This article reviews the advances in the research of the structural characteristics and the activating process of heat shock factor 1 (HSF-1), the factors that influence the expression of HSF-1, and the relationship between HSF-1 and the expression levels of NF-κB and heat shock protein (HSP). The expression of HSF-1 could be regulated in several stages in the course of interconversion between its active and inactive status. Unusual expression of HSF-1 mediated by NF-κB can lead to the quantitative and functional change of HSP. The quantitative and functional variation of HSP caused by regulation of HSF-1 could influence the normal synthesis and the pathological changes induced by excessive synthesis of protective proteins in cells under stress. We expect that further research would help elucidate novel pathways about the genesis and evolution mechanism of keloid, and it may finally help to find a novel strategy in the treatment of keloid.
Animals ; DNA-Binding Proteins ; metabolism ; Heat Shock Transcription Factors ; Heat-Shock Proteins ; metabolism ; Humans ; Transcription Factors ; metabolism

Crystallography, X-Ray ; DNA ; chemistry ; Heat Shock Transcription Factors ; chemistry ; Heat-Shock Proteins ; chemistry ; Humans ; Molecular Dynamics Simulation ; Transcription Factors ; chemistry

OBJECTIVE: To observe the effect of heat shock factor 1 (HSF1) on heat stress-induced apoptosis in Raw264.7 macrophages. METHODS: Raw264.7 cells transfected with pcDNA3.1 and pcDNA3.1-HSF1 were exposed to heat stress (42.5 degrees C +/- 0.5 degrees C) for 1 h and recovered at 37 degrees C for 6, 9, 12, and 24 h respectively. Flow cytometry (FCM), Hoechst 33258 staining and DNA ladder assays were performed to assess the apoptosis. RESULTS: After heat stress, FCM showed that apoptotic cells were increased significantly and reached the peak at 9 h in Raw 264.7 cells transfected with pcDNA3.1, and were characterized with classical morphologic changes including apoptotic body and nuclear condensation. Agarose gel electrophoresis showed that "DNA ladder" could be observed clearly at 6, 9, and 12 h after the heat stress. But the overexpression of HSF1 could reduce the number of apoptotic cells and inhibit DNA fragmentation. CONCLUSION HSF1 can inhibit heat stress-induced apoptosis in Raw264.7 macrophages.
Animals ; Apoptosis ; drug effects ; Cells, Cultured ; DNA-Binding Proteins ; pharmacology ; Heat Shock Transcription Factors ; Heat-Shock Response ; Macrophages ; cytology ; Mice ; Rats ; Transcription Factors ; pharmacology ; Transfection

With the constant change of global climate, plants are often affected by multiple abiotic stresses such as heat stress, drought stress, cold stress and saline-alkali stress. Heat shock transcription factors (HSFs) are a class of transcription factors widely existing in plants to respond to a variety of abiotic stresses. In this article, we review and summarize the structure, signal regulation mechanism of HSFs and some research in plants like Arabidopsis thaliana, tomato, rice and soybean, to provide reference for further elucidating the role of HSFs in the stress regulation network.
Arabidopsis/metabolism* ; Droughts ; Gene Expression Regulation, Plant ; Heat Shock Transcription Factors/genetics* ; Plant Proteins/genetics* ; Stress, Physiological ; Transcription Factors/metabolism*

OBJECTIVETo study how the combined effects of various differentiation inducers and heat stress on the expression of JWA protein in K562 cell, the relationship between JWA and Hsp70 expression, and the signal regulation mechanism possibly involved.

METHODSThe experimental model was established in K562 cells. Various directional differentiation inducers (TPA, Ara-C, hemin, adriamycin, ATRA and As(2)O(3)) were used alone or combined with heat shock treatment (42 degrees C, 2 h). Western blot was used for detecting expressions of JWA, Hsp70, heat stress factor 1 (HSF1) and HSF2.

RESULTS(1) The expressions of both JWA protein and Hsp70 were significantly up-regulated after K562 cells treated by TPA (100, 200 ng/ml) or adriamycin (4 x 10(-8) mol/L) 48 h, and followed by heat shock (42 degrees C, 2 h). However, the opposite effects were observed when the cells treated by hemin (3 x 10(-5) mol/L, 48 h), Ara-C (80 ng/ml, 48 h) and As(2)O(3) (1 x 10(-6) mol/L, 48 h) followed by 2 h heat shock. No obvious changes were found when the cells treated by ATRA (1 x 10(-6) mol/L, 48 h) alone or followed by heat shock. (2) Both the heat shock transcriptional factors HSF1 and HSF2 did not show any significant changes when K562 cells were treated with various differentiation inducers and followed by heat stress.

CONCLUSIONJWA not only takes part in the regulation of K562 cellular differentiation, but also of heat stress, it might be the co-target gene of several differentiation inducers and heat stress. The expression of Hsp70 seems not mediated by both HSF1 and HSF2 in K562 cells undergoing directional differentiation or heat stress treatment. JWA is likely to be a new signal molecule similar to Hsp70 signal pathways. The results show that JWA takes part in the mechanism of K562 cell response to heat stress.

Blotting, Western ; DNA-Binding Proteins ; analysis ; Flow Cytometry ; HSP70 Heat-Shock Proteins ; analysis ; Heat Shock Transcription Factors ; Heat-Shock Proteins ; analysis ; Hot Temperature ; Humans ; Intracellular Signaling Peptides and Proteins ; K562 Cells ; Transcription Factors ; analysis

Heat shock protein 90 (HSP90) is involved in conformational and structural maturation of signalling molecules and transcription factors in immune reaction. HSP90 inhibitors induce immune modulation via anti-inflammatory effect, regulating humoral and cellular immune responses. Therefore, HSP90 inhibitors potentially useful target for the autoimmune disease and chronic inflammatory diseases.
Autoimmune Diseases ; Heat-Shock Proteins* ; Immunity, Cellular ; Interleukin-17 ; Transcription Factors

Heat stress transcription factors (Hsf) family is one of the most important transcription factor families in plants, and plays an important role in the growth and development of plants when encountering abiotic stresses such as heat, drought, and heavy metals. In this study, 20 SpbHsf genes were identified from the full-length transcriptome database of Setcreasea purpurea, and the structure and function of the Hsf gene family were analyzed using bioinformatics tools and qRT-PCR. The results showed that all SpbHsf proteins were hydrophilic. There were 12 SpbHsf proteins located in the nucleus, and the content of α-helix and random coil in the secondary structure of all SpbHsf proteins was high. The SpbHsf genes are divided into three subfamilies, each of which contains unique conserved motifs. All SpbHsf proteins contain DBD and HR-A/B domains. Phylogenetic analysis showed that OsHsf in Oryza sativa protein had the highest homology with SpbHsf protein. All the 20 SpbHsf genes were expressed in the root tissues of S. purpurea. Among them, 8 were significantly up-regulated while 8 were significantly down-regulated under Cu²⁺ stress. This study may help better understand the function and expression pattern of the S. purpurea Hsf gene family.
Droughts ; Gene Expression Regulation, Plant ; Heat Shock Transcription Factors/metabolism* ; Humans ; Phylogeny ; Plant Proteins/metabolism*

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

OBJECTIVE: To observe the effect of Krüppel-like factor 4 (KLF4) overexpression on heat stress-induced apoptosis of Raw264.7 macrophages. METHODS: The fragment containing full length mouse KLF4 cDNA coding sequence was inserted into the pcDNA3.1 vector and Raw264.7 macrophages were transfected with pcDNA3.1-KLF4 plasmids using lipofectamine.The expression of KLF4 was examined by Western blot in the Raw264.7 macrophages stably transfected with pcDNA3.1- KLF4 plasmids. Raw264.7 cells transfected with pcDNA3.1 and pcDNA3.1-KLF4 were exposed to heat stress (42 degrees C) for 1h and recovered at 37 degrees C for 12h. Flow cytometry, Hoechest 33258 staining assay, and DNA ladder assays were performed to assess the apoptosis. RESULTS: The KLF4 overexpressed Raw264.7 macrophages were established. After the heat stress, flow cytometry showed that apoptotic cells increased significantly in KLF4 overexpressed cells compared with the vector control; Hoechest 33258 staining was characterized with classical changes including apoptotic body, and nuclear condensation. Agarose gel electrophoresis showed that "DNA ladder" could be observed clearly. CONCLUSION KLF4 overexpression can increase heat stress-induced apoptosis of Raw264.7 macrophages.
Animals ; Apoptosis ; genetics ; Cell Line ; Genetic Vectors ; Heat-Shock Response ; Kruppel-Like Transcription Factors ; genetics ; Macrophages ; cytology ; Mice ; Plasmids ; Transfection

AIMTry to clarify the effects of HSF1 gene on the constitutively expressed alphaBC.

METHODSTo investigate the levels of constitutively expressed alphaB-Crystallin (alphaBC) in hsf1 knockout (hsf1 -/-) and hsf1 wild type (hsf1 +/+) mice myocardium by Western blot and immunohistochemistry.

RESULTSThe alphaBC levels in hsf1 -/- and hsf1 +/+ were 68.42% +/- 4.16%, 100% +/- 7.58%, respectively (P < 0.05, cytosolic fraction), and 20.53% +/- 1.01%, 37.55% +/- 1.91%, respectively (P < 0.05, pellet fraction). The alphaBC signals decreased significantly in hsf1 -/- myocardium compared with hsf1 +/+ myocardium stained with fluorescence immunohistochemistry.

CONCLUSIONhsf1 is the important, but not the only factor, which mediates the constitutively expressed alphaBC.

Animals ; DNA-Binding Proteins ; genetics ; Female ; Genotype ; Heat Shock Transcription Factors ; Male ; Mice ; Mice, Knockout ; Myocardium ; metabolism ; Transcription Factors ; genetics ; alpha-Crystallin B Chain ; genetics ; metabolism