The influence of exercise at high temperature on adult males' routine blood indexes and biochemical indexes and the expression of HSP72 in peripheral blood lymphocytes (PBLs) was studied in order to provide theoretical ground for health supervision of adults receiving exercise at high temperature. 180 adult males were selected and divided into exercise group and control group, in which the exercise group was subdivided into subgroup 1 and subgroup 2 receiving exercise at high temperature in the afternoon and in the morning, respectively. Peripheral venous blood was phlebotomized before and after the exercise to examine routine blood indexes and blood biochemical indexes. The expression levels of HSP72 in PBLs were detected by flow cytometry. The results showed that the routine blood indexes and biochemical indexes in each group were within the range of normal values of male adults. There was no significant difference between each exercise group and control group in indexes before exercise. After exercise, the expression levels of HSP72 in PBLs in exercise groups were higher than those before exercise, and HSP72 expression levels in subgroup 1 were obviously higher than those in subgroup 2 and control group. The contents of ALT, urea, Na+, Cl-, Ca2+ and K+ in subgroups 1 and 2 were lower than those in control group, but CK level was higher than in control group (P<0.05). The contents of Na+ and Cl- in subgroup 1 were relatively lower than those in subgroup 2 (P<0.05). It was concluded that while receiving exercise at high temperature, adult males' HSP72 levels in PBLs could be increased and the biochemical indexes changed. Attention should be paid to health supervision to avoid obvious body injuries at high temperature.
Blood Chemical Analysis/*methods ; Exercise/*physiology ; HSP72 Heat-Shock Proteins/*blood ; HSP72 Heat-Shock Proteins/metabolism ; Hot Temperature ; Lymphocytes/*metabolism ; Young Adult

BACKGROUND AND OBJECTIVES: Heat shock protein (HSP) is to be involved in inflammation. HSP may be expressed in allergic rhinitis which is an inflammation disease. The purpose of this study was to investigate whether overexpression of HSP72 is specific for allergic rhinitis and is correlated with clinical severity of disease. MATERIALS AND METHODS: We studied expression of HSP72 by immunohistochemistry using ABC technique on nasal mucosa from 20 patients with allergic rhinitis, 10 patients with chronic hypertrophic rhinitis and 10 patients with normal turbinates. RESULTS: In biopsies from patients with allergic rhinitis, immunopositive cells were observed on epithelium, basement membrane, submucous gland cells, and inflammatory cells. Expression of HSP72 in patients with allergic rhinitis was significantly increased in nasal mucosa (p<0.01) and was significantly correlated with clinical severity of the disease (p<0.01) and eosinophil count (p<0.01). CONCLUSION: Inflammation of nasal mucosa in patients with allergic rhinitis may be linked to production of HSP72.
Basement Membrane ; Biopsy ; Eosinophils ; Epithelium ; Heat-Shock Proteins ; HSP72 Heat-Shock Proteins ; Humans ; Immunohistochemistry ; Inflammation ; Nasal Mucosa* ; Rhinitis* ; Turbinates

BACKGROUND AND OBJECTIVES: Heat shock proteins (HSPs) are group of evolutionary conserved proteins whose synthesis are greatly enhanced in cells following exposure to various stressors and play an important role in cellular protection and survival. The purpose of this study was to determine whether olfactory stimulation induces the synthesis of HSP72 in olfactory system of the rat. MATERIALS AND METHODS: Animals were exposed to odorant stimuli using 2% propionic acid odorant stimuli and expression pattern of HSP72 in the olfactory system were detected by immunohistochemistry using anti-HSP72 antibody according to time course and by Western blotting. RESULTS: HSP72 immunopositive cells were expressed in the olfactory epithelium and in the olfactory bulb neurons and a 72 kD band was detected by Western blotting. CONCLUSION: These results suggest that expression of HSP72 in olfactory system of the rat following exposure to odor may serve as a marker for cellular stress and potential damage and may be involved in cellular protection against injuries.
Animals ; Blotting, Western ; Diethylpropion ; Heat-Shock Proteins* ; Hot Temperature* ; HSP72 Heat-Shock Proteins* ; Immunohistochemistry ; Neurons ; Odors* ; Olfactory Bulb ; Olfactory Mucosa ; Rats*

BACKGROUND AND OBJECTIVES: Several studies have attempted to show the reasons for ototoxicity induced by cisplatin, but the cochlear ototoxicity remained poorly understood. Recently, it is considered that free radicals play an important role in cisplatin ototoxicity. Heat shock proteins (HSP) are consistently present at some level in normal tissues and increased synthesis following stress. They have been implicated in the role of cellular protection during sub-lethal stressors. Many studies have demonstrated the increased synthesis of HSP following hyperthermia, ischemia, surgical injury and noise exposure. Free radicals are also considered as important inducer of HSP. The purpose of this study was to demonstrate the increase of HSP after cisplatin injection. MATERIALS AND METHOD: Thirty six Albano guinea pigs were used in this study. The animals were injected with a dose of 8 mg/kg cisplatin intraperitoneally. Cochleae are harvested 1, 3, 5 or 6, 12, 24 hours after injection. Immunocytochemistry and surface preparation method were used to detect the expression of HSP 72 in the cochlear tissues. RESULTS: The level of HSP 72 immunoreactivity began increasing by 3 hours after injection and continued to increase thereafter to reach maximal levels at 6 hours. Twelve hours after injection, the level of HSP 72 seemed to decrease to its normal levels. The increase of HSP 72 was mainly detected in Deiters' cells. CONCLUSION: Cisplatin induces a HSP in the guinea pig cochlea, particularly in the organ of Corti. However, further studies including quantitative analysis should be followed.
Animals ; Cisplatin* ; Cochlea ; Fever ; Free Radicals ; Guinea Pigs ; Heat-Shock Proteins* ; Hot Temperature* ; HSP72 Heat-Shock Proteins* ; Immunohistochemistry ; Intraoperative Complications ; Ischemia ; Noise ; Organ of Corti

OBJECTIVETo examine the inhibition of nitric oxide (NO) synthesis during ischemic preconditioning (IP) upon the induction of heat-shock protein 72 (HSP72) and the size-limiting effect of the second window of protection on infarction.

METHODSRabbits were subjected to either 4 cycles of 5-min long coronary artery occlusion separated by 10 min of reperfusion, or a sham operation. During this procedure, we administered 10 mg/kg of N(G)-nitro-L-arginine methyl ester (L-NAME, an inhibitor of NO synthase) intravenously 5 min before IP followed by its continuous infusion (1.5 mg/kg/min). Twenty-four hours after IP or the sham operation, the hearts were rapidly excised for assay of HSP72 expression or were subjected to 30 min of coronary artery occlusion followed by 120 min of reperfusion, at which point infarct size (IS) was measured.

RESULTSTwenty-four hours after IP or the sham operation, there was no difference in heart rate or mean arterial pressure between the groups. Immunoblotting revealed an increase in HSP72 protein levels in the IP group, which was blocked by L-NAME. IS in the IP rabbits was reduced compared with controls (29.8 +/- 3.7% vs. 50.8 +/- 4.3%, P < 0.01). IS in the IP rabbits was elevated as a result of L-NAME treatment (46.0 +/- 5.1%). Administration of L-arginine reversed the effects of L-NAME on the induction of HSP72 and IS (33.5 +/- 4.0%). The intravenous administration of S-nitroso-N-acetylpenicillamine (an NO donor, 15 microg/kg/min) over 20 min increased the induction of HSP72 and reduced IS (31.3 +/- 5.7%, P < 0.01 vs. control) 24 h later.

CONCLUSIONThese findings suggest that NO may be involved in the induction of HSP72 and the opening of the second window of protection of IP.

Animals ; HSP72 Heat-Shock Proteins ; Heat-Shock Proteins ; biosynthesis ; Hemodynamics ; drug effects ; Ischemic Preconditioning, Myocardial ; Male ; Myocardial Infarction ; pathology ; Nitric Oxide ; physiology ; Penicillamine ; analogs & derivatives ; pharmacology ; Rabbits

OBJECTIVETo investigate the effect of graded hypothermia on neuropathologic alterations of neonatal rat brain after exposed to hypoxic-ischemic insult at 37°C, 33°C, 31°C, and 28°C, respectively, and to observe the effect of hypothermia on 72-kDa heat shock protein (HSP72) expression after hypoxic-ischemic insult.

METHODSSeven days old Wistar rats were subjected to unilateral common carotid artery ligation followed by exposure to hypoxia in 8% oxygen for 2 hours at 37°C, 33°C, 31°C, and 28°C, respectively. The brain temperature was monitored indirectly by inserting a mini-thermocouple probe into the temporal muscle during hypoxia. After hypoxia-ischemia their mortality was assessed. Neuronal damage was assessed with HE staining 72 hours after hypoxia. HSP72 expression at 0.5, 24, and 72 hours of recovery was immunohistochemically assessed using a monoclonal antibody to HSP72.

RESULTSHypoxia-ischemia caused 10.5% (2/19) of mortality in rat of 37°C group, but no death occurred in 33°C, 31°C or 28°C groups. HE staining showed neuropathologic damage was extensive in rats exposed to hypoxia-ischemia at 37°C (more than 80.0%). The incidence of severe brain damage was significantly decreased in 33°C (53.3%) and 31°C groups (44.4%), and no histologic injury was seen in the 28°C group of rats. Expression of HSP72 was manifest and persistent in the rat brain of 37°C group, but minimum in the rat brain of 28°C group.

CONCLUSIONMild and moderate hypothermia might prevent cerebral visible neuropathologic damage associated with hypoxic-ischemic injury by decreasing stress response.

Animals ; Animals, Newborn ; Body Temperature ; Female ; HSP72 Heat-Shock Proteins ; metabolism ; Hypothermia ; Hypoxia-Ischemia, Brain ; pathology ; Pregnancy ; Rats ; Rats, Wistar

BACKGROUNDHeat shock protein 70 (HSP70) is expressed highly in epithelial tumours associated closely with human papillomavirus 16 (HPV16) infections. However, evidence about the direct relationship between HSP70 expression and HPVs infections are still lacking. In the present study, we examined the expression of HSP70 in keratinocytes introduced with HPV16 E6/E7 oncogenes.

METHODSStable transfected cells were established by transfection of the plasmids pLXSN16E6/E7 into cultured primary keratinocytes and subsequently selected by plasmid specific selection antibiotic (G418) at the required concentration. The expression of HSP70 in pLXSN16E6/E7 transfected keratinocytes was determined by Western blot. The correlation of HSP70 expression and E6/E7 transfection was further confirmed by doubly labelled immunofluorescent staining.

RESULTSCompared to non-transfected keratinocytes, there was a significant trend for higher levels of HSP70 in pLXSN16E6/E7 transfected keratinocytes. Doubly labelled immunofluorescent staining experiment showed that the co-localization of HPV16 E6/E7 and HSP70 in transfected keratinocytes was observed and increased expression of HSP70 was strongly associated with the transfection of HPV16 E6/E7.

CONCLUSIONSOur studies demonstrated increased levels of HSP70 proteins in keratinocytes stably transfected by HPV16 E6/E7 oncogenes. It suggests that the expression of HSP70 is modulated by HPV16 E6/E7 proteins, which may be involved in HPV16 E6/E7 induced immortalization.

Cells, Cultured ; HSP72 Heat-Shock Proteins ; biosynthesis ; Humans ; Keratinocytes ; metabolism ; Oncogene Proteins, Viral ; genetics ; Papillomavirus E7 Proteins ; Repressor Proteins ; genetics ; Transfection

The causal relationship between heat shock protein (HSP) and second window of cardioprotective effect is still undetermined. In the present study, we assessed whether HSP-producing substances, amphetamine and ketamine, afforded protection against reperfusion-induced ventricular fibrillation (VF) and these protective effect remained after the inhibition of HSP72 production by quercetin, a mitochondrial ATPase inhibitor. Adult mongreal male cats (n=60, 2.5 ~ 4 kg) were used in this study. Experimental animals were divided into five groups; control group (n=15), amphetamine ('A', n=11) group, ketamine ('K', n=9) group, amphetamine-ketamine ('AK', n=16) group and amphetamine-ketamine-quercetin ('AKQ', n=9) group. Twenty-four hours after the drug treatment, an episode of 20-min coronary artery occlusion was followed by 10-min reperfusion. The incidence of reperfusion-induced VF in the AK and AKQ groups was significantly lower than that in control group (p<0.01). After the ischemia/reperfusion procedure, western blot analysis of HSP72 expression in the myocardial tissues resected from each group was performed. HSP72 production in the AK group was marked, whereas HSP72 was not detected in the AKQ and control groups. These results suggest that the suppressive effect against reperfusion-induced VF induced by amphetamine and ketamine is not mediated by myocardial HSP72 production but by other mechanisms.
Adenosine Triphosphatases ; Adult ; Amphetamine ; Animals ; Arrhythmias, Cardiac* ; Blotting, Western ; Cats ; Coronary Vessels ; Heat-Shock Proteins* ; Hot Temperature* ; HSP72 Heat-Shock Proteins* ; Humans ; Incidence ; Ketamine ; Male ; Quercetin ; Reperfusion* ; Ventricular Fibrillation

Recently, there are numerous efforts to explain the psycho-, neurological events through molecular biological standards. Because of the property as a strong stimulant to neural cells, convulsions induced by electroconvulsive shock (ECS) or kainic acid are used for neurobiological research. In this study, the effect of systemic administration of kainic acid and ECS on the expression of hsp 72 mRNA in the rat brain was investigated with in situ hybridization histochemistry. The induction of hsp 72 mRNA was observed in the dentate gyrus from 2 hr after KA treatment. After that, the expression was gradually increased in the various areas including dentate gyrus, hippocampus, olfactory bulb, cerebral cortex, caudate-putamen, thalamus, and peaked at 9 hr after KA treatment. At the 72 hr after KA treatment, weak expression was found only in the CA3 area of hippocampus. However, the expression of hsp 72 mRNA was not detected in any ESC treated rat brains, we examined.The inducton of c-fos was observed from 15 min, peaked at 6 hr, and returned to basal level at 48 hr after KA treatment. The expression of c-fos was observed in the same areas that showed induction of hsp 72 mRNA. In the ECS treated rat brains, the induction of c-fos was found in the dentate gyrus, olfactory bulb and cerebral cortex at 15 min and 30 min after ESC. From these results, it may be suggested that the effects of KA treatment and ECS on the neuronal cells are different, and it is due to difference in induction mechanism of convulsion between KA and ECS. And, the similarity between the expression pattern of hsp 72 mRNA by KA and KA receptor suggests that the induction of hsp 72 mRNA is based on the direct effect of KA through KA receptor.
Animals ; Brain* ; Cerebral Cortex ; Dentate Gyrus ; Electroshock ; Gene Expression ; Heat-Shock Proteins* ; Hippocampus ; Hot Temperature* ; HSP72 Heat-Shock Proteins* ; In Situ Hybridization ; Kainic Acid ; Neurons ; Olfactory Bulb ; Rats* ; RNA, Messenger ; Seizures ; Thalamus

Heat shock protein 72 (HSP72) appears to play an important role in cell survival in the hypertonic conditions of the renal medulla. The purpose of this study was to examine the effect of potassium deprivation on renal HSP72 expression. Male Sprague-Dawley rats were fed potassium deficient diet for 2 weeks. Kidney tissues were preserved by in vivo perfusion with paraformaldehyde-lysine-periodate (PLP) and processed for Western blot analysis and immunocytochemistry. Serum potassium concentration and urine osmolality decreased in potassium deprivated animals. In control kidneys, HSP72 immunostaining was observed mainly in the inner medulla in almost all cells including the inner medullary collecting duct and papillary surface epithelial cells. In potassium deprivated kidneys, HSP72 expression decreased dramatically in the inner medulla. However, strong HSP72 immunostaining remained in some inner medullary collecting duct and papillary surface epithelial cell. These results demonstrated that potassium deprivation induced down regulation of HSP72 in the renal medulla, at least in part, through cell-specific manner.
Animals ; Blotting, Western ; Cell Survival ; Diet ; Down-Regulation ; Epithelial Cells ; Heat-Shock Proteins* ; Hot Temperature* ; HSP72 Heat-Shock Proteins* ; Humans ; Immunohistochemistry ; Kidney* ; Male ; Osmolar Concentration ; Perfusion ; Potassium ; Rats* ; Rats, Sprague-Dawley