• Proceedings of the Korean Society of Life Science Conference
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• 2001.09a
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• pp.79-80
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• 2001

• Journal of Animal Reproduction and Biotechnology
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• v.34 no.3
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• pp.240-246
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• 2019

The aim of this study was to investigate effect of heat stress on expression levels of plasminogen activators (PAs) related mRNAs and proteins, and changes of PAs activity in porcine endometrial explants. The endometrial explants (200 ± 50 mg) were isolated from middle part of uterine horn at follicular phase (Day 19-21) and were pre-incubated in serum-free culture medium at 38.5℃ in 5% CO₂ for 18 h. Then, the tissues were transferred into fresh medium and were cultured at different temperature (38.5, 39.5, 40.5 or 41.5℃) for 24 h. The expression level of urokinase-type PA (uPA), type-1 PA inhibitor (PAI-1), type-2 PAI (PAI-2), and heat shock protein-90 (HSP-90) mRNA were analysis by reverse-transcription PCR and proteins were measured by western blotting. The supernatant were used for measurement of PAs activity. In results, mRNA and protein levels of HSP-90 was higher in 41.5℃ treatment groups than other treatment groups (p < 0.05). The expression of uPA, PAI-1, and PAI-2 mRNA were slightly increased by heat stress, however, there were no significant difference. Heat stress condition suppressed expression of active uPA and PAI-2 proteins (p < 0.05), whereas PAI-1 protein was increased (p < 0.01). Although PAI-1 protein was increased and active uPA was decreased, PAs activity was greatly enhanced by exposure of heat stress (p < 0.05). These results suggest that heat stress condition could change intrauterine microenvironment through regulation of PAs activity and other factors regarding with activation of PAs might be regulate by heat stress. Therefore, more studies regarding with regulatory mechanism of PAs activation are needed.

• Genomics & Informatics
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• v.7 no.1
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• pp.26-31
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• 2009

Heat shock proteins are a class of molecular chaperones that can be found in nearly all organisms from Bacteria, Archaea and Eukarya domains. Heat shock proteins experience increased transcription during periods of heat induced osmotic stress and are involved in protein disaggregation and refolding as part of a cell's danger signaling cascade. Heat shock protein, Hsp20 is a small molecular chaperone that is approximately 20kDa in weight and is hypothesized to prevent aggregation and denaturation. Hsp20 can be found in several strains of Proteobacteria, which comprises the largest phyla of the Bacteria domain and also contains several medically significant bacterial strains. Genomic analyses were performed to determine a common evolutionary pattern among Hsp20 sequences in Proteobacteria. It was found that Hsp20 shared a common ancestor within and among the five subclasses of Proteobacteria. This is readily apparent from the amount of sequence similarities within and between Hsp20 protein sequences as well as phylogenetic analysis of sequences from proteobacterial and non-proteobacterial species.

• Development and Reproduction
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• v.13 no.3
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• pp.199-205
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• 2009

HSP70 has widely been induced in in vivo hyperthermia conditions in various organisms to study gene regulation and recently neuroprotectve roles of the induced gene expression under varying conditions. We investigated different responses among various tissues in zebrafish under heat shock to evaluate whether spatial and temporal expression pattern of zebrafish (z) hsp70 in transcriptional and translational level under heat shock stress in different brain regions. Heat shock groups were given for 1 h at $37^{\circ}C$ after recovery by transferring the treated animals back to $28^{\circ}C$ for 1, 2 and 24 h for recovery, respectively. Control (CTRL) group was kept at $28^{\circ}C$. At the end of treatments, five animals were collected and used for isolation of total RNAs and peptides from the corresponding tissues. Expression of zhsp70 mRNA showed different patterns in recovery periods in the tissues including the brain, eye, intestines, muscles, heart and testis by RT-PCR. Unlike the RT-PCR analysis, Northern blot analysis demonstrated nearly 30-fold increase in zhsp70 at 1 h heat shock, suggesting that RT-PCR may not be appropriate in unmasking regulation of the time-dependent zhsp70 expression. In the experiment involving different brain regions, the cerebellum showed gradual activation at 1 h to R1h and decreases in R2h and R24h, while the medulla oblongata and optic tectum showed gradual increase at R1h and decrease at R24h, indicating that different brain tissues respond specifically to heat shock in inducing zhsp70 and recovering from the heat shock status. Western blot analysis also demonstrated that the intracellular levels of zHSP70 in three different brain regions including the cerebellum, medulla oblongata and optic tectum are differently induced and recovered to normal state. These results clearly demonstrate that different regions of the body and the brain tissues are responding differently to heat shock in the aspects of its level of expression and speed of recovery.

• 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.

• CELLMED
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• v.9 no.3
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• pp.4.1-4.8
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• 2019

Now researchers have focused attention on exploring the mechanism of acute responses of heat stress given in heat therapy that ultimately promotes the long term health benefits. Heat therapy is not a new idea rather it was practiced since thousands years back in the form of hot bath, sauna bath, steam room. Similarly in Ayurveda there is very comprehensive description of heat therapy in the form of Svedan karma (Sudation therapy). Svedan is a process to induce sweating artificially in a patient who had already undergone Snehan. Svedan is applied for purification of body, as well as in management of various disorders originated due to vitiation of Vata, Kapha Dosha, Meda Dhatu and musculoskeletal disorders. It produces various beneficial effects by augmenting the Agni like clears the channels, liquefies the deposited Dosha, regulates Vata Dosha, helps in removal and pacification of Dosha, augments metabolism (Agni Deepan), increases appetite, flexibility in body parts, softness and shining of skin, removes coldness, stiffness, drowsiness, improves joint motility. However, Svedana karma is vastly used by Ayurveda Physicians in treatment of various disorders but the mechanisms of beneficial effects produced by Svedan Karma are yet not completely explored on scientific basis. In this article, we will discuss and try to establish a possible mechanism of action of Svedana karma in relation to heat stress, mitochondrial adaptation, heat shock protein (HSP) and glucocorticoids as these are secreted under stressful conditions.

• 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 Physiology & Pathology in Korean Medicine
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• v.16 no.2
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• pp.220-225
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• 2002

To determine the anti-stress effect of KCG(加味天麻鉤藤飮) extract on sprague-dawley rats. we conducted a research about the change of weight, activity, reactivity, c-fos protein, cytotoxicity against PC12 cell line and heal shock protein. 1) KCG extract siginificantly inhibited the decrease of body weight induced by stress, compared with the control group. 2) KCG extract had no siginificant effect in the activity and reactivity of rats between the control and the experimental groups. 3) KCG extract siginificantly restrained c-fos protein manifestation, compared with the control group. 4) KCG extract siginificantly restrained heat shock protein, compared with the control group. These results suggested that KCG might be usefully anti-stress effect.

• 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 Plant Biotechnology
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• v.44 no.3
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• pp.287-295
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• 2017

Water temperature is one of the major factors that impacts the growth and life cycle of Pyropia tenera, one of the most valuable and cultivated marine red algae belonging to Bangiales (Rhodophytes). We analyzed transcriptome from gametophyte of P. tenera under normal and high temperature conditions, and identified four small heat shock proteins (sHSPs). They have no significant amino acid sequence homology with known proteins in public databases except PhsHSP22 from Pyropia haitanensis. PtsHSP19.3 gene responded to high temperature but slightly or not to desiccation, freezing or high salt condition. When the PtsHSP19.3 gene was overexpressed in Chlamydomonas reinhardtii, transformed Chlamydomonas lines revealed much higher growth rate than that of control cells under heat stress condition. Transformed cells also grew well in those of the control cell onto the medium containing high salt or $H_2O_2$. When the PtsHSP19.3 was fused to GFP and introduced into tobacco protoplast, fluorescence was detected at several spots. Results indicate that PtsHSP19.3 may form super-molecular assembles and be involved in tolerance to heat stress.