• Korean Journal of Biological Psychiatry
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• v.14 no.4
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• pp.221-231
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• 2007

Recent researches have shown that important cellular-based autoprotective mechanisms are mediated by heat-shock proteins(HSPs), also called 'molecular chaperones'. HSPs as molecular chaperones are the primary cellular defense mechanism against damage to the proteome, initiating refolding of denatured proteins and regulating degradation after severe protein damage. HSPs also modulate multiple events within apoptotic pathways to help sustain cell survival following damaging stimuli. HSPs are induced by almost every type of stresses including physical and psychological stresses. Our nervous system in the brain are more vulnerable to stress and damage than any other tissues due to HSPs insufficiency. The normal function of HSPs is a key factor for endogenous stress adaptation of neural tissues. HSPs play an important role in the process of neurodevelopment, neurodegeneration, and neuroendocrine regulation. The altered function of HSPs would be associated with the development of several neuropsychiatric disorders. Therefore, an understanding of HSPs activities could help to improve autoprotective mechanism of our neural system. This paper will review the literature related to the significance of HSPs in neuropsychiatric field.

• Journal of The Korean Society of Grassland and Forage Science
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• v.18 no.4
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• pp.303-310
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• 1998

We studied expression patterns of thermotolerance gene (BcHSP17.6) in cabbages which was isolated from Chinese cabbage and we will attempt transformation of forage crops with the gene in order to increase thermotolerance of forage crops. Antiserum against a BcHSP17.6 protein was reacted with its antigen. With this antiserum, the accumulation of the 15- to 18-kD LMW HSPs under various heat shock (HS) conditions was quantified. The LMW HSPs began to be detectable at $35^{\circ}C$, and after 4 hours at $40^{\circ}C$ they were accumulated to a maximum level of 1.56 micrograms per 100 micrograms of total proteins in cabbage leaves and remained almost unchanged up to 24 hours after HS. Accumulation of the HSPs was reduced at temperatures higher than $40^{\circ}C$. We conclude that accumulation of these LMW HSPs are necessary for Chinese cabbages to survive at an otherwise lethal temperature.

• Korean Journal of Poultry Science
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• v.43 no.3
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• pp.177-189
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• 2016

This study was conducted to verify the relationships between the expression values of stress-related markers and their production performances in 25 strains of Korean domestic chicken breeds. For stress response markers, the amount of telomeric DNA; expression levels of heat shock protein (HSP)-70, $HSP-90{\alpha}$, and $HSP-90{\beta}$; and comet scores were analyzed. Production performances were measured by the survival rate, body weights, days at first egg laying, egg weight and hen housed egg production. The results showed that the production traits and values of stress-related markers showed significant differences between strains. In general, the stress response of pure bred chickens with heavy weights was relatively high, while that of hybrid chickens with light weights was relatively low. The correlation coefficients between telomere contents and body weights showed that there were weak negative relationships. However, the correlations of telomere content with the survival rate and egg production were weakly positive after 20 weeks old. The expression levels of HSP genes and DNA damage rate (comet scores) were positively correlated to body weight, but were negatively correlated to the survival rate and egg production. The results implied that increasing body weight was associated with increasing HSPs expression and the DNA damage rate was associated with decreasing telomere content. In addition, increasing HSPs expression and the DNA damage rate decreased the survival rate and egg production, but the relationships with the telomere content was the reverse. Correlations among the stress-related markers showed that there were significant correlation coefficients between all of the marker values. HSPs expression was negatively correlated to the telomere content, while it was positively correlated to the DNA damage rate. There was a highly negative correlation between the telomere content and DNA damage rate. In conclusion, increasing the HSP values and DNA damage rate can promote telomere reduction, which led to a decrease in disease resistance and robustness of the chicken. Thus, increasing the stress response was verified to adversely affect the laying performance and viability of chickens.

• Molecules and Cells
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• v.23 no.2
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• pp.123-131
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• 2007

Extracellular stresses induce heat shock response and render cells resistant to lethal stresses. Heat shock response involves induction of heat shock proteins (Hsps). Recently the roles of Hsps in neurodegenerative diseases and cancer are attracting increasing attention and have accelerated the study of heat shock response mechanism. This review focuses on the stress sensing steps, molecules involved in Hsps production, diseases related to Hsp malfunctions, and the potential of proteomics as a tool for understanding the complex signaling pathways relevant to these events.

• The Plant Pathology Journal
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• v.31 no.4
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• pp.323-333
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• 2015

As sessile organisms, plants are exposed to persistently changing stresses and have to be able to interpret and respond to them. The stresses, drought, salinity, chemicals, cold and hot temperatures, and various pathogen attacks have interconnected effects on plants, resulting in the disruption of protein homeostasis. Maintenance of proteins in their functional native conformations and preventing aggregation of non-native proteins are important for cell survival under stress. Heat shock proteins (HSPs) functioning as molecular chaperones are the key components responsible for protein folding, assembly, translocation, and degradation under stress conditions and in many normal cellular processes. Plants respond to pathogen invasion using two different innate immune responses mediated by pattern recognition receptors (PRRs) or resistance (R) proteins. HSPs play an indispensable role as molecular chaperones in the quality control of plasma membrane-resident PRRs and intracellular R proteins against potential invaders. Here, we specifically discuss the functional involvement of cytosolic and endoplasmic reticulum (ER) HSPs/chaperones in plant immunity to obtain an integrated understanding of the immune responses in plant cells.

• Korean Journal of Poultry Science
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• v.43 no.2
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• pp.77-88
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• 2016

To establish a new synthetic Korean meat chicken breed, we tested $5{\times}5$ diallel cross mating experiment with domestic chicken breeds. Comparing stress responses among diallel crossed chicken breeds, we analyzed telomere length, DNA damage and expressions of heat shock protein genes (HSPs) as the markers of the stress response. The telomere length was measured by quantitative fluorescence in situ hybridization on the nuclei of lymphocytes. The expression levels of HSP-70, $HSP-90{\alpha}$ and $HSP-90{\beta}$ genes were analyzed by quantitative real-time polymerase chain reaction in lymphocytes. The DNA damage rate of lymphocytes was quantified by the comet assay known as the single cell gel electrophoresis. In results, there were significant differences in the values of the stress markers such as telomere length, HSPs and DNA damage rate, and also were significant differences in viabilities and body weights among the $5{\times}5$ diallel crossed chicken breeds. The telomere shortening rate, expression values of HSPs and DNA damage rate were significant low in W and Y crossed chickens compare to the others, but GG pure breed showed the highest values in the 25 crossed chickens. Estimating correlation coefficient, the survival rate positively correlated to telomere length, but negatively correlated to the expression levels of HSP-70, $HSP-90{\alpha}$, $HSP-90{\beta}$ genes and to the value of % DNA in tail as DNA damage rate. The expression levels of HSP-70, $HSP-90{\alpha}$ and $HSP-90{\beta}$ genes of dead chickens had significantly higher than those of survival chickens. According to the results on the stress marker analysis, it would be considered that the crossed breeds had more stress resistant than the pure breeds, and the crossed chickens with a light strain such as W or Y were relatively resistant to stress, but the crossed chickens with a heavy strain such as G, H, F were susceptible to stress.

• Journal of fish pathology
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• v.12 no.2
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• pp.89-99
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• 1999

New sixteen heat shock proteins (Hsps) and ten ethanol shock proteins were appeared on the analysis with SDS-PAGE when cultivation temperature for the Vibrio vulnifrcus ATCC 27562 strain was shifted-up to $42^{\circ}C$ from $30^{\circ}C$ for 20 mins and treated with of 6% ethanol for 10 mins, respectively. Even the induction of thermotolerance in V. vulnificus was coincided with the induction of Hsps if the pre-shock was adjusted to thermal temperature. Outer membrane proteins (OMPs) that were purified from the membrane of cells after heat shock showed more immunodominant pattern to the immunized rabbit anti-V. vulnificus O serum in enzyme-linked immunosorbent assay (ELISA). On the western immunoblot analysis it was confirmed that both 62 kDa IMP and 69 kDa OMP in the Hsps and 48 kDa IMP a major OMP in the ethanol shock proteins were reacted with rabbit anti-V. vulnificus O sera. Agglutination titer of the heat shocked V. vulnificus with rabbit anti-V. vulnificus O serum was higher than that of the untreated bacteria.

• Journal of Microbiology and Biotechnology
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• v.19 no.12
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• pp.1628-1634
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• 2009

Small heat shock proteins (sHSPs) function as molecular chaperones that protect cells against environmental stresses. In the present study, the genes of hsp17.6 and hsp17.7, cytosolic class I sHSPs, were cloned from a tropical plant, Ageratina adenophorum. Their C-terminal domains were highly conserved with those of sHSPs from other plants, indicating the importance of the C-terminal domains for the structure and activity of sHSPs. The recombinant HSP17.6 and HSP17.7 were applied to determine their chaperone function. In vitro, HSP17.6 and HSP17.7 actively participated in the refolding of the model substrate citrate synthase (CS) and effectively prevented the thermal aggregation of CS at $45^{\circ}C$ and the irreversible inactivation of CS at $38^{\circ}C$ at stoichiometric levels. The prior presence of HSP17.7 was assumed to suppress the thermal aggregation of the model substrate CS. Therefore, this report confirms the chaperone activity of HSP17.6 and HSP17.7 and their potential as a protectant for active proteins.

• Korean Journal of Poultry Science
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• v.47 no.4
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• pp.219-227
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• 2020

As the earth's average temperature rises, crop and livestock productions are at risk. Chickens are sensitive to heat stress, and increased temperatures may have adverse effects on their production performance and animal welfare. Reliable stress measurements are crucial for heat stress adaptation. Therefore, various measurement methods and biomarkers are used to evaluate poultry stress levels. Heat shock proteins (HSPs) are heat sensitive biological markers that are highly expressed under stress, thereby acting as a cellular thermometer. HSPs also have chaperone activity, which protects cells from heat stress. This review details the role of HSP70 as a molecular chaperone and biomarker for heat stress, which is important for breeding climate-adaptable, thermo-tolerant poultry.

• Fisheries and Aquatic Sciences
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• v.2 no.1
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• pp.85-92
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• 1999

We examined the expression patterns of heat shock proteins in primary cultured hepatocytes from flounder (Paralichthys olivaceus) exposed to heat shock. The expression of hsp90, hsp70, hsp40, hsp30, and hsp27 was induced and major polypeptides were hsp70, hsp30 and hsp27. Northern blot analysis showed that expression of hsp70 was inhibited by transcriptional inhibitor actinomycin D, suggesting that expression of hsp70 gene is regulated at the transcriptional level. Prolonged exposure of cells to an elevated incubation temperature $(30^{\circ}C)$ induced the transient synthesis of hsp90, hsp70, hsp40, and hsp30 whereas maintenance of cells at a slightly higher incubation temperature $(32^{\circ}C)$ induced the continuous syntheses of these hsps. When cells were incubated at a higher temperatures $(35^{\circ}C\;or\;37^{\circ}C)$, the synthesis of hsps was almost similar to that of hsps in cells exposed to 32't except for the induction of hsp27 synthesis. These results that temperature and incubation time for optimum expression of each hsp during prolonged heat shock are different.