history of personal and occupational exposure, and the work environment were investigated. Blood samples were collected immediately after a shift at the end of a working day from 288 coke oven workers and 38 control workers. Levels of HSP90, HSP60 and HSP27 in peripheral blood lymphocytes were measured by Western blot, and the degree of DNA damage was detected by the comet assay.

RESULTSLevels of HSP90 in peripheral blood lymphocytes in three groups were 0.24 +/- 0.32, 0.12 +/- 0.30 and 0.06 +/- 0.33 respectively. They increased significantly compared with that of the control. But levels of HSP60 and HSP27 were not significantly different among those groups. Compared with the control group, there was significant difference in tail length, olive tail moment et al of SCGE (G +/- s(G)) of occupational exposure workers. High-dose group > low-dose group > control group (P < 0.05). The degree of DNA damage increased with the rise of exposure BaP dose (Spearman r = -0.345, P < 0.01).

CONCLUSIONLevels of HSP90 in peripheral blood lymphocytes and the degree of DNA damage increase with the rise of exposure polycyclic aromatic hydrocarbons (PAHs) dose.

Adult ; Chaperonin 60 ; blood ; Coke ; adverse effects ; Comet Assay ; DNA Damage ; drug effects ; HSP27 Heat-Shock Proteins ; blood ; HSP90 Heat-Shock Proteins ; blood ; Humans ; Lymphocytes ; metabolism ; Male ; Occupational Exposure ; adverse effects ; Polycyclic Aromatic Hydrocarbons ; adverse effects