• 생물정신의학
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• 제14권4호
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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.

• The Plant Pathology Journal
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• 제31권4호
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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.

• 한국어병학회지
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• 제12권2호
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• pp.89-99
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• 1999

V. vulnificus ATCC 27562균주의 배양 온도를 $2^{\circ}C $, 20분간 및 6% 에탄올, 10분간으로 반응시켰을 때 SDS-PAGE상에서 새로운 16가지의 heat shock protein(hsps)과 10가지의 ethanol shock protein이 나타났다. Lethal temperature에 노출하기전에 미리 열 충격을 가한 경우 thermo tolerance가 유도되었다. 균체면역에 의해 생성된 항혈청과 열 충격 세포에서 분리된 막단백질과의 ELISA에서는 Outer Membrane Protein(OMP)에서 높은 면역반응을 나타냈으며 western blotting으로는 Inner Membrane Protein(IMP)에서는 62kDa, OMP에서는 69 kDa단백이 높은 면역원성을 나타냈다. ethanol 충격 반응에서는 IMP에서는 48 kDa, OMP에서는 오직 major밴드에서만 면역반응성이 확인되었다. anti-V, vulnificus혈청에 대한 균체 응집시험에서는 열 충격 반응 후의 균체가 정상 균체에 비해 응집반응성이 높았다.

• Molecules and Cells
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• 제23권2호
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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.

• Mycobiology
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• 제43권3호
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• pp.272-279
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• 2015

To screen molecular chaperones similar to small heat shock proteins (sHsps), but without ${\alpha}$-crystalline domain, heat-stable proteins from Schizosaccharomyces pombe were analyzed by 2-dimensional electrophoresis and matrix assisted laser desorption/ionization time-of-flight mass spectrometry. Sixteen proteins were identified, and four recombinant proteins, including cofilin, NTF2, pyridoxin biosynthesis protein (Snz1) and Wos2 that has an ${\alpha}$-crystalline domain, were purified. Among these proteins, only Snz1 showed the anti-aggregation activity against thermal denaturation of citrate synthase. However, pre-heating of NTF2 and Wos2 at $70^{\circ}C$ for 30 min, efficiently prevented thermal aggregation of citrate synthase. These results indicate that Snz1 and NTF2 possess molecular chaperone activity similar to sHsps, even though there is no ${\alpha}$-crystalline domain in their sequences.

• Fisheries and Aquatic Sciences
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• 제2권1호
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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.

• 한국동물학회지
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• 제39권1호
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• pp.47-53
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• 1996

K562 백혈구암 세포의 phorbol 12-myristate 13-acetate(PMA)에 의한 대핵세포로의 분화과정에서 heat shock proteins(HSPs)와 glucose-regulated proteins(GRPs)의 발현을 조사하였다. PMA에 의한 K562 세포의 분화 특징은 세포성장의 억제, 형태학적 변화, gpllIa의 발현 증가, c-myc 발현의 감소 등으로 나타난다. PMA에 의한 대핵세포 분화과정에서, HSP90A, HSP90B 그리고 HSP28 mRNA와 단백질 합성은 현저히 감소하는 반면, GRP78/BiP와 GRP94의 mRNA 합성은 증가하였다. 한편 HSP7OA와 HSP7OB의 mRNA 합성은 감소하였지만, HSP70 단백질의 합성은 변함이 없었다. 이러한 결과는 HSPs와 GRPs가 K562 세포의 증식 또는 대핵세포 분화 과정에서 특이한 역할을 할 것임을 시사하고 있다.

• 한국초지조사료학회지
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• 제18권4호
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• pp.303-310
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• 1998

목초의 내하고성을 증진시킬 목적으로 이용하고자 하는 내열성 유전자 (BcHSP17.6)의 발현양상을 배추에서 조사하였다. BcHSP17.6 단백질을 항원으로 한 항체를 생산하여 항원-항체 반응으로 확인한 결과, 생산된 항체는 항원과 결합하므로서 항체가 정상적으로 생산되었음을 확인하였다. 이 항체를 이용하여 다양한 heat shock (HS) 조건에서 15-~18-kD low molecular weight heat shock proteins (LMW HSPs)가 축적되는지를 조사하였다. 이들 LMW HSPs는 $35^{\circ}C$ 처리에서 나타나기 시작하였으며, $40^{\circ}C$에서 4시간 처리하였을 때 total protein 100 mg당 $1.56{\mu}g$이 축적되어 최대치를 나타내었다. 또한 합성된 이들 LMW HSPs는 HS 처리후 24시간이 경과되어도 거의 변함이 없었으며, $40^{\circ}C$ 보다 높은 온도 조건에서는 축적량이 감소하였다. 이와 같이 일단 합성된 LMW HSPs가 장시간 동안 감소하지 않는다는 사실로부터, 이들 HSPs들이 식물체가 내열성을 가지도록 하는데 관여하며, 더 나아가서 배추가 정상 생육온도보다 더 높은 치사온도에서도 살아남을 수 있도록 하는데 중요한 역할을 하는 것으로 사료된다.

• 한국가금학회지
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• 제47권4호
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• pp.219-227
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• 2020

기후변화는 현대 축산업이 직면한 가장 큰 위협 중의 하나이고, 특히 열 스트레스는 가금의 생산성 저하뿐만 아니라, 가축의 불편함과 고통을 증가시켜 동물의 복지에도 치명적 영향을 미칠 수 있다. 열 스트레스를 완화시키기 위한 다양한 전략들이 요구되는데, 가축의 열 스트레스에 대한 정확한 평가와 생물학적 평가지표의 개발은 기후변화에 대한 적응과 열 저항성 가금의 육종, 지속 가능한 가금 산업과 동물복지를 위해서 매우 중요하다. 스트레스호르몬, hetero- phils lymphocytes의 비율, 텔로미어 마모 정도 등 열 스트레스에 대한 다양한 바이오마커 중에 열충격단백질(HSPs)은 세포내 온도계로 여겨지며, HSPs 중에서도 HSP70은 가장 풍부한 단백질이면서 열 충격에 민감하게 반응하는 바이오 마커로 알려져 있다. HSP는 또한 열 충격으로부터 세포를 보호해주는 샤페론 활성을 지니고 있다. 따라서 HSP70 바이오마커는 가축의 열 스트레스에 대한 체계적 평가방법으로 주목받고 있으며, HSP70의 발현 변화의 이해는 기후변화에 대처하면서 지속가능한 가금 산업을 위해 매우 중요하고 판단된다. 이에 본 논문에서는 닭의 열 스트레스와 관련하여 HSP70을 중심으로 HSP의 작용기전과 역할, 열 스트레스와 HSP, 내열성 가축 선발을 위한 HSP70의 잠재성, 그리고 열 스트레스 바이오마커로서의 HSP70 등에 대한 최근까지의 연구들을 소개한다.

• Molecules and Cells
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• 제19권3호
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• pp.328-333
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• 2005

Small heat shock proteins (sHSPs) are widely distributed, and their function and diversity of structure have been much studied in the field of molecular chaperones. In plants, which frequently have to cope with hostile environments, sHSPs are much more abundant and diverse than in other forms of life. In response to high temperature stress, sHSPs of more than twenty kinds can make up more than 1% of soluble plant proteins. We isolated a genomic clone, NtHSP18.3, from Nicotiana tabacum that encodes the complete open reading frame of a cytosolic class I small heat shock protein. To investigate the function of NtHSP18.3 in vitro, it was overproduced in Escherichia coli and purified. The purified NtHSP18.3 had typical molecular chaperone activity as it protected citrate synthase and luciferase from high temperature-induced aggregation. When E. coli celluar proteins were incubated with NtHSP18.3, a large proportion of the proteins remained soluble at temperatures as high as $70^{\circ}C$. Native gel analysis suggested that NtHSP18.3 is a dodecameric oligomer as the form present and showing molecular chaperone activity at the condition tested. Binding of bis-ANS to the oligomers of NtHSP18.3 indicated that exposure of their hydrophobic surfaces increased as the temperature was raised. Taken together, our data suggested that NtHSP18.3 is a molecular chaperone that functions as a dodecameric complex and possibly in a temperature-induced manner.