scholarly journals Heat shock protein 70 could enhance porcine epidemic diarrhoea virus replication by interacting with membrane proteins

2021 ◽  
Vol 52 (1) ◽  
Author(s):  
Jae-Yeon Park ◽  
Jihoon Ryu ◽  
Jung-Eun Park ◽  
Eui-Ju Hong ◽  
Hyun-Jin Shin
Keyword(s):  
Heat Shock ◽  
Membrane Proteins ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Early Stage ◽  
Hsp70 Expression ◽  
Porcine Epidemic Diarrhoea Virus ◽  
Diarrhoea Virus ◽  
M Proteins ◽  
Infected Cells

AbstractIn this study, we investigated the role of heat shock protein 70 (HSP70) in porcine epidemic diarrhoea virus (PEDV) replication. We found that PEDV infection induced strong HSP70 overexpression in the very early stage of infection. We also confirmed that HSP70 overexpression increased the speed of PEDV replication, resulting in the generation of more virions. In contrast, knockout of HSP70 in cells significantly downregulated PEDV protein expression, resulting in a significant reduction in PEDV replication. Most importantly, we confirmed that among the structural proteins of PEDV, membrane (M) proteins have this important role. We found that membrane proteins control cellular HSP70 expression in PEDV-infected cells. We confirmed HSP70/M complex formation by both immunoprecipitation and immunofluorescence assays. Additionally, PEDV M overexpression induced strong HSP70 expression. All our results clearly confirmed that in PEDV-infected cells, the M protein plays a very important role in PEDV replication in collaboration with HSP70.

scholarly journals Effects ofHelicobacter pyloriand Heat Shock Protein 70 on the Proliferation of Human Gastric Epithelial Cells

2014 ◽  
Vol 2014 ◽  
pp. 1-5 ◽  
Author(s):  
Liping Tao ◽  
Hai Zou ◽  
Zhimin Huang
Keyword(s):  
Helicobacter Pylori ◽  
Heat Shock ◽  
Epithelial Cells ◽  
Heat Shock Protein ◽  
Mtt Assay ◽  
Heat Shock Protein 70 ◽  
Hsp70 Expression ◽  
Gastric Epithelial Cells ◽  
Ags Cells ◽  
H Pylori

Infection ofHelicobacter pylori (H. pylori)changed the proliferation of gastric epithelial cells and decreased the expression of heat shock protein 70 (HSP70). However, the effects ofH. pylorion the proliferation of gastric epithelial cells and the roles of HSP70 during the progress need further investigation.Objective.To investigate the effects ofHelicobacter pylori (H. pylori)and heat shock protein 70 (HSP70) on the proliferation of human gastric epithelial cells.Methods. H. pyloriand a human gastric epithelial cell line (AGS) were cocultured. The proliferation of AGS cells was quantitated by an MTT assay, and the expression of HSP70 in AGS cells was detected by Western blotting. HSP70 expression in AGS cells was silenced by small interfering RNA (siRNA) to investigate the role of HSP70. ThesiRNA-treated AGS cells were cocultured withH. pyloriand cell proliferation was measured by an MTT assay.Results.The proliferation of AGS cells was accelerated by coculturing withH. pylorifor 4 and 8 h, but was suppressed at 24 and 48 h. HSP70 expression was decreased in AGS cells infected byH. pylorifor 48 h. The proliferation in HSP70-silenced AGS cells was inhibited after coculturing withH. pylorifor 24 and 48 h compared with the control group.Conclusions.Coculture ofH. pylorialtered the proliferation of gastric epithelial cells and decreased HSP70 expression. HSP70 knockdown supplemented the inhibitory effect ofH. pylorion proliferation of epithelial cells. These results indicate that the effects ofH. pylorion the proliferation of gastric epithelial cells at least partially depend on the decreased expression of HSP70 induced by the bacterium.

Effects of ferulic acid on oxidative stress, heat shock protein 70, connexin 43, and monoamines in the hippocampus of pentylenetetrazole-kindled rats

2017 ◽  
Vol 95 (6) ◽  
pp. 732-742 ◽  
Author(s):  
Abdelaziz M. Hussein ◽  
Khaled M. Abbas ◽  
Osama A. Abulseoud ◽  
El-Hussainy M.A. El-Hussainy
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Ferulic Acid ◽  
Group Treatment ◽  
Heat Shock Protein 70 ◽  
Connexin 43 ◽  
Hsp70 Expression ◽  
Neuroprotective Effects ◽  
Cx43 Expression

The present study investigated the effects of ferulic acid (FA) on pentylenetetrazole (PTZ)-induced seizures, oxidative stress markers (malondialdehyde (MDA), catalase, and reduced glutathione (GSH)), connexin (Cx) 43, heat shock protein 70 (Hsp 70), and monoamines (serotonin (5-HT) and norepinephrine (NE)) levels in a rat model of PTZ-induced kindling. Sixty Sprague Dawley rats were divided into 5 equal groups: (a) normal group; (b) FA group: normal rats received FA at a dose of 40 mg/kg daily; (c) PTZ group: normal rats received PTZ at a dose of 50 mg/kg i.p. on alternate days for 15 days; (d) FA-before group: treatment was the same as for the PTZ group, except rats received FA; and (e) FA-after group: rats received FA from sixth dose of PTZ. PTZ caused a significant increase in MDA, Cx43, and Hsp70 along with a significant decrease in GSH, 5-HT, and NE levels and CAT activity in the hippocampus (p < 0.05). Pre- and post-treatment with FA caused significant improvement in behavioral parameters, MDA, CAT, GSH, 5-HT, NE, Cx43 expression, and Hsp70 expression in the hippocampal region (p < 0.05). We conclude that FA has neuroprotective effects in PTZ-induced epilepsy, which might be due to attenuation of oxidative stress and Cx43 expression and upregulation of neuroprotective Hsp70 and neurotransmitters (5-HT and NE).

scholarly journals The effect of red-fleshed pitaya (Hylocereus polyrhizus) on heat shock protein 70 and cortisol expression in strenuous exercise induced rats

F1000Research ◽  
2019 ◽  
Vol 8 ◽  
pp. 130
Author(s):  
Novita Sari Harahap ◽  
Aznan Lelo ◽  
Ambrosius Purba ◽  
Awaluddin Sibuea ◽  
Rina Amelia ◽  
...  
Keyword(s):  
Body Weight ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
The Body ◽  
Male Rats ◽  
Strenuous Exercise ◽  
Hsp70 Expression ◽  
Average Weight ◽  
Significant Difference

Background: Oxidative stress from exercise can contribute to damaging cells, increasing heat shock protein 70 (HSP70) and suppressing the immune system in the body. This research aimed to determine the antioxidant potential of red-fleshed pitaya extract on HSP70 and cortisol expression in rats which were subjected to strenuous exercise. Methods: The subjects of this research were 32 Sprague Dawley male rats, aged 3 months, with an average weight of 200 g. Red-fleshed pitaya extract was obtained from methanol extraction process; a maceration technique was performed and the extract was concentrated using an air-drying method. Rats were randomly divided into four groups. Group 1 were subjected to strenuous exercise and treated with distilled water only; while Groups 2, 3 and 4 were subjected to strenuous exercise and treated with 100 mg/kg body weight, 200 mg/kg body weight and 300 mg/kg body weight of red-fleshed pitaya extract, respectively. Strenuous exercises in rats was performed by intense swimming of 20 min/day, 3 days a week for 3 weeks. HSP70 expression and cortisol were measured with Enzyme-Linked Immune Sorbent Assay (ELISA) method. Results: There was a significant reduction of HSP70 (p=0.000) and cortisol expression (p=0.000) between the groups. Also, there was a significant difference in the average decreasing of HSP70 expression between group 4 and either groups 1 or 2 (p=0.000). However, a significant difference between groups 4 and 3 was not observed (p=0.813). Lastly, a significant difference was found in the average decrease of cortisol expression between groups 4 and 1 (p=0.000), 2 (p=0.000), and 3 (p=0.000) respectively. Conclusion: Red-fleshed pitaya is potential to be utilized as antioxidant to decrease the HSP70 and cortisol expression.

scholarly journals Expression of heat shock protein 70 is insufficient to extend Drosophila melanogaster longevity

2019 ◽  
Author(s):  
Chengfeng Xiao ◽  
Danna Hull ◽  
Shuang Qiu ◽  
Joanna Yeung ◽  
Jie Zheng ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Resistance ◽  
Heat Shock Protein 70 ◽  
Biological Effect ◽  
Hsp70 Expression ◽  
Gene Encoding ◽  
Shock Proteins

AbstractIt has been known for over 20 years that Drosophila melanogaster flies with twelve additional copies of the hsp70 gene encoding the 70 kDa heat shock protein lives longer after a non-lethal heat treatment. Since the heat treatment also induces the expression of additional heat shock proteins, the biological effect can be due either to HSP70 acting alone or in combination. This study used the UAS/GAL4 system to determine whether hsp70 is sufficient to affect the longevity and the resistance to thermal, oxidative or desiccation stresses of the whole organism. We observed that HSP70 expression in the nervous system or muscles has no effect on longevity or stress resistance but ubiquitous expression reduces the life span of males. We also observed that the down-regulation of Hsp70 using RNAi did not affect longevity.

scholarly journals Circulating Heat Shock Protein 70 Is a Novel Biomarker for Early Diagnosis of Lung Cancer

2018 ◽  
Vol 2018 ◽  
pp. 1-8 ◽  
Author(s):  
Tielong Tang ◽  
Chao Yang ◽  
Ham Ebo Brown ◽  
Jing Huang
Keyword(s):  
Lung Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Patients ◽  
Heat Shock Protein 70 ◽  
Early Stage ◽  
Growth And Survival ◽  
Lung Cancer Patients ◽  
Cellular Stresses ◽  
Sensitivity Specificity

Heat shock protein 70 (HSP70) was a highly conserved protein which was significantly induced in response to cellular stresses. HSP70 played an important role in the pathogenesis of cancer which stabilized the production of large amount of oncogenic proteins and finally supported growth and survival of tumor. However, there was no report about the diagnosis of circulating HSP70 in lung cancer patients. In this study, a total of 297 participants (lung cancer: 197, healthy control: 100) were enrolled in the detection of circulating HSP70 level in plasma by ELISA assay. The results indicated that circulating HSP70 significantly decreased in lung cancer patients compared to healthy controls (P<0.0001). Receiver operating characteristic (ROC) analysis showed that HSP70 (AUC: 82.2%, SN: 74.1%, SP: 80.0%) had higher diagnosis value than clinical existing biomarkers CEA (AUC: 80.1%, SN: 76.8%, SP: 67.3%) and CA 19-9 (AUC: 63.7%, SN: 64.2%, SP: 54.0%). In the analysis of early lung cancer patients, ROC results also revealed that HSP70 (AUC: 83.8%, SN: 71.2%, SP: 84.0%) have higher sensitivity, specificity, and AUC than CEA (AUC: 73.7%, SN: 73.2%, SP: 69.1%) and CA 19-9 (AUC: 61.5%, SN: 69.4%, SP: 53.4%). In analysis of specific histological classifications, HSP70 showed more valuable in the diagnosis of SCC (AUC: 85.9%, SN: 86.1.9%, SP: 81.0%) than ADC (AUC: 81.0%, SN: 69.1%, SP: 81.0%). Combined analysis of HSP70 and existing biomarker: CEA and CA 19-9 exhibited that HSP70 combined CEA and CA 19-9 showed the highest AUC (0.945, 95% CI, 0.855–1.000). The importance of our results was that we found decreased circulating HSP70, in combination with elevated CEA and CA 19-9, could be utilized in the diagnosis of early (stage I and II) lung cancer.

scholarly journals miR-16-1 Promotes the Aberrantα-Synuclein Accumulation in Parkinson Disease via Targeting Heat Shock Protein 70

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Zhelin Zhang ◽  
Yan Cheng
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Parkinson Disease ◽  
Heat Shock Protein 70 ◽  
Neuroblastoma Cell ◽  
Neuroblastoma Cell Line ◽  
Hsp70 Expression ◽  
Human Neuroblastoma Cell ◽  
Human Neuroblastoma ◽  
Human Neuroblastoma Cell Line

There is striking evidence that heat shock protein 70 (Hsp70) negatively regulatesα-synuclein aggregation, which plays a significant role in the formation and progression of Parkinson disease (PD). However, how the Hsp70 in neurons fails to prevent or even reverseα-synuclein aggregation and toxicity in PD still remains to be determined. In the present study, we constructed anα-synuclein-overexpressed human neuroblastoma cell line, SH-SY5Y-Syn, in which the blockage of Hsp70 promotedα-synuclein aggregation. And we also found that miR-16-1 downregulated Hsp70 and promotedα-synuclein aggregation in the SH-SY5Y-Syn cells. This study revealed a novel regulatory mechanism of Hsp70 expression, which might contribute to the PD development.

Exogenous heat shock protein-70 inhibits cigarette smoke-induced intimal thickening

2008 ◽  
Vol 295 (4) ◽  
pp. R1320-R1327 ◽  
Author(s):  
Michiaki Matsumoto ◽  
Paul C. Dimayuga ◽  
Charles Wang ◽  
Jonathan Kirzner ◽  
Miha Cercek ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cigarette Smoke ◽  
Heat Shock Protein 70 ◽  
Nuclear Antigen ◽  
Cigarette Smoke Exposure ◽  
Hsp70 Expression ◽  
Intimal Thickening ◽  
Hsp70 Mrna ◽  
Recombinant Hsp70

Cigarette smoke is associated with increased carotid intimal thickening or stroke. Preliminary work showed that exposure to smoke resulted in a 4.5-fold reduction of heat shock protein-70 (HSP70) expression in spleens of mice using gene microarray analysis. In the current study, we investigated the role of extracellular HSP70 in carotid intimal thickening of mice exposed to cigarette smoke. Intimal thickening was induced by placement of a cuff around the right carotid artery of mice. Cuff injury resulted in increased HSP70 mRNA expression in carotid arteries that persisted for 21 days. Cigarette smoke exposure decreased arterial HSP70 expression and significantly increased intimal thickening compared with mice exposed to air. Treatment of mice exposed to cigarette smoke with intravenous recombinant HSP70 attenuated intimal thickening through reduced phosphorylated extracellular signal-regulated kinase (pERK) expression in the arterial wall. In vitro experiments with rat aortic smooth muscle cells confirmed that recombinant HSP70 decreases pERK and proliferating cell nuclear antigen (PCNA) expression in cells exposed to cigarette smoke extract and H2O2. Our study suggests that decreased expression of arterial HSP70 is an important mechanism by which exposure to cigarette smoke augments intimal thickening. The effects of recombinant HSP70 suggest a role for extracellular HSP70.

scholarly journals THE EFFECT OF PSYCHOLOGICAL STRESS ON MPF INTRAFOLLICULAR

2019 ◽  
pp. 127-130
Author(s):  
REVI GH NOVIKA ◽  
BUDI SANTOSO ◽  
WIDJIATI WIDJIATI
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Psychological Stress ◽  
Heat Shock Protein 70 ◽  
Regulatory Protein ◽  
Control Group ◽  
Hsp70 Expression ◽  
Control Group Design ◽  
Cortisol Levels ◽  
Experimental Group

Objective: The aim of the study is to investigate the influence of cortisol and Heat Shock Protein 70 (HSP70) on the stressed mice to maturationpromoting factor (MPF) expression intrafollicular.Methods: Experimental laboratory with Randomized Post Test Only Control Group Design was carried out on intrafollicular mice. Divided into twogroups, experimental and control groups. The experimental group was given a 95 dB 4 hours/day noisy exposure for 5 days which was analogous topsychological stress in humans and the control group was not given noisy exposure. Furthermore, both groups were examined for cortisol levels toensure stress in mice. Heat shock protein 70 (HSP70) expression was examined as the main regulatory protein for stress response and Maturationpromoting factor (MPF) expression which is a mediator for oocyte maturation.Results: Psychological stress by 95 dB/4 hours/day noisy exposure for 5 days significantly increased serum cortisol levels in experimental group(p=0.000) and HSP70 expression (p=0.000). The effect of Increased cortisol levels and HSP70 expression significantly decrease in MPF expression(p=0.000).Conclusion: The study concluded that psychological stress could be seen by increasing cortisol and HSP70 expression affected to decreasing MPFexpression intrafollicular

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