• The Korean Journal of Physiology and Pharmacology
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• v.14 no.3
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• pp.157-161
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• 2010

Heat shock proteins (HSPs) are specifically induced by various forms of stress. Hsp70.1, a member of the hsp70 family is known to play an important role in cytoprotection from stressful insults. However, the functional role of Hsp70 in motor function after spinal cord injury (SCI) is still unclear. To study the role of hsp70.1 in motor recovery following SCI, we assessed locomotor function in hsp70.1 knockout (KO) mice and their wild-type (WT) mice via the Basso, Beattie and Bresnahan (BBB) locomotor rating scale, before and after spinal hemisection at T13 level. We also examined lesion size in the spinal cord using Luxol fast blue/cresyl violet staining. One day after injury, KO and WT mice showed no significant difference in the motor function due to complete paralysis following spinal hemisection. However, when it compared to WT mice, KO mice had significantly delayed and decreased functional outcomes from 4 days up to 21 days after SCI. KO mice also showed significantly greater lesion size in the spinal cord than WT mice showed at 21 days after spinal hemisection. These results suggest that Hsp70 has a protective effect against traumatic SCI and the manipulation of the hsp70.1 gene may help improve the recovery of motor function, thereby enhancing neuroprotection after SCI.

• Proceedings of the KSAR Conference
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• 2002.06a
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• pp.59-59
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• 2002

돼지에서 스트레스관련 PSS(porcine stress syndrome) 및 HSP70(heat shock protein 70) 유전자형이 번식능력과 관련된 유전특성을 구명하기 위하여 PCR 용 프라이머의 염기서열을 설계하였다. PSS 는 Brenig등 (1992)의 RYR1 유전자 exon17 영역의 DNA에 근거한 18586-18659 영역과 GenBank (accession No. X68213) 의 HSP70 cDNA에 근거하여 290-512, 830-1424 및 1363-2041 영역으로 이루어졌다. (중략)

• Korean Journal of Environmental Biology
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• v.21 no.3
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• pp.313-318
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• 2003

Environmental stresses, such as heat shock, alcohol and physiological salt have been shown to induce a group of protein called heat shock protein (HSPs) in various tissues. In this investigation, we studied that arsenic stress would alter contraction of isolated rat aorta and expression of heat shock protein 70 and investigated the relation between expression of HSP 70 and vascular contractility of isolated rat aorta. Rat aorta strips, mounted in organ baths were exposed to 0, 0.5, 1,2 and 4 mM arsonic for 60 min. and 1,3 and 8 hours later tested for contractile response and expression of heat shock protein 70. Contractility of rat aorta were determined by isometric transducer connected to computerized physiograph and expression of HSP 70 was characterized by western blotting, respectively. Potassium chloride (55 mM) significantly augmented vascular contractility of yat aorta by 39％ compared with the control at 8 hours but not one or three hours after treatment of 4 mM arsenic. Arsonic stress (4 mM) also increased the expression of HSP 70 in rat aorta at 8 hours but one or three hours compared with the control and HSP expressed in vascular smooth muscle cells and some expressed in endothelium cells. These results suggest that arsenic stress not only did alter the magnitude of the contractile response to high potassium chloride but also increased the expression of HSP 70 in the rat aorta.

• Journal of the Korean Association of Oral and Maxillofacial Surgeons
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• v.30 no.4
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• pp.323-330
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• 2004

Estrogen may promote osteoblast/osteocyte viability by limiting apoptotic cell death. We hypothesize that hsp27 is an estrogen- regulated protein that can promote osteoblast viability by increasing osteoblast resistance to apoptosis. The purpose of this study was to determine the effect of estrogen treatment and heat shock on $TNF{\alpha}$ - induced apoptosis in the MC3T3-E1 cell line. Cells were treated with 0 - 100 nM $17{\beta}$ estradiol (or ICI 182780) for 0 - 24 hours before heat shock. After recovery, apoptosis was induced by treatment with 0 - 10 ng/ml TNF${\alpha}$. Hsp levels were evaluated by Northern and Western analysis using hsp27, hsp47, hsp70c and hsp70i - specific reagents. Apoptosis was revealed by in situ labeling with Terminal Deoxyribonucleotide Transferase (TUNEL). A 5 - fold increase in hsp27 protein and mRNA was noted after 5 hours of treatment with 10 - 20 nM $17{\beta}$ estradiol prior to heat shock. Increased abundance of hsp47, hsp70c or hsp70i was not observed. TUNEL indicated that estrogen treatment also reduced (50%) MC3T3-E1 cell susceptibility to $TNF{\alpha}$ - induced apoptosis. Treatment with hsp27-specific antisense oligonucleotides prevented hsp27 protein expression and abolished the protective effects of heat shock and estrogen treatment on $TNF{\alpha}$- induced apoptosis. Hsp27 is a determinant of osteoblast apoptosis, and estrogen treatment increases hsp27 levels in cultured osteoblastic cells. Hsp27 contributes to the control of osteoblast apoptosis and may be manipulated by estrogenic or alternative pathways for the improvement of bone mass.

• Entomological Research
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• v.48 no.5
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• pp.416-428
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• 2018

To gain an insight into the function of heat shock proteins (HSPs) in insects during thermal stress, three HSP cDNAs were identified in the transcriptome of adult Heortia vitessoides, one of the most destructive defoliating pests in Aquilaria sinensis (Loureiro) Sprenger forests. The open reading frames of HvHsp60, HvHsp70, and HvHsp90 were 1,719, 2,070, and 2,151 bp in length, respectively, and encoded proteins with molecular weights of 61.05, 75.02, and 82.23 kDa, respectively. Sequence analysis revealed that all three HSPs were highly conserved in structure. Regarding the stage-specific expression profiles, HvHsp60, HvHsp70, and HvHsp90 mRNAs were detected in all developmental stages. Regarding the tissue-specific expression profiles, the expression levels of the three HSP genes were different in various larval and adult tissues. Moreover, the expression patterns of heat-stressed larvae, pupae, and adults indicated that HvHsp60, HvHsp70, and HvHsp90 were heat-inducible. In particular, HvHsp60 transcripts increased dramatically in larvae and pupae that were heat-stressed at $40^{\circ}C$ and were upregulated in adults that were heat-stressed at $35^{\circ}C$ and $40^{\circ}C$. The expression of HvHsp70 significantly increased in all of the three different developmental stages at $35^{\circ}C$, $40^{\circ}C$, and $45^{\circ}C$. The expression of HvHsp90 obviously increased at $30^{\circ}C$, $35^{\circ}C$, and $40^{\circ}C$ in larvae and could be induced at $35^{\circ}C$ in pupae and adults. The results suggest that HSP60, HSP70, and HSP90 play a major role in protecting H. vitessoides against high-temperature stress.

• Journal of Embryo Transfer
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• v.22 no.4
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• pp.257-263
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• 2007

This study was performed to investigate the relationship between PSS-HSP70 gene polymorphism and artificial insemination (AI) reproductivity in the pigs. The RFLP polymorphism of PSS and the SSCP polymorphisms of HSP70 K1, K3 and K4 PCR product were detected different patterns. In the experiment for AI of fresh semen, spring and fall season showed higher litter size born of 10.89 head than 10.47 head of summer season. Landrace was showed higher litter size of 9.96 head than that of Duroc and Yorkshire (p<0.05). Stress relating PSS and HSP70 polymorphism of PSS-Normal, HSP70 K1-BB, K3-AB, K4-AA showd a highest litter size born of 10.97 head and litter size born alive of 10.69 head than that of the other polymorphisms(p<0.05). In the experiment for AI of frozen semen, effects of season and pig breeds were not showed for litter size born. The stress relating polymorphism of PSS-Carrier, HSP70 K1-BB, K3-BB, K4-AB showed highest litter size born of 11.29 head and litter size born alive of 10.82 head and PSS-Normal, HSP70 K1-BB, K3-AB, K4-AA showed the lowest litter size born of 8.48 head and litter size born alive of 7.33 head than that of the other polymorphisms(p<0.05). These results suggest that AI litter size born for the stress of forzen thawed semen may be affected by PSS and HSP70 polymorphism in pigs.

• Journal of Life Science
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• v.26 no.1
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• pp.101-108
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• 2016

The aim of this study was to evaluate the relationships between the expression of Heat shock protein70 (HSP70), Raf-1 and Bcl-2-associated athanogene-1 (BAG1) protein in diffuse type gastric carcinoma and examine association of HSP70, Raf-1 and BAG1 expression with various clinic-pathological factors and survival. Heat shock protein70 is induced in the cells in response to various stress conditions, including carcinogens. Overexpression of heat shock protein 70 has been observed in many types of cancer. The proto-oncoprotein Raf is pivotal for mitogen-activated protein kinase (MAPK) signaling, and its aberrant activation has been implicated in multiple human cancers. Overexpression of BAG1 protein has been documented in some type of human cancer. BAG1 has been reported to interact with protein involved with a variety of signal pathway, and regulation of cell differentiation, survival and apoptosis. These interaction partners include HSP70 and Raf-1. The percentage of tumors exhibiting HSP70 positivity was significantly in cases of positive lymph node metastasis (64.9%) compared to cases without lymph node metastasis (35.1%, p=0.007). HS70 expression was correlated with pathological N-stage (p=0.006). Expression of BAG1 was detected in the majority of diffuse type gastric carcinoma tissues (71.7%), especially in younger patients (80% vs 52.6%, p=0.035). Furthermore BAG1 expression was correlated with tumor size (p=0.020). Raf-1 expression was found to be significantly associated with tumor size (p=0.005). The result indicate that HSP70 was significantly correlated the progression of diffuse type gastric cancer. Expression of BAG1 and Raf-1 may be used as diagnostic markers for gastric carcinoma.

• Journal of Aquaculture
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• v.12 no.2
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• pp.91-100
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• 1999

The complete nucleotide sequence of olive flounder (Paralichthys olivaceus) hsp70-related rDNA was determined by RT- and RACE-PCR methods. A full-length of hsp70-related cDNA has an open reading frame of 1.95 kb encoding 650 amino acids with a calculated molecular weight of 71.1 kD. A corresponding hsp70-related protein contains a number of conserved elements including an ATP-binding domain, a nuclear localization signal and the carboxyl terminal motif, EEVD, which may have a role in chaperone function. Comparison of nucleotide and predicted amino acid sequence between olive flounder hsp70-related gene and hsp/hsc70 genes of other species revealed a high similarity with the cognate form of these genes. These results indicated that we recovered likely to be a olive flounder cognate hsc70 gene.

• IMMUNE NETWORK
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• v.4 no.1
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• pp.7-15
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• 2004

Background: The heat shock proteins (HSPs) play an important role in cellular protection mechanisms against physical or chemical stresses. In this study scFv antibodies specific for human HSP70.1 were isolated from a semi-synthetic human scFv library with the ultimate goal of developing anti-HSP70.1 intracellular antibody (intrabody) that may offer an attractive alternative to gene targeting to study the function of the protein in cells. Methods: A semi-synthetic human scFv display library ($5{\times}10^{8}$ size) was constructed using pCANTAB-5E vector and the selection of the library against bacterially expressed recombinant human HSP70.1 was attempted by panning. Results: Three positive clones specific for recombinant HSP70.1 were identified. All three clones used $V_{H}$ subgroup III. On the other hand, $V_{L}$ of two clones belonged to the kappa light chain subgroup I, but the other utilized $V_{k}$ subgroup IV Interestingly, these scFv molecules specifically reacted to the recombinant HSP70.1, yet failed to recognize native HSP70 induced in U937 human monocytic cells by heat treatment. Conclusion: Our results indicated that affinity selection of an scFv phage display library using recombinant antigens produced in E. coli might not guarantee the isolation of scFv antibody molecules specific for a native form of the antigen. Therefore, the source of target antigens needs to be chosen carefully in order to isolate biofunctional antibody molecules.

• Journal of Nutrition and Health
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• v.44 no.5
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• pp.378-383
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• 2011

This study examined the effect of supplementary selenium on leukocytes and heat shock protein (HSP) 70 expression in serum during half-body immersion. The subjects were male college tennis athletes. All subjects participated in two repeated experiments with a 1 week interval. During the 30 min intermittent half-body immersion, subjects were given 500 mL of water with or without selenium (100 ${\mu}g$). Blood samples were taken from the antecubital vein, and differential counts were made. Serum HSP70 protein was analyzed using a commercial ELISA kit. After half-body immersion, leukocytes and lymphocytes increased significantly but neutrophils decreased significantly in both trials (with or without selenium). Selenium supplementation, compared with placebo, decreased levels of leukocytes, neutrophils, and monocytes, but not lymphocytes, to the resting level or below 60 min after immersion. Only lymphocytes continued to increase in both trials during the recovery period. Serum HSP70 protein level did not change after immersion, but it decreased 60 min after immersion with the administration of selenium. In conclusion, supplementary selenium reduced the systemic immune response and serum HSP70 protein accumulation after half-body immersion.