No abstract available.
Heat-Shock Proteins* ; Hot Temperature*

No abstract available.
Heat-Shock Proteins* ; Hot Temperature*

No abstract available.
Heat-Shock Proteins* ; Hot Temperature*

BACKGROUND: When cells or organisms are exposed to environmental stresses, they respond by synthesizing a characteristic group of proteins called heat shock proteins(HSP) or stress proteins. In a variety of HSP, the so-called HSP 70 family is the most prominent, conserved, and best characterized. The HSP 70 family is required for survival of cells during and after thermal stress. OBJECTIVE: The purpose of this study is to investigate if the cultured human melanocytes and rnelanotic malignant melanoma cell lines(SK 30) expressed HSP 70 family unstressed, after heat shock and ultraviolet exposure. METHODS: Protein was isolated from melanocytes and SK 30. Western blotting was done for identification of the HSP 70 family. RESULTS: HSP 70 family expression could be detected in the unstressed cultured human melanocytes and SK 30(malignant melanoma cell lines). HSP 70 family expression inereased in the melanocytes and SK 30 after heat shock. Irradiation of the melanocytes with UVA resulted in a decrease in expression of HSP 70 family after 32, 48 J/cm compared with 4, l6 J/cm. Irradiation of the melanocytes with UVA + B resulted in a dose-dependent increase in expression of HSP 70 family but a decrease in expression of HSP 70 family after 80mJ/cm. Irradiation of SK 30 with UVA resulted in a dose-dependent decrease in expression of the HSP 70 family. CONCLUSION: HSP 70 family expression was detected even unstressed. This high base line HSP 70 family expression may suggest that melanocytes have ability to protect from environmental stresses like keratinocytes.
Blotting, Western ; Heat-Shock Proteins* ; Hot Temperature* ; HSP70 Heat-Shock Proteins* ; Humans ; Keratinocytes ; Melanocytes* ; Melanoma ; Shock

BACKGROUND: When cells or organisms are exposed to environmental stresses, they respond by synthesizing a characteristic group of proteins called heat shock proteins(HSP) or stress proteins. In a variety of HSP, the so-called HSP 70 family is the most prominent, conserved, and best characterized. The HSP 70 family is required for survival of cells during and after thermal stress. OBJECTIVE: The purpose of this study is to investigate if the cultured human melanocytes and rnelanotic malignant melanoma cell lines(SK 30) expressed HSP 70 family unstressed, after heat shock and ultraviolet exposure. METHODS: Protein was isolated from melanocytes and SK 30. Western blotting was done for identification of the HSP 70 family. RESULTS: HSP 70 family expression could be detected in the unstressed cultured human melanocytes and SK 30(malignant melanoma cell lines). HSP 70 family expression inereased in the melanocytes and SK 30 after heat shock. Irradiation of the melanocytes with UVA resulted in a decrease in expression of HSP 70 family after 32, 48 J/cm compared with 4, l6 J/cm. Irradiation of the melanocytes with UVA + B resulted in a dose-dependent increase in expression of HSP 70 family but a decrease in expression of HSP 70 family after 80mJ/cm. Irradiation of SK 30 with UVA resulted in a dose-dependent decrease in expression of the HSP 70 family. CONCLUSION: HSP 70 family expression was detected even unstressed. This high base line HSP 70 family expression may suggest that melanocytes have ability to protect from environmental stresses like keratinocytes.
Blotting, Western ; Heat-Shock Proteins* ; Hot Temperature* ; HSP70 Heat-Shock Proteins* ; Humans ; Keratinocytes ; Melanocytes* ; Melanoma ; Shock

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

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: The present study aimed to determine the intracellular action of the antidepressant, venlafaxine, in C6 glioma cells using heat shock protein 70 (HSP70) immunocytochemistry and HSP70 Western blots; HSP70 is known to be associated with stress and depression. METHODS: The extent of HSP70 expression was measured after rat C6 glioma cells were treated with 1) dexamethasone only, 2) venlafaxine only, 3) simultaneous venlafaxine and dexamethasone, or 4) dexamethasone after venlafaxine pretreatment. Dexamethasone (10 microM, 6 hours) did not affect the level of HSP70 expression relative to control. RESULTS: Short-term (1 hour) venlafaxine treatment significantly increased the level of HSP 70 expression. Simultaneous long-term (72 hours) venlafaxine and dexamethasone treatment significantly reduced the level of HSP70 expression. Dexamethasone treatment administered following long-term (24 and 72 hours) pretreatment with venlafaxine also significantly reduced the level of HSP70 expression. CONCLUSION: Short-term treatment with venlafaxine increases the expression of HSP70, but prolonged treatment with dexamethasone suppresses the venlafaxine-induced expression of HSP70. These findings suggest that HSP70 and dexamethasone play a significant role in the pathophysiology of depression.
Animals ; Cyclohexanols ; Depression ; Dexamethasone ; Glioma ; Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; Immunohistochemistry ; Rats ; Venlafaxine Hydrochloride

BACKGROUND: The present study was designed to investigate the expression of p53, Heat Shock Protein 70 (HSP70), and Topoisomerase (Topo) II alpha in the preneoplastic lesions and carcinomas of the gallbladder (GB) and to assess the correlation between the expression of these proteins and the clinicopathologic parameters by performing immunohistochemistry. METHODS: The immunohistochemical expressions of p53, HSP70 and Topo II alpha were evaluated in 38 gallbladder carcinomas and 3 adenomas. Fifteen CIS(s) and 8 dysplasias that were located adjacent to invasive carcinomas were also studied. RESULTS: A p53 expression was identified in 22 (57.9%) of the 38 GB carcinomas, in 9 (64.3%) of 14 CISs, and in none of the 8 dysplasias and 3 adenomas. A HSP70 expression was found in 11 (29%) of the 38 carcinomas, in 11 (78.6%) of 14 CIS(s), and in 4 (57.2%) of 7 dysplasias. A Topo II alpha expression was present in 36 (94.7%) of the 38 carcinomas, in 13 (92.9%) of 14 CIS(s), in 7 (100%) of 7 dysplasias and in 3 (100%) of 3 adenomas. p53 overexpression was related to the T stage of the primary tumor, while HSP70 and Topo II alpha were not related to any of the clinicopathologic parameters. CONCLUSION: p53 may be involved in GB carcinogenesis and in the progression of cancer. p53 may be also helpful for making the differential diagnosis between dysplasia and CIS. A further large study is needed to better elucidate the roles of HSP70 and Topo II alpha in GB carcinogenesis.
Adenoma ; Carcinogenesis ; Diagnosis, Differential ; Gallbladder* ; Heat-Shock Proteins* ; Hot Temperature* ; HSP70 Heat-Shock Proteins* ; Immunohistochemistry

BACKGROUND: The heat shock proteins (HSPs) are stress-responsive genes present in all species and play a major role in many cellular processes. These proteins are highly conserved molecules whose expression is induced in eukaryotic cells by a variety of environmental stresses. These proteins can also be expressed in virally transformed cells and cancer cells. Especially, HSP70 is found at a higher level in growing cells than in resting cells. Sulphomucin is secreted by immature foveolar cells of stomach and expressed in gastric adenocarcinomas. Also, it is known that the population of sulphomucin-producing cells increases with long-lasting stress. The purpose of this study was to determine HSP70 and sulphomucin expressions in gastric adenocarcinoma and the significance of expressions. METHODS: Thirty-one paraffin-embeded surgical specimens of gastric adenocarcinomas were obtained from April 1992 to March 1995 and were selected for analysis. The expressions of HSP70 and sulphomucin were analyzed by immunohistochemical staining with HSP70 monoclonal antibody and the Spicer (HID) method. RESULTS: The expressions of HSP70 and sulphomucin were positive in 13 (42%) cases and 11 (35%) cases, respectively. The expression of HSP70 correlated with neither clinopathological factors nor sulphomucin expression. There was a significant correlation not only between sulphomucin expression and histologic differentiation (p=0.001) but also between disease-free survival and sulphomucin expression. CONCLUSIONS: Sulphomucin expression in gastric adenocarcinoma may be useful as a prognostic factor of gastric adenocarcinomas.
Adenocarcinoma* ; Disease-Free Survival ; Eukaryotic Cells ; Heat-Shock Proteins* ; Hot Temperature* ; HSP70 Heat-Shock Proteins* ; Stomach