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

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*

OBJECTIVE: To analyze HSP70/HSP27 protein expression in the nasopharyngeal carcinoma (NPC) primary tissues and the residual lesion, and to explore its predictive value. METHODS: Immunohistochemical experiment was performed to detect the expression of HSP70 and HSP27 in 58 NPC primary tissues: 28 were in the experimental group with the local residual lesion and 30 in the control group without recurring and metastasis within 5 years by conventional radiotherapy. RESULTS: The positive expression of HSP70 and HSP27 in the experimental group was 92.9%(26/28) and 53.6%(15/28), while that in the control group was 53.3%(16/30) and 53.3%(16/30),respectively. There was significant difference in the 2 groups. The common positive expression of HSP70 and HSP27 between the 2 groups had significant difference, 50.0% (14/28) in the experimental group and 16.7% (5/30) in the control group, respectively. There was no significant difference in the negative ratio of HSP70 and HSP27 common expression between the 2 groups, 3.6% (1/28) in the experimental group and 10.0% (3/30) in the control group, respectively. CONCLUSION HSP70 may have an important role in the radioresistance of NPC, and may predict the residual lesion after radiotherapy.
Adult ; Aged ; Carcinoma, Squamous Cell ; metabolism ; radiotherapy ; Female ; HSP27 Heat-Shock Proteins ; metabolism ; HSP70 Heat-Shock Proteins ; metabolism ; Humans ; Male ; Middle Aged ; Nasopharyngeal Neoplasms ; metabolism ; radiotherapy ; Young Adult

OBJECTIVEA proteomics approach was applied for finding multi-drug resistance (MDR) related proteins in hepatic cancer cell lines.

METHODSTwo-dimensional electrophoresis (2-DE) was used to separate the total proteins of vincristine-resistant hepatic cancer cell line HepG2/VCR and its counterpart HepG2. The differential expression proteins between the two cell lines were identified by both MALDI-TOF-MS and ESI-Q-TOF-MS. Heat-shock protein 27 (HSP27), one of the differential expression proteins in the development of MDR of HepG2/VCR, was analyzed by HSP27 antisense oligonucleotides (ASOs).

RESULTSAs a high expression protein in HepG2/VCR, HSP27 was identified, and the suppression of HSP27 expression by HSP27 ASO enhanced the vincristine chemosensitivity of HepG2/VCR (P less than 0.05).

CONCLUSIONHSP27 is linked to MDR in human hepatic cancer cell line HepG2/VCR.

Drug Resistance, Multiple ; Drug Resistance, Neoplasm ; HSP27 Heat-Shock Proteins ; metabolism ; Hep G2 Cells ; Humans ; Liver Neoplasms ; metabolism

OBJECTIVES: The pathogenesis of androgenetic alopecia (AGA) is related to the level of androgen and its metabolic pathways. The binding of androgen and androgen receptor (AR) depends on the assistance of heat shock protein 27 (HSP27). HSP27 combined with microRNAs (miR)-1 can regulate AR levels. However, it is not clear whether HSP27 and miR-1 jointly participate in the pathogenesis of AGA. This study aims to investigate the role of AR up-regulation in the pathogenesis of AGA and underlying mechanisms. METHODS: A total of 46 male AGA patients (AGA group), who admitted to the First Affiliated Hospital of Guangzhou Medical University from September 2019 to February 2020, and 52 healthy controls admitted to the same period were enrolled in this study. Serum levels of dihydrotestosterone (DHT) and HSP27 in patients and healthy controls were measured by ELISA. Western blotting was used to detect the protein expression of HSP27 and AR in scalp tissues of patients and the healthy controls. The levels of HSP27, AR, and miR-1 were analyzed using real-time PCR. Human dermal papilla cells were transfected with HSP27 siRNA to inhibit the expression of HSP27. MiR-1 and miR-1 inhibitors were transfected simultaneously or separately into cells and then the changes in AR protein expression were detected. RESULTS: The levels of DHT and HSP27 in the AGA group were (361.4±187.7) pg/mL and (89.4±21.8) ng/mL, respectively, which were higher than those in the control group [(281.8±176.6) pg/mL and (41.2±13.7) ng/mL, both P<0.05]. However, there was no significant difference in serum HSP27 and AR levels among AGA patients with different degrees of hair loss (P>0.05). Correlation analysis showed that there was a positive correlation between HSP27 level and DHT level in the AGA patients (P<0.05). The level of HSP27 mRNA in scalp tissue was negatively correlated with that of miR-1 mRNA (P<0.05). Compared with the control group, the levels of HSP27 protein, AR protein, HSP27 mRNA, and AR mRNA in scalp tissues of AGA group were significantly increased (P<0.05). The up-regulation of HSP27 in scalp tissues of AGA patients was closely related to the increased levels of AR. However, the level of miR-1 in scalp tissues of AGA patients was significantly down-regulated, contrary to the expression of AR (P<0.05). Further in cell studies showed that inhibition of HSP27 or miR-1 expression in human dermal papilla cells could inhibit the expression of AR, and inhibition of both HSP27 and miR-1 expression was found to have an accumulative effect on AR, with statistically significant differences (all P<0.05). CONCLUSIONS HSP27 could combine with miR-1 to up-regulate AR levels, which is closely related to the development of AGA.
Alopecia/pathology* ; HSP27 Heat-Shock Proteins/metabolism* ; Humans ; Male ; MicroRNAs/genetics* ; RNA, Messenger ; Receptors, Androgen/metabolism* ; Up-Regulation

Adenocarcinoma ; metabolism ; pathology ; Adenoma ; metabolism ; pathology ; Colonic Neoplasms ; metabolism ; pathology ; Cytoplasm ; metabolism ; Female ; HSP27 Heat-Shock Proteins ; Heat-Shock Proteins ; analysis ; Humans ; Intestinal Mucosa ; metabolism ; pathology ; Male ; Neoplasm Proteins ; analysis ; Proteome ; analysis ; Proteomics ; methods ; Rectal Neoplasms ; metabolism ; pathology

OBJECTIVETo 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).

METHODSThe 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.

RESULTSThe 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).

CONCLUSIONThe 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

OBJECTIVETo examine the differences in the expression of HSP27 and c-kit between benign prostatic hyperplasia (BPH) and prostatic cancer (PCa) tissues and to analyse the relationship between their expression and BPH and PCa, especially the relationship with the occurrence, development, prognosis and treatment of PCa.

METHODSAn immunohistochemical staining (SP method) for HSP27 and c-kit was undertaken on 40 BPH and 40 PCa tissues samples.

RESULTSConsistent patterns of cytoplasmic staining for HSP27 were seen in all sections of tissue from BPH. The glandular epithelium stained very strongly positively and the stroma stained positively. The staining for HSP27 in PCa tissues was located in the cytoplasm of glandular epithelia, but the expression of HSP27 in PCa was higher than BPH (P < 0.05). The staining for c-kit in BPH tissues was located in the cytoplasm of smooth muscle cells, and in PCa tissues was located in epithelial cells. The expression of c-kit in PCa tissues was lower than BPH (P < 0.05). The expression level of both HSP27 and c-kit were decreased with the development of grade of PCa (P < 0.05); HSP27 was increased with the development of clinical stage of PCa (P < 0.05 ); c-kit was decreased with the development of clinical stage of PCa (P < 0.05).

CONCLUSIONThe expression level of HSP27 and c-kit was highly correlated with the process of the development from BPH to PCa, and also correlated with tumor grades and stages. The expression of HSP27 and c-kit may be used as an important pathological index and may be helpful for the treatment of PCa.

Aged ; Aged, 80 and over ; HSP27 Heat-Shock Proteins ; Heat-Shock Proteins ; biosynthesis ; Humans ; Immunohistochemistry ; Male ; Middle Aged ; Neoplasm Proteins ; biosynthesis ; Prostatic Hyperplasia ; metabolism ; pathology ; Prostatic Neoplasms ; metabolism ; pathology ; Proto-Oncogene Proteins c-kit ; biosynthesis

BACKGROUNDIncreased reactive oxygen species (ROS) formation, which in turn promotes cardiomyocytes apoptosis, is associated with the pathogenesis and progression of various cardiac diseases such as ischemia and heart failure. Recent studies have shown that over expression of heat shock protein 27 (Hsp27) confers resistance to cardiac ischemia/reperfusion injury. However, not much is known about the regulation of myocyte survival by Hsp27.

METHODSThe rat cardiac cell line H9c2, with a stable overexpression of Hsp27, was established, with empty vector transfected H9c2 cells as controls. Following the cells challenged by Hydrogen Peroxide (H2O2), lactate dehydrogenase (LDH) release, apoptosis, intracellular ROS, cell morphology, mitochondrial transmembrane potential and the activation of serine/threonine kinase Akt were determined.

RESULTSAlong with marked suppression of H2O2-induced injury by Hsp27 overexpression in H9c2 cells, ROS generation and the loss of mitochondrial membrane potential were also significantly depressed. Furthermore, augmented Akt activation was observed in Hsp27 overexpressed H9c2 cells following H2O2 exposure.

CONCLUSIONSHsp27 inhibits oxidative stress-induced H9c2 damage and inhibition of ROS generation and the augmentation of Akt activation may be involved in the protective signaling.

Animals ; Apoptosis ; Cell Line ; HSP27 Heat-Shock Proteins ; Heat-Shock Proteins ; physiology ; Humans ; Hydrogen Peroxide ; toxicity ; Myocytes, Cardiac ; pathology ; Neoplasm Proteins ; physiology ; Oxidative Stress ; Proto-Oncogene Proteins c-akt ; metabolism ; Rats ; Reactive Oxygen Species ; metabolism

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