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

<b>OBJECTIVEb>To 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).

<b>METHODSb>The 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.

<b>RESULTSb>The 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).

<b>CONCLUSIONb>The 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

Heat shock protein 27 (HSP27) and alpha B crystallin (aBC) belong to the small heat shock protein (sHSP) family and have similar amino acid sequences. However, no study has compared the distributional patterns of these two sHSPs in the retina and optic nerve. In this study, we compared the spatiotemporal distributions of the expressions of HSP27 and aBC in the developing chick retina and optic nerve. Both HSP27 and aBC were first expressed in the retina and optic nerve at embryonic day 16 (E16). At E20 the expressions of the two proteins were increased in the retina and optic nerve. Double immunofluorescence demonstrated that HSP27 and aBC were expressed in oligodendrocytes of the retina and optic nerve. In addition, HSP27 was also found to be expressed in ganglion cells in the retina. The findings of this study suggest that HSP27 and aBC act to protect ganglion cells and oligodendrocytes during late development of the chick retina and optic nerve.
alpha-Crystallin B Chain* ; Amino Acid Sequence ; Animals ; Chick Embryo* ; Fluorescent Antibody Technique ; Ganglion Cysts ; Heat-Shock Proteins ; HSP27 Heat-Shock Proteins* ; Humans ; Oligodendroglia ; Optic Nerve* ; Retina*

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

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

Heat shock proteins (HSPs) form the most ancient defense system in all living organisms. These proteins act as molecular chaperones by helping the refolding of misfolded proteins and assisting their elimination if they become irreversibly damaged. HSPs interact with a number of cellular systems and form efficient cytoprotective mechanisms. HSPs allow cells to adapt to gradual changes in their environment and to survive in otherwise lethal conditions. The events of cell stress and cell death are linked, and HSPs induced in response to stress appear to function at key regulatory points in the control of apoptosis. HSPs include antiapoptotic and proapoptotic proteins that interact with a variety of cellular proteins. Their expression levels can determine the fate of the cell in response to death stimulus. On the other hand, HSPs are overexpressed in tumor cells, and the inhibition of HSP90 has recently been regarded as a very promising tool to combat various cancers. HSPs can be secreted to circulatory system from a variety of cell types in response to stress. The secreted exogenous proteins act as cytokines and have potential modulatory functions in immune system. Cell surface-bound HSP70 can render tumor cell more sensitive to natural killer cell-mediated cytolytic attack. Therefore, modulator of chaperone activities is becoming a new target of drug development, such as in apoptosis and tumor immunity fields.
Animals ; Apoptosis ; drug effects ; Cytoprotection ; drug effects ; Drug Delivery Systems ; economics ; methods ; trends ; Drug Screening Assays, Antitumor ; HSP70 Heat-Shock Proteins ; antagonists & inhibitors ; metabolism ; HSP90 Heat-Shock Proteins ; antagonists & inhibitors ; metabolism ; Heat-Shock Proteins ; antagonists & inhibitors ; metabolism ; Humans ; Molecular Chaperones ; Pharmaceutical Preparations ; administration & dosage ; chemical synthesis

alphaB-crystallin is the structural protein of vertebrate lens, which is widely expressed in non-lens tissue. As one of the heat shock protein family members, alphaB-crystallin possesses biological properties of molecular chaperones and anti-apoptotic effects. Multi-factor injuries, such as retinopathy, inflammation and nervous system diseases, have a closely relationship with alphaB-crystallin. This paper reviews the research progress of the expression and mechanism of alphaB-crystallin in retina and extraocular tissues and organs.
Crystallins ; Gene Expression Regulation, Developmental ; Heat-Shock Proteins/metabolism* ; Humans ; Lens, Crystalline ; Retina ; alpha-Crystallin B Chain/metabolism*

This study describes the expression of heat shock protein70 (HSP70) and alpha-basic-crystallin (alpha-BC) and their association with apoptosis and some related adaptor proteins in the pathogenesis of foot-and-mouth disease virus (FMDV)-induced myocarditis in lambs. HSP70 was generally overexpressed in the myocardial tissues and inflammatory cells of FMDV-induced myocarditis with differential accumulation and localization in same hearts when compared to non-foot-and-mouth disease control hearts. alpha-BC immunolabeling showed coarse aggregations in the Z line of the cardiomyocytes in FMDV-infected hearts in contrast to control hearts. Overall, the results of this study show that the anti-apoptotic proteins, HSP70 and alpha-BC, were overexpressed with increased apoptosis in FMDV-infected heart tissues. Both proteins failed to protect the cardiomyocytes from apoptosis as defense mechanisms to the FMDV during the infection, suggesting that the virus is able to increase apoptosis via both downregulation and/or upregulation of these anti-apoptotic proteins.
Animals ; Apoptosis Regulatory Proteins/metabolism ; Foot-and-Mouth Disease/*complications/*virology ; Foot-and-Mouth Disease Virus/*classification ; Gene Expression ; HSP70 Heat-Shock Proteins/*metabolism ; Myocarditis/complications/pathology/*veterinary/virology ; Myocardium/pathology ; Sheep ; Sheep Diseases/*virology ; Turkey ; alpha-Crystallin B Chain/*metabolism

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