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

The expression levels of heat shock protein 70 (HSP70) from peripheral lymphocytes of the patients with allergic rhinitis (AR) and the clinical implication were investigated. In the morning, 3 ml of fasting venous blood was taken out. The lymphocytes were isolated by using Ficoll-Hypaque and the expression of HSP70 in the lymphocytes was detected by using Western blot. In the AR patients the HSP70 level (41.49 +/- 15.77 integrated optical density, IOD) were significantly higher than that in the control group (23.89 +/- 10.13 IOD, P < 0.05). Western blot demonstrated that HSP70 bands in AR patients were more intensive than those in the control group. It was concluded that the elevated HSP70 level in peripheral lymphocytes of the AR patients might contribute to the development of AR.
Gene Expression Regulation ; HSP70 Heat-Shock Proteins/*biosynthesis ; HSP70 Heat-Shock Proteins/blood ; HSP70 Heat-Shock Proteins/genetics ; Lymphocytes/*metabolism ; Rhinitis, Allergic, Seasonal/*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

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

OBJECTIVES: Contemporary understanding of schizophrenia has evolved over the last century, yet its pathogenesis is not clear. Environmental stresses in early gestational period, which in turn, can cause neurodevelopmental abnormalities, is one possible etiologic factors in the development of schizophrenia. Heat shock protein 70(HSP70), which is thought to be a protective factor against environmental stresses in a cell, might be involved in the development of schizophrenia. Abnormal immunoreactivity to HSP70 has been identified in patients with schizophrenia. Therefore, genes for HSP70 might be candidates that affect susceptibility to schizophrenia. Three genes encoding HSP70 such as HSP70-1, HSP70-hom and HSP70-2 have been identified in the MHC class III region and they have been known to have genetic polymorphisms. We examined the association of schizophrenia and polymorphisms of HSP70-1, HSP70-hom and HSP70-2 genes in this study. METHODS: We investigated 161 patients with schizophrenia and 165 controls. DNA analysis with polymerase chain reaction(PCR) followed by enzyme restriction was used for the allelic typing of each polymorphism of HSP70-1, HSP70-hom and HSP70-2. The significances of genetic association of the polymorphisms with the disease and with clinical variables were estimated by chi-square test and analysis of variances. RESULTS: 1) There were no significant differences in allelic or genotype frequencies of HSP70-1 and HSP70-hom between the group of patients with schizophrenia and controls. 2) There was a tendency of difference in genotype frequency of HSP70-2, and a significant difference in allelic frequency of HSP70-2 between the group of patients with schizophrenia and controls. 3) There were no significant differences in terms of severity of symptoms and age at onset among the three HSP70 genotypes in the group of patients with schizophrenia. CONCLUSION: These results suggest that polymorphism of HSP70-2 might be related to the pathogenesis of schizophrenia.
DNA ; Genotype ; Heat-Shock Proteins* ; Hot Temperature* ; HSP70 Heat-Shock Proteins* ; Humans ; Polymorphism, Genetic ; Schizophrenia*

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

No abstract available.
Animals ; Diuresis* ; Heat-Shock Proteins ; HSP70 Heat-Shock Proteins* ; Rats* ; Urinary Bladder*

Heat shock proteins (HSPs) widely exist in all organisms, the structures of which are usually extraordinarily conservative. They are also well-known stress proteins that are involved in response to physical, chemical and biological stresses. HSP70 is an important member of the HSPs family. In order to study the roles of amphibians HSP70 during infection, the cDNA sequence of Rana amurensis hsp70 family genes were cloned by homologous cloning method. The sequence characteristics, three-dimensional structure and genetic relationship of Ra-hsp70s were analyzed by bioinformatics methods. The expression profiles under bacterial infection were also analyzed by real-time quantitative PCR (qRT-PCR). Expression and localization of HSP70 protein were tested by immunohistochemical techniques. The results showed that three conservative tag sequences of HSP70 family, HSPA5, HSPA8 and HSPA13, were found in HSP70. Phylogenetic tree analysis indicated four members are distributed in four different branches, and members with the same subcellular localization motif are distributed in the same branch. The relative expression levels of the mRNA of four members were all significantly upregulated (P < 0.01) upon infection, but the time for up-regulating the expression levels were diverse in different tissues. The immunohistochemical analysis showed that HSP70 was expressed to different degrees in the cytoplasm of liver, kidney, skin and stomach tissue. The four members of Ra-hsp70 family have ability to respond bacterial infection to varying degrees. Therefore, it was proposed that they are involved in biological processes against pathogen and play different biological functions. The study provides a theoretical basis for functional studies of HSP70 gene in amphibians.
Heat-Shock Proteins/genetics* ; Phylogeny ; Amino Acid Sequence ; HSP70 Heat-Shock Proteins/metabolism* ; Stress, Physiological