• Korean Journal of Environmental Agriculture
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• v.27 no.4
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• pp.456-459
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• 2008

Quality of rice grain changes during dry storage with internal physiological changes and external injury by organism. Storage rice changes by condition with respiration via variable temperature, hydrolysis enzyme reaction, lipid peroxidation occurs with change of palatability. During dry storage, physiological change with protein variation pattern was examined by image analysis on proteomic technology. Analysis revealed that protein activity had no change store at room temperature and store at $40^{\circ}C$, but decreased store at $60^{\circ}C$. Analysis of variable hydrophobic protein pattern revealed that protein activity of beta-tubulin, protein disulfide isomerase, vacuolar ATPase b subunit, globulin was not significantly decreased all dry and store condition. However, heat shock protein 70, and glutathione transferase was significantly decreased when rice dried at $60^{\circ}C$ compared with room temperature and $40^{\circ}C$ dry condition.

• Korean Journal of Microbiology
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• v.38 no.2
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• pp.67-73
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• 2002

The cellular responses of soil-borne bacterium, Pseudomonas sp. HK-6 to explosive 2,4,6-trinitrotoluene (TNT) were examined. Two stress shock proteins (SSPs), approximately 70-kDa DnaK and a 60-kDa GroEL were found in HK-6 cells in response to TNT. Analyses of SDS-PAGE and Western blot using anti-DnaK and GroEL revealed that SSPs were induced in HK-6 cells exposed to 0.5 M of TNT far 6-12 hrs. The maximum induction of proteins was achieved at 8-hr incubation point after HK-6 cells'exposure to TNT. Similar SSPs were found to be induced in HK-6 cells by heat shock (shift of temperature, from $30^{\circ}C$ to $42^{\circ}C$) or cold shock (shift of temperature,$30^{\circ}C$ to $4^{\circ}C$).2D-PAGE of soluble protein tractions from the culture of Pseudomonas sp. HX-6 exposed to TNT demonstrated that approximately 450 spots were observed on the silver stained gels ranging from pH 3 to pH 10. Among them, 12 spots significantly induced and expressed in response to TNT were selected and analyzed. Approximately 60-kDa protein, which was assumed highly expressed on the gel, was used for amino acid sequencing. N-terminal microsequencing with in-gel digestion showed that N-terminal sequence of the TNT-induced protein, <$^1XXAKDVKFGDSARKKML^17$, shared extensive similarity with $^1XXAKDVKFGDSARKKML^17$, N-terminal sequence of (P48216) GroEL of Pseudomonas putida.

• Weed & Turfgrass Science
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• v.4 no.3
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• pp.256-261
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• 2015

Trampling stress in turfgrass fields caused by traffics often occurs in zoysiagrass (Zoysia japonica) fields including golf course. In order to know the influences of trampling stress on the growth and development of turfgrass, leaf and root growth, chlorophyll fluorescence, chlorophyll content and 2-DE protein analysis were conducted in the turfgrass plants subjected to various levels of trampling stress from 0 to $9,420J\;day^{-1}$ day. Shoot growth was more highly inhibited by trampling stress than root growth. Although root growth was affected by trampling with weak intensity, the highest root length was observed in the turfgrass treated with weak trampling ($1,570J\;day^{-1}$). Chlorophyll fluorescence (Fv $Fm^{-1}$) was drastically lowered by trampling stress with moderate intensity. Leaf number showed similar tendency with leaf greenness. The number was decreased as the trampling intensity was increased. Shoot dry weight was decreased showing a similar tendency with the result of shoot length. The specific protein expressions under weak trampling were related to the functions of stress amelioration. Heat shock 70 kDa protein 10 and oxygen-evolving enhancer protein 1 were the proteins increased positively under trampling stress.

• BMB Reports
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• v.55 no.10
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• pp.488-493
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• 2022

The specific pair of heat shock protein 70 (Hsp70) and Hsp40 constitutes an essential molecular chaperone system involved in numerous cellular processes, including the proper folding/refolding and transport of proteins. Hsp40 family members are characterized by the presence of a conserved J-domain (JD) that functions as a co-chaperone of Hsp70. Tumorous imaginal disc 1 (Tid1) is a tumor suppressor protein belonging to the DNAJA3 subfamily of Hsp40 and functions as a co-chaperone of the mitochondrial Hsp70, mortalin. In this work, we performed nuclear magnetic resonance spectroscopy to determine the solution structure of JD and its interaction with the glycine/phenylalanine-rich region (GF-motif) of human Tid1. Notably, Tid1-JD, whose conformation was consistent with that of the DNAJB1 JD, appeared to stably interact with its subsequent GF-motif region. Collectively with our sequence analysis, the present results demonstrate that the functional and regulatory mode of Tid1 resembles that of the DNAJB1 subfamily members rather than DNAJA1 or DNAJA2 subfamily proteins. Therefore, it is suggested that an allosteric interaction between mortalin and Tid1 is involved in the mitochondrial Hsp70/Hsp40 chaperone system.

• Molecules and Cells
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• v.46 no.6
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• pp.374-386
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• 2023

Thermal stress induces dynamic changes in nuclear proteins and relevant physiology as a part of the heat shock response (HSR). However, how the nuclear HSR is fine-tuned for cellular homeostasis remains elusive. Here, we show that mitochondrial activity plays an important role in nuclear proteostasis and genome stability through two distinct HSR pathways. Mitochondrial ribosomal protein (MRP) depletion enhanced the nucleolar granule formation of HSP70 and ubiquitin during HSR while facilitating the recovery of damaged nuclear proteins and impaired nucleocytoplasmic transport. Treatment of the mitochondrial proton gradient uncoupler masked MRP-depletion effects, implicating oxidative phosphorylation in these nuclear HSRs. On the other hand, MRP depletion and a reactive oxygen species (ROS) scavenger non-additively decreased mitochondrial ROS generation during HSR, thereby protecting the nuclear genome from DNA damage. These results suggest that suboptimal mitochondrial activity sustains nuclear homeostasis under cellular stress, providing plausible evidence for optimal endosymbiotic evolution via mitochondria-to-nuclear communication.

• Journal of the Korean Society of Physical Medicine
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• v.8 no.1
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• pp.111-116
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• 2013

연구목적: 본 연구는 흰쥐를 대상으로 정강뼈의 관절연골에 적용한 맥동전자장과 맥동초음파가 HSP70(Heat shock protein 70)의 발현을 통한 연골 형성에 미치는 영향을 알아보고자 실시하였다. 연구방법: 36마리의 200~250g의 Sprague-Dawley 흰쥐를 대조군, 맥동전자장 적용군, 맥동초음파 적용군으로 각 집단별로 12마리씩 무작위 배정하여 실험을 진행하였다. 맥동전자장은 27.12 MHz의 주파수, 5가우스의 강도, 450 W의 출력으로 10분간 적용하였고, 맥동초음파는 20%의 맥동비, 1MHz의 주파수, $1.5W/cm^2$의 강도로 10분간 적용하였다. 연구결과: 맥동전자장 적용군과 맥동초음파 적용군의 관절연골 조직에서 유의한 수준의 HSP70 발현량을 나타냈다. 또한 맥동전자장 적용군과 맥동초음파 적용군에서는 Akt, Erk1, CREB의 높은 활성도를 나타내었고, 맥동초음파 적용군에 비해서 맥동전자장 적용군의 더 높은 수준의 활성도를 보였다. 결론: 맥동전자장과 맥동초음파는 HSP70의 과발현을 유발하고, 이를 통해 연골형성을 증가시키는 것으로 나타나, 향후 관절연골의 손상에 대한 임상적 적용을 위한 추가적인 연구가 진행되어야 할 것으로 생각된다.

• Journal of Aquaculture
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• v.19 no.4
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• pp.315-322
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• 2006

The objective of the present study was to investigate the expression of heat shock protein 90 (HSP90) and 70 (HSP70) mRNA as cellular stress responses, the levels of plasma cortisol with glucose as neuro-endocrine stress responses during water temperature rising in freshwater adapted black porgy, Acanthopagrus schlegeli. A cDNA fragment of 891 (HSP90) and 465 (HSP70) bp was cloned from black porgy testis by Reverse transcription-polymerase chain reaction (RT-PCR) with primers designed from the conserved regions of other teleost. The PCR product of HSP90 showed very high homology to red seabream (99%), rainbow trout (95%), Atlantic salmon (94%), zebrafish (94%) HSP90, HSP70 of black porgy was also highly similar to those of rainbow trout (96%), silver seabream (95%), zebrafish (95%) HSP70. Water temperature rising ($20{\sim}30^{\circ}C$) induced elevation of HSP90 mRNA in black porgy gonad, liver, brain, intestine and kidney, whereas it resulted in an induction of the HSP70 mRNA expression in gonad only. Plasma cortisol levels increased significantly at $30^{\circ}C$ in the fish compared to those at $20^{\circ}C$. Glucose levels of the fish showed a tendency of co-increase with cortisol during water temperature rising. These results suggest that increased HSP90 mRNA in liver with plasma cortisol following heat shock may be related to increasing glucose for homeostasis in this species.

• Journal of Animal Reproduction and Biotechnology
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• v.34 no.3
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• pp.173-182
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• 2019

This study was performed to evaluate the effect of heat stress on the status of physiological responses, blood parameter, serum T3 and cortisol, and heat shock proteins (HSP 27, 70, and 90) of Hanwoo cattle. Six Hanwoo steers (242.8 ± 7.2 kg of BW) were housed in the climate-controlled respiration chambers. The experiment consisted of 7 days (control; 0 day) at thermoneutral (air temperature (Ta) of 15℃ and relative humidity (RH) of 60%; temperature-humidity index (THI) = 64), and by 3 and 6 days (treatment groups) at heat stress (Ta of 35℃ and RH of 60%; THI = 87). Body temperature of each parts (frank, rump, perineum and foot) and rectal temperature elevated in heat stress groups (3 days and 6 days) than the control group (0 day). Respiration rates increased in 3 days and 6 days (88.5 ± 0.96 bpm and 86.3 ± 0.63 bpm, respectively) from 0 days (39.5 ± 0.65 bpm). Feed intake significantly decreased in heat stress groups (3 days and 6 days, 3.7 ± 0.14 kg and 4.0 ± 0.15 kg, respectively) than the control group (0 day, 5.0 ± 0.00 kg). In addition, final BW significantly decreased in heat stress groups (3 days and 6 days, 211.8 ± 4.75 kg and 215.5 ± 3.50 kg, respectively) than the control group (0 day, 240.0 ± 25.00 kg). However, heat stress has no significant effect on blood parameter, serum T3 and cortisol. Nevertheless, heat stress increased HSPs mRNA expression in liver tissue, and serum concentration of HSPs. Despite Hanwoo cattle may have high adaptive ability to heat stress, our results suggested that heat stress directly effect on body temperature and respiration rate as well as serum and tissue HSPs. Therefore, we are recommended that HSPs could be the most appropriate indicators of Hanwoo cattle response to heat stress.

• Journal of Animal Science and Technology
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• v.57 no.12
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• pp.44.1-44.9
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• 2015

Background: Heat shock proteins play an important role in protection from stress stimuli and metabolic insults in almost all organisms. Methods: In this study, computational tools were used to deeply analyse the physicochemical characteristics and, using homology modelling, reliably predict the tertiary structure of the blunt snout bream (Ma-) Hsp70 and Hsc70 proteins. Derived three-dimensional models were then used to predict the function of the proteins. Results: Previously published predictions regarding the protein length, molecular weight, theoretical isoelectric point and total number of positive and negative residues were corroborated. Among the new findings are: the extinction coefficient (33725/33350 and 35090/34840 - Ma-Hsp70/ Ma-Hsc70, respectively), instability index (33.68/35.56 - both stable), aliphatic index (83.44/80.23 - both very stable), half-life estimates (both relatively stable), grand average of hydropathicity (-0.431/-0.473 - both hydrophilic) and amino acid composition (alanine-lysine-glycine/glycine-lysine-aspartic acid were the most abundant, no disulphide bonds, the N-terminal of both proteins was methionine). Homology modelling was performed by SWISS-MODEL program and the proposed model was evaluated as highly reliable based on PROCHECK's Ramachandran plot, ERRAT, PROVE, Verify 3D, ProQ and ProSA analyses. Conclusions: The research revealed a high structural similarity to Hsp70 and Hsc70 proteins from several taxonomically distant animal species, corroborating a remarkably high level of evolutionary conservation among the members of this protein family. Functional annotation based on structural similarity provides a reliable additional indirect evidence for a high level of functional conservation of these two genes/proteins in blunt snout bream, but it is not sensitive enough to functionally distinguish the two isoforms.

• Journal of the Korean Association of Oral and Maxillofacial Surgeons
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• v.36 no.5
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• pp.346-352
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• 2010

Introduction: Heat shock protein70 (HSP70) is a highly conserved family of proteins produced after a variety of stresses. Many studies reported that the overexpression of HSP70 can improve the prognosis of the patients with sepsis through a reduction of the nitric oxide concentration. However, these results only revealed the effect of HSP70 and nitric oxide. No studies have examined the relationship between HSP70 and nitric oxide. The aim of this study was to evaluate the effect of the overexpression of HSP70 on the expression of inducible nitric oxide synthase and the nitric oxide concentration. In addition, the mechanism of the relationship of HSP70 and inducible nitric oxide synthase (iNOS) in sepsis was examined. Materials and Methods: The experiments were performed on male sprague-dawley rats. Sepsis was induced by a cecal ligation and puncture (CLP). Glutamine (GLN) or saline was administered 1 hour after the initiation of sepsis. Serum and lung tissues were acquired from the rats 12 hours or 24 hours after the initiation of sepsis. The nitric oxide concentration, the expression of HSP70 in lung, and the gene expression of iNOS in lung were analyzed. The three groups, sham operation, CLP and CLP+GLN, were compared. Results: Compared to the other groups, in CLP+GLN, GLN administered after the initiation of sepsis enhanced the expression of HSP70 in the lung at 12 hours ($47.19{\pm}10.04$ vs. $33.22{\pm}8.28$, P=0.025) and 24 hours ($47.06{\pm}10.60$ vs. $31.90{\pm}4.83$, P=0.004). In CLP+GLN, GLN attenuated the expression of iNOS messenger RNA (mRNA) in the lung at 12 hours ($5,513.73{\pm}1,051.60$ vs. $4,167.17{\pm}951.59$, P=0.025) and 24 hours ($18,740.27{\pm}8,241.20$ vs. $9,437.65{\pm}2,521.07$, P=0.016), and reduced the concentration of nitric oxide in the serum at 12 hours ($0.86{\pm}0.48$ vs. $3.82{\pm}2.53$, P=0.016) and 24 hours ($0.39{\pm}0.25$ vs. $1.85{\pm}1.70$, P=0.025). Conclusion: The overexpression of HSP70 induced by the administration of GLN in sepsis attenuates the expression of the iNOS gene but reduces the nitric oxide concentration.