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

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

OBJECTIVETo investigate the expression of Caspase-3 and Hsp70 in rabbits after severe traumatic brain injury (TBI) and to explore the feasibility of its application in estimation of injury time in forensic medicine.

METHODSA rabbit model of heavy TBI was developed by high velocity impact on the parietal bone with an iron stick. Totally 8 healthy adult New Zealand white rabbits were randomly divided into control group (n equal to 2) and injury group (n equal to 6). Four hours after injury, tissue specimens from the parietal lobe, temporal lobe, occipital lobe, cerebellum and brainstem were harvested to detect the expression of Hsp70 and Caspase-3 by immunohistochemistry. Besides, the gray values of cells positive for Hsp70 and Caspase-3 were analyzed with an image analyzer.

RESULTSImmunohistochemistry staining demonstrated a low level of Caspase-3 and Hsp70 expression in normal control group. While in injury group, both the Caspase-3 and Hsp70 expression was significantly elevated (P less than 0.05). Positive cells gathered around the lesion focus. Occipital lobe and cerebellum had fewer positive cells while temporal and brainstem had the fewest.

CONCLUSIONThe expression of Caspase-3 and Hsp70 at an early stage following severe TBI is characteristic and can be applied to estimate the time of injury.

Animals ; Brain Injuries ; metabolism ; Caspase 3 ; metabolism ; HSP70 Heat-Shock Proteins ; metabolism ; Immunohistochemistry ; Rabbits ; Random Allocation

Adenosine Monophosphate ; metabolism ; Genetic Pleiotropy ; HSP70 Heat-Shock Proteins ; metabolism ; Humans ; Neurodegenerative Diseases ; metabolism

AIMTo explore the effects of gentamicin ototoxicity on the expression of heat shock protein 70 in guinea pigs cochlea.

METHODSWe used immunohistochemistry staining and image quantitative analysis system, combined with auditory brainstem response (ABR) measurement to investigate the change on the expression of HSP70 in guinea pigs cochlea of gentamicin ototoxicity.

RESULTSThe levels of HSP70 immunoreactivity in guinea pigs cochlea of experimental animals were high including Corti's organ, stria vascularis, medial spiral limbus, spiral ganglion cells and the threshold of ABR was in high correlation with the expression of HSP70 ([ r] > 0.8, P < 0.01).

CONCLUSIONGentamicin can induce expression of HSP 70 in guinea pigs cochlea and protect hearing function.

Animals ; Cochlea ; drug effects ; physiopathology ; Gentamicins ; toxicity ; Guinea Pigs ; HSP70 Heat-Shock Proteins ; metabolism ; Heat-Shock Response ; drug effects

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

OBJECTIVETo investigate the protective role of inducible heat shock protein 70 (Hsp70) against damage induced by formaldehyde.

METHODSHuman bronchial epithelium (HBE) cells were transfected with plasmid harboring hsp70 gene to increase the protein expression level. HBE cells transfected with pcDNA3.1 plasmid were used as transfection control and HBE cells cultured at normal condition served as control. Three groups were marked as HBE/hsp70, HBE/pcDNA and HBE. Hsp70 expression levels of 3 groups were detected. The cells of HBE/hsp70 and HBE groups were exposed to different concentrations of formaldehyde (0,0.39,1.56,6.25 mmol/L) for 4 h. The contents of GSH and MDA were measured, and KCl-SDS method was applied to measure DNA-protein crosslink (DPC).

RESULTSHsp70 level in HBE/hsp70 group increased by 80% compared with HBE group. GSH contents in HBE/hsp70 group significantly increased and were 141.0, 119.6 mg/gpro at 0.39, 1.56 mmol/L, respectively (P<0.01), as compared with HBE group. However, it decreased when formaldehyde concentration increased to 6.25 mmol/L. While GSH content in HBE group remained decreasing. MDA contents in HBE/hsp70 and HBE group increased with formaldehyde. MDA content in HBE/hsp70 was 0.088 micromol/gpro and significantly lower than that (0.138 micromol/gpro) in HBE group (P<0.05) when formaldehyde concentration was 1.56 mmol/L, At the formaldehyde dose of 6.25 mmol/L MDA content in HBE/hsp70 was 0.140 micromol/gpro which was significantly lower than that (0.289 micromol/gpro) in HBE group (P<0.01). DPC% in two groups increased with formaldehyde. At the formaldehyde dose of 0.39 mmol/L, DPC% in HBE/hsp70 group was 3.94% which was significantly lower than that (6.25%) in HBE group (P< 0.01). At the formaldehyde dose of 1.56 mmol/L, DPC% in HBE/hsp70 group was 11.86% which was significantly lower than that (20.89%) in HBE group (P<0.05).

CONCLUSIONHsp70 can reduce formaldehyde-induced damages in human bronchial epithelium cells in vitro.

Cells, Cultured ; Epithelial Cells ; drug effects ; metabolism ; Formaldehyde ; toxicity ; Glutathione ; metabolism ; HSP70 Heat-Shock Proteins ; metabolism ; Humans ; Malondialdehyde ; metabolism ; Transfection

It has been proved in recent studies that the chronic gastric disease (CGD) of Pi-Wei damp-heat syndrome type (CGD-PWDH) is closely related with heat shock protein 70 (HSP70) and nuclear factor-kappa B (NF-kappaB). HSP70 can protect the auto-stability of cells and elevate the immune function in organism against tumor or multiple exogenous pathogens. Increasing of NF-kappaB expression presents in case of Helicobacter pylori (Hp) stimulation, it could induce inflammatory reaction, while inflammation factors could act inversely to enhance the expression of NF-kappaB, thus to cause and expand the damage of gastric mucosa. In addition, HSP shows blocking effect on the activation and expression of NF-kappaB. So, the author considered that in patients of Hp associated CGD-PEDH, HSP 70 exhibits the effect as that of "vital energy" and NF-kappaB play a role as the "evil qi" in Chinese medicine, the expressions of the two may embody the vital-evil combating manner of Pi-Wei damp-heat syndrome.
Gastrointestinal Diseases ; diagnosis ; metabolism ; HSP70 Heat-Shock Proteins ; metabolism ; Humans ; Medicine, Chinese Traditional ; methods ; NF-kappa B ; metabolism

BACKGROUNDGlucocorticoid (GC) insensitivity/GC resistance is an important etiological and prognostic factor in multiple diseases and pathophysiological processes such as scald, shock and asthma. The function of GC was mediated by glucocorticoid receptor (GR). Scald not only decreased the expression of GR but also reduced the affinity of GR, which played an important role in GC resistance in scalded rats. Whereas the molecular mechanism responsible for the decrease of GR affinity resulted from scald remains unclear. Recent studies showed that the changes of heat shock proteins (hsp) especially hsp90 and hsp70 of GR heterocomplex were associated with GR low affinity in vitro.

METHODSThe affinity of GR in hepatic cytosols and in the cytosols of SMMC-7721 cells were determined by radioligand binding assay and scatchard plot. GR heterocomplex in cytosols were captured by coimmunoprecipation and the levels of hsp90 and hsp70 of GR complex were detected by quantitative Western blotting.

RESULTSSimilar with that of hepatic cytosol of scalded rats, a remarkable decrease of GR affinity was also found in the cytosol of heat stressed SMMC-7721 cells. The level of hsp70 of GR complex in hepatic cytosol of scalded rats (30% total body surface area immersion scald) and in cytosol of heat stressed human hepatocarcinoma cell line SMMC-7721 were both increased by 1.5 fold, whereas no change of hsp90 in GR heterocomplex was found. According to the correlation analysis, there may be a positive relationship between increased hsp70 of GR complex and decreased GR affinity in the cytosols.

CONCLUSIONSThe primary results indicated that the level of hsp70 of GR heterocomplex was increased in the hepatic cytosol of scalded rats and the cytosol of heat stressed SMMC-7721 cells. The increase of hsp70 of GR complex might be associated with the decrease of GR affinity.

Animals ; Blotting, Western ; Burns ; physiopathology ; Cell Line ; HSP70 Heat-Shock Proteins ; metabolism ; Heat-Shock Response ; physiology ; Immunoprecipitation ; Protein Binding ; physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, Glucocorticoid ; metabolism

Animals ; Apoptosis ; Caspase 3 ; metabolism ; Caspase 8 ; metabolism ; Cells, Cultured ; HSP70 Heat-Shock Proteins ; metabolism ; Heat Stress Disorders ; metabolism ; Myocytes, Cardiac ; metabolism ; Rats ; Rats, Wistar