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

PURPOSE: Heat shock protein 27 (HSP27) is induced by heat shock and other pathophysiologic stresses. We examined the relationship between HSP27 expression and Gleason score and pathologic stage of prostate cancer. MATERIALS AND METHODS: Fifty-three men were treated by radical prostatectomy for prostate cancer diagnosed from May 2004 to April 2007. Prostate tissues (n=53) were obtained from radical prostatectomy specimens of prostate cancer. The overall percentage of cancer cells showing staining (0% to 100%) was indicated by visual scoring. Specimens were graded from +1 to +3 intensity representing the range of staining area, for which below 5% is +1 grade, 5-50% is +2 grade, over 50% is +3 grade and focal reaction is +0.5 grade. RESULTS: An HSP27-positive reaction was seen in 2 of 11 cases (18.2%) with a Gleason score of 4-6, 11 of 19 cases (57.9%) with a Gleason score 7, 6 of 10 cases (60.0%) with a Gleason score 8, 12 of 13 cases (92.3%) with a Gleason score of 9 (p=0.001); the mean HSP27 reaction scores were 0.27, 0.86, 0.83, and 1.54 respectively (p=0.006). An HSP27-positive reaction was seen in 17 of 37 cases (46.0%) with pathologic stage T2, 10 of 12 cases (83.3%) with pathologic stage T3, and 4 of 4 cases (100%) with pathologic stage T4 (p=0.0032); the mean HSP27 reaction scores were 0.64, 1.17, and 2, respectively (p=0.007). HSP27 expression was not statistically significant according to age. CONCLUSIONS: There is correlation between HSP27 expression and Gleason score, pathologic stage of prostate cancer.
Heat-Shock Proteins ; Hot Temperature ; HSP27 Heat-Shock Proteins ; Humans ; Male ; Neoplasm Grading ; Prostate ; Prostatectomy ; Prostatic Neoplasms ; Shock

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

heat shock response of mammalian cells. The heat shock response is a coordinated biochemical response that helps to protect cells from stresses of various forms. Several protective proteins, termed heat shock proteins (hsp) are produced as part of this response. To begin to understand the role of the stress response of osteoblasts during surgical manipulation of bone, the heat shock protein response was evaluated in osteoblastic cells.MATERIALS AND METHODS: With primary cell culture studies and ROS 17/2.8 osteoblastic cells transfected with hsp27 encoding vectors culture studies, the thermal stress response of mammalian osteoblastic cells was evaluated by immunohistochemistry and western blot analysis.RESULTS: Immunocytochemistry indicated that hsp27 was present in unstressed osteoblastic cells, but not fibroblastic cells. Primarily cultured osteoblasts and fibroblasts expressed the major hsp in response to thermal stress, however, the small Mr hsp, hsp27 was shown to be a constitutive product only in osteoblasts. Creation of stable transformed osteoblastic cells expressing abundant hsp27 protein was used to demonstrate that hsp27 confers stress resistance to osteoblastic cells.CONCLUSIONS: The demonstrable presence and function of hsp27 in cultured bones and cells implicates this protein as a determinant of osteoblastic cell fate in vivo.]]>
Blotting, Western ; Fibroblasts ; Heat-Shock Proteins ; Heat-Shock Response ; HSP27 Heat-Shock Proteins ; Immunohistochemistry ; Osseointegration ; Osteoblasts ; Primary Cell Culture ; Proteins ; Staphylococcal Protein A

OBJECTIVETo evaluate the mRNA expression of heat shock protein 27 (HSP27) in different prostate cancer cell lines including RWPE-1, LNCaP, PC-3, and TSU-Pr1 and to further analyze the effect of quercetin on PC-3 cell lines.

METHODSThe in vitro cultured human prostate cancer cell lines RWPE-1, LNCaP, PC-3, and TSU-Pr1 were randomly divided into four groups: control group; negative control group (treated with dimethyl sulfoxide), high-dose group (treated with 150 Μl 0.6 mg/ml quercetin), and low-dose group (treated with 150 Μl 0.3 mg/ml quercetin). The mRNA expression of HSP27 was detected by reverse transcription polymerase chain reaction (RT-PCR) and immunofluorescence staining.

RESULTSRT-PCR and immunofluorescence staining showed that HSP27 expression were highly dependent on the cell types and increased in an order of RWPE-1, LNCaP, PC-3, and TSU-Pr1 after quercetin treatment. The HSP27 mRNA expression levels were 128%, 110%, 50%, and 60% in control group, negative control group, high-dose group, and low-dose group. Obviously, it was significantly lower in the high-dose group and low-dose group than in the control group (both P<0.05).

CONCLUSIONSHSP27 expression level is associated with the the degree of prostate cancer. Quercetin may inhibit HSP27 expression in PC-3 cell.

Cell Line, Tumor ; HSP27 Heat-Shock Proteins ; metabolism ; Humans ; Male ; Prostatic Neoplasms ; metabolism ; pathology ; Quercetin ; pharmacology

OBJECTIVEThis research aimed to observe the expression of heat shock protein 27 (HSP27) in human gingival fibroblasts (HGFs) cell injury induced by different concentrations of cigarette smoke extract (CSE).

METHODSThe third to eighth generations of cultured HGFs were treated with serially diluted CSE of different concentrations (0, 2.5%, 5.0%, 12.5%, 25.0%, 50.0%). Wound-healing assay was performed to determine the migration of HGFs, and Western blot was used to determine the expression of HSP27.

RESULTSThe migration capability of HGFs weakened with the increase of CSE concentration. HSP27 expression was negative in normal HGFs but positive in CSE-intervened HGFs in a concentration-dependent manner.

CONCLUSIONHSP27 concentration increased in the CSE-induced injury of HGFs. This finding suggests that HSP27 plays an important role in CSE-induced epithelial injury.

Cells, Cultured ; Fibroblasts ; Gingiva ; HSP27 Heat-Shock Proteins ; Humans ; Smoke ; Tobacco ; Wound Healing

Objective: To study the effect of anti-fibrotic tetrapeptide N-acetyl-seryl-aspartyl-lysyl-proline (Ac-SDKP) on phosphorylated heat shock protein 27 (P-HSP27) and zinc finger family transcriptional repressor 1 (SNAI1) expression to explore the anti-silicosis fibrosis effect of Ac-SDKP. Methods: In December 2014, the rat silicosis animal model was prepared by one-time bronchial infusion of silicon dioxide (SiO(2)) dust. 80 SPF healthy adult Wistar rats were selected, and the rats were divided into 8 groups according to the random number table method, 10 in each group. Model control group for 4 weeks (feeding for 4 weeks) , model control group for 8 weeks (feeding for 8 weeks) : bronchial perfusion with normal saline 1.0 ml per animal. Silicosis model group for 4 weeks (feeding for 4 weeks) and silicosis model group for 8 weeks (feeding for 8 weeks) : bronchial perfusion of 50 mg/ml SiO(2) suspension 1.0 ml per animal. Ac-SDKP administration group for 4 weeks (feeding for 4 weeks) , Ac-SDKP administration group for 8 weeks (feeding for 8 weeks) : Ac-SDKP 800 μg·kg(-1)·d(-1) was administered by intraperitoneal pump. Ac-SDKP preventive treatment group: 48 h after Ac-SDKP 800 μg·kg(-1)·d(-1) administration, bronchial perfusion of SiO(2) suspension 1.0 ml per animal, raised for 8 weeks. Ac-SDKP anti-fibrosis treatment group: after bronchial perfusion of 1.0 ml of SiO(2) suspension for 4 weeks, Ac-SDKP 800 μg·kg(-1)·d(-1) was administered for 4 weeks. Western blotting was used to detect the expression of P-HSP27, SNAI1, α-smooth muscle actin (α-SMA) , and collage typeⅠ and Ⅲ in each group. The expression of P-HSP27 and SNAI1 was detected by immunohistochemistry, and the co-localized expression of P-HSP27 and α-SMA was detected by laser confocal microscopy. Results: Compared with the model control group, the expressions of P-HSP27, SNAI1, α-SMA, and collage typeⅠ and Ⅲ in the silicosis fibrosis area of the rats in the silicosis model group were enhanced, and the differences were statistically significant (P<0.05) . After Ac-SDKP intervention, compared with silicosis model group for 8 weeks, the expressions of P-HSP27, SNAI1 α-SMA, and collage typeⅠ and Ⅲ in the Ac-SDKP preventive and anti-fibrosis treatment groups were significantly decreased, and the differences were statistically significant (P<0.05) . However, the expressions of P-HSP27 SNAI1, and collage typeⅠ and Ⅲ between the Ac-SDKP administration group and the model control group did not change significantly, and the differences were not statistically significant (P>0.05) . Laser confocal results showed that the positive cells expressing P-HSP27 and α-SMA in the lung tissue of the silicosis model group were more than those in the model control group. Compared with the silicosis model group, the Ac-SDKP prevention and anti-fibrosis treatment groups expressing the positive cells of P-HSP27 and α-SMA decreased. Compared with the model control group for 8 weeks, there were some double-positive cells expressing P-HSP27 and α-SMA in the nodules of the silicosis model group for 8 weeks. Conclusion: Ac-SDKP may play an anti-silicic fibrosis effect by regulating the P-HSP27/SNAI1 pathway.
Animals ; HSP27 Heat-Shock Proteins ; Oligopeptides ; Rats ; Rats, Wistar ; Silicon Dioxide ; Silicosis/metabolism*

BACKGROUND: Heat shock protein 27 (HSP27) is induced by heat shock and other pathophysiologic stresses, including neoplastic transformation. We examined the relationship between the HSP27 expression and the clinical and histologic parameters to elucidate the biologic and prognostic significance of HSP27 in renal cell carcinomas (RCCs). Its regulation of apoptosis in RCC development was also observed. METHODS: We performed immunohistochemical studies for HSP27, caspase 3 and TUNEL on paraffin-embedded tissue microarray specimens from 48 RCCs. RESULTS: There was a tendency to higher expression of HSP27 in the RCC than in normal renal tubular cells. Of the 48 RCCs, the HSP27 expression was positive in 38 cases. An inverse relationship was found between the Fuhrman nuclear grade and HSP27 expression, but this was without statistical significance (r=-0.218, p=0.093). No relationship between the HSP27 expression and the other parameters was observed. Also, no statistically significant difference was observed between apoptosis and the HSP27 expression more (p=0.951). CONCLUSIONS: Although HSP27 expression was increased in RCC than in normal renal tubular cell the HSP27 expression may not be a powerful and statistically significant prognostic indicator in patients with RCC.
Apoptosis ; Carcinoma, Renal Cell* ; Caspase 3 ; Heat-Shock Proteins* ; Hot Temperature* ; HSP27 Heat-Shock Proteins* ; Humans ; In Situ Nick-End Labeling ; Shock

PURPOSE: This study was designed to examine whether human articular chondrocytes express heat shock protein 27 (hsp27) and to evaluate the relation between hsp27 and the apoptosis of chondrocytes. MATERIALS AND METHODS: Knee joint articular cartilage was obtained from femoral condyle in osteoarthritis patients who underwent joint replacement surgery. Chondrocytes were isolated, cultured and then exposed to heat shock (42degrees C) for 1 hour to induce the expression of hsp27. 20 mM of sodium nitroprusside (SNP) was then added for 12 hours to evaluate the ability of hsp27 to prevent SNPinduced chondrocyte apoptosis. The expression of hsp27 was verified by Western blot and the rate of apoptosis was determined by flow cytometric analysis. RESULTS: Heat shock resulted in the increased expression of hsp27 in chondrocytes. Heat-shocked groups had smaller numbers of apoptotic cells than control groups when both were exposed to apoptosis inducing stimuli. CONCLUSION: We conclude that hsp27 was expressed in human articular chondrocytes by heat shock and that the expression of hsp27 in chondrocytes increases their resistance to apoptosis. This result presents clues, which suggest that the induction of hsp27 could be a desirable future therapeutic strategy in human osteoarthritis
Apoptosis* ; Blotting, Western ; Cartilage, Articular ; Chondrocytes* ; Heat-Shock Proteins* ; Hot Temperature* ; HSP27 Heat-Shock Proteins* ; Humans ; Joints ; Knee Joint ; Nitroprusside ; Osteoarthritis ; Shock

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*