• Journal of Periodontal and Implant Science
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• 제33권2호
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• pp.179-191
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• 2003

Since periodontal infections are suggested as risk factors for the development of cardiovascular diseases, the present study was performed to evaluate the T cell immune responses specific to Pophylomonas gingivalis(P. gingivalis) heat shock protein(hsp) 60 and T-cell and B-cell epitope specificities for P. gingivalis hsp60 in atherosclerosis. Anti-P, gingivalis IgG antibody titers were elevated in all patients. We could establish P. gingivalis hsp-specific T cell lines from the atheroma lesions, a mixture of $CD4^+$ and $CD8^+$ cells producing the cytokines characteristic of both Th1 and Th2 subsets. of 108 overlapping synthetic peptides spanning whole P. gingivalis hsp60 molecule, ten peptides with common epitopes specificities for both T-cell and B-cell were identified. it was concluded that P. gingivalis hsp60 might K involved in the immunoregulatory process of atherosclerotic diseases with epitope specificities.

• 한국수산과학회지
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• 제51권2호
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• pp.163-169
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• 2018

This study examined the expression of heat shock protein 70 (Hsp70) in red seabream Pagrus major infected by the, acanthocephalan parasites Longicollum pagrosomi. We cloned the full-length Hsp70 cDNA from the liver of the red seabream. The full-length cDNA had a 1,950 bp open reading frame (ORF) that encoded a protein of 650 amino acids. The deduced amino acid sequence of Hsp70 contained all of the conserved Hsp70 family signature sequences and an adenosine triphosphate (ATP)/guanosine triphosphate (GTP) binding motif, including the EEVD (consensus sequence that terminates in Hsp70 family) consensus sequence. The expression of Hsp70 mRNA was upregulated int the fish head-kidney and liver, as determined by quantitative real-time PCR. We quantified the Hsp70 mRNA expression in normal red seabream and fish infected fish by L. pagrosomi. The expression of Hsp70 mRNA was significantly higher in the infected red seabream. These results suggest that Hsp70 play a role of protection against stress and inflammation caused by the parasite and may help maintain homeostasis.

• Molecules and Cells
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• 제39권2호
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• pp.163-168
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• 2016

Caffeine has both positive and negative effects on physiological functions in a dose-dependent manner. C. elegans has been used as an animal model to investigate the effects of caffeine on development. Caffeine treatment at a high dose (30 mM) showed detrimental effects and caused early larval arrest. We performed a comparative proteomic analysis to investigate the mode of action of high-dose caffeine treatment in C. elegans and found that the stress response proteins, heat shock protein (HSP)-4 (endoplasmic reticulum [ER] chaperone), HSP-6 (mitochondrial chaperone), and HSP-16 (cytosolic chaperone), were induced and their expression was regulated at the transcriptional level. These findings suggest that high-dose caffeine intake causes a strong stress response and activates all three stress-response pathways in the worms, including the ER-, mitochondrial-, and cytosolic pathways. RNA interference of each hsp gene or in triple combination retarded growth. In addition, caffeine treatment stimulated a food-avoidance behavior (aversion phenotype), which was enhanced by RNAi depletion of the hsp-4 gene. Therefore, up-regulation of hsp genes after caffeine treatment appeared to be the major responses to alleviate stress and protect against developmental arrest.

• Journal of Microbiology
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• 제34권2호
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• pp.158-165
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• 1996

The signal transduction pathways through the RAS gene product and adenyl cyclease play a critical role in regulation of the cell cycle in yeast, Saccharomyces cerevisiae. We examined the genetic relationship between the spt3 gene and ras/cAMP pathway. A mutation in the SPT3 gene suppressed cell cycle arrest at the G1 phase caused by either an inactivation of the RAS or CYR1 gene which encodes a yeast homologue of human ras proto-oncogene or adenyl cyclase, respectively. The phenotypes such as sporulation and heat shock resistancy, that resulted from a partial inactivation of the RAS or CYR1 genes, were also suppressed by the spt3 mutation. Expression of the SSA1 gene encoding one of th heat shock proteins (Hsp70) can be induced by heat shock or nitrogen starvation. Expression of this gene is derepressed in cry1-2 and spt3 mutants. The bcy 1 mutation repressed by the bcy1 mutation, but not in spt3 mutants. These results suggest that the SPT gene is involved in expression of genes that are affected by the RAS/cAMP pathway.

• 한국동물위생학회지
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• 제29권4호
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• pp.469-482
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• 2006

The term 'heat shock protein (Hsps)' was derived from the fact that these proteins were initially discovered to be induced by hyperthermic conditions. In response to a range of stressful stimuli, including hyperthermia, immobilization, UV radiation, amino acid analogues, arsenite, various chemicals, and drugs the mammalian brain demonstrates a rapid and intense induction of the heat shock protein. Moreover, Hsps were expressed on the various pathological conditions including trauma, focal or global ischemia, hypoxia, infarction, infections, starvation, and anoxia. Especially, Hsp25 has a protective activity, facilitated by the ability of the protein to decrease the intracellular levels of reactive oxygen species (ROS) as well as its chaperone activity, which favors the degradation of oxidized proteins. Recently, it has clearly demonstrated that Hsp25 is constitutively expressed in the adult mouse cerebellum by parasagittal bands of purkinje cells in three distinct regions, the central zone (lobule VI-VII) and nodular zone (lobule IX-X), and paraflocculus. The Mongolian gerbil has been introduced into stroke study model because of its unique brain vasculature. There are no significant connections between the basilarvertebral system and the carotid system. This anatomy feature renders the mongolian gerbil susceptible to forebrain ischemia-induced seizure. The present study is designed to examine the pattern of Hsp25 expression in the cerebellum of this animal in comparison with that in mouse.

• BMB Reports
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• 제40권1호
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• pp.107-112
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• 2007

To study the functioning of HSP70 in Escherichia coli, we selected NtHSP70-2 (AY372070) from among three genomic clones isolated in Nicotiana tabacum. Recombinant NtHSP70-2, containing a hexahistidine tag at the amino-terminus, was constructed, expressed in E. coli, and purified by $Ni^{2+}$ affinity chromatography and Q Sepharose Fast Flow anion exchange chromatography. The expressed fusion protein, $H_6NtHSP70$-2 (hexahistidine-tagged Nicotiana tabacum heat shock protein 70-2), maintained the stability of E. coli proteins up to 90$^{\circ}C$. Measuring the light scattering of luciferase (luc) revealed that NtHSP70-2 prevents the aggregation of luc without ATP during high-temperature stress. In a functional bioassay (1 h at 50$^{\circ}C$) for recombinant $H_6NtHSP70$-2, E. coli cells overexpressing $H_6NtHSP70$-2 survived about seven times longer than those lacking $H_6NtHSP70$-2. After 2 h at 50$^{\circ}C$, only the E. coli overexpressing $H_6NtHSP70$-2 survived under such conditions. Our NtHSP70-2 bioassays, as well as in vitro studies, strongly suggest that HSP70 confers thermo-tolerance to E. coli.

• Food Science and Biotechnology
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• 제18권3호
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• pp.788-792
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• 2009

Gamma $({\gamma})-irradiation$ can be used to control pathogens such as Vibrio vulnificus in seafood. The effects of irradiation on microbial cell populations (%) have been studied in order to develop detection methods for irradiated foods. The method used in this study was ethidium bromide monoazide (EMA) real-time polymerase chain reaction (PCR), using V. vulnificus specific primer, EMA, and $SYBR^{(R)}$ Green to discriminate between ${\gamma}-irradiated$ and non-irradiated cells. Confocal microscope examination showed that ${\gamma}-irradiation$ damaged portions of the cell membrane, allowing EMA to penetrate cells of irradidated V. vulnificus. ${\gamma}-Irradiation$ at 1.08 KGy resulted in log reduction ($-1.15{\pm}0.13$ log reduction) in genomic targets derived from EMA real-time PCR. The combination cold/heat shock resulted in the highest ($-1.74{\pm}0.1$ log reduction) discrimination of dead irradiated V. vulnificus by EMA real-time PCR.

• Journal of Photoscience
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• 제9권3호
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• pp.41-43
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• 2002

PDT-mediated cyototoxicity basically depends on the penetrated light-dose into the tumor tissue. This limits the efficiency of PDT to the superficial tumor region typically less than 1 cm. The localized photochemical generation of reactive oxygen species, including singlet oxygen is known to increase expression of assortment of early response genes including heat shock protein. In order to increase PDT cytotoxicity in the treatment of solid tumor, it is desirable to combine PDT with other therapeutic effects. In this preliminary study we evaluated enhanced cytotoxicity from the PDT-mediated expression of thymidine kinase in a transfected tumor cell line. Two types of photo sensitizers, a hematoporphyrin derivative(Photogem, Russia) and aluminium sulphonated phthalocyanine(Photosense, Russia) were used to evaluate the overexpression of hsp-70 in PDT-treated cell. Transient increase of hsp-70 was observed at 6-8 hrs later following irradiation in the photosense-treated cell whereas it was not observed in Photogem-treated cell. In the presence of ganciclovia, transfected cell showed a 17％ increase in the cytotoxicity compared to the PDT only cell.

• Animal Bioscience
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• 제34권4호
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• pp.724-733
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• 2021

Objective: The objectives of this study were to investigate the direct antioxidative effect of 90 Kda heat shock protein (Hsp90) obtained from duck muscle. Methods: The interaction of Hsp90 with phospholipids and oxidized phospholipids was studied with surface plasmon resonance (SPR), and their further oxidation in the presence of Hsp90 was evaluated with thiobarbituric acid reactive substances (TBARS) assay. The scavenging effect on the 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid (ABTS) was measured, and the electron paramagnetic resonance (EPR) spectroscopy in combination with 5-tert-Butoxycarbonyl-5-methyl-1-pyrroline-N-oxide and 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) was utilized to determine the abilities of Hsp90 in scavenging hydroxyl and PTIO radicals. Results: SPR showed Hsp90 could bind with both phospholipids and oxidized phospholipids, and prevent their further oxidation by the TBARS assay. The DPPH and ABTS scavenging activity increased with Hsp90 concentration, and could reach 27% and 20% respectively at the protein concentration of 50 μM. The EPR spectra demonstrated Hsp90 could directly scavenge ·OH and PTIO· radicals. Conclusion: This suggests that Hsp90, a natural antioxidant in meat, may play an important role in cellular defense against oxidative stress, and may have potential use in meat products.

• Parasites, Hosts and Diseases
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• 제59권4호
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• pp.409-413
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• 2021

In this study, we have collected and screened a total of 268 stool samples from diarrheal patients admitted to an Infectious disease hospital in Kolkata for the presence of Cryptosporidium spp. The initial diagnosis was carried out by microscopy followed by genus specific polymerase chain reaction assays based on 70 kDa heat shock proteins (HSP70). DNA sequencing of the amplified locus has been employed for determination of genetic diversity of the local isolates. Out of 268 collected samples, 12 (4.48%) were positive for Cryptosporidium spp. Sequences analysis of 70 kDa heat shock proteins locus in 12 Cryptosporidium local isolates revealed that 2.24% and 1.86% of samples were showing 99% to 100% identity with C. parvum and C. hominis. Along with the other 2 major species one recently described globally distributed pathogenic species Cryptosporidium viatorum has been identified. The HSP70 locus sequence of the isolate showed 100% similarity with a previously described isolate of C. viatorum (Accession No. JX978274.1, JX978273.1, and JN846706.1) present in GenBank.