• 대한의생명과학회지
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• 제12권1호
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• pp.53-56
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• 2006

The suprachiasmatic nucleus (SCN) of the anterior hypothalamus is the circadian pacemaker entrained to the 24-hr day by environmental time cues. Major circadian genes such as mPeriod ($mPer1{\sim}3$) and mCryptochrome ($mCry1{\sim}2$) are actively transcribed by the action of CLOCK/BMAL heterodimers, and in turn, these are being suppressed by the mPER/mCRY complex. In the study, the locomotor activity rhythms of mPer1 Knockout (KO) mice are measured, and the expression profiles of Heat Shock Protein 105kDa (HSP 105) genes in the SCN were measured by in situ hybridization. In agreement with previous reports, the locomotor activity rhythm of mPer1 KO mice was much shorter than that of wildtype. In addition, the total bout of activity of mPer1 KO was less in comparison to control mice. The expression of HSP 105 in the SCN of mPer1 KO mice was ranged from CT6 to CT22, with a peak level at CT14, implying that the gene are under the control of circadian clock. However, the expression of HSP 105 in the SCN of wildtype could not be detected in our study. Further analysis will reveal the direct or indirect regulation by mPer1 on the expression in the SCN and the role of the gene in the circadian clock.

• 생명과학회지
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• 제28권6호
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• pp.639-647
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• 2018

한국의 고급 양식대상 어종인 붉바리(Epinephelus akaara)로부터 새로운 heat shock protein (Hsp) 70을 동정하였다. 붉바리 Hsp70 (RgHsp70)의 cDNA는 RACE (rapid amplification of cDNA ends)법을 사용하였고, RgHsp70 cDNA의 전장은 2,152 bp이고, 5'-terminal untranslated region (UTR)은 105 bp, 3'-terminal UTR은 274 bp, 590개의 아미노산을 암호화하는 open reading frame (ORF)는 1,773 bp였으며, 분자무게(molecular weight)는 64.9 kDa 및 등전위값(isoelectric point, pI)은 5.2였다. 추정되는 아미노산 비교 및 계통발생학적 분석 결과, 다른 어종과 마찬가지로 Hsp70 고유의 signature를 포함하는 것을 비롯하여 높은 유사성을 나타내었으므로 RgHsp70이 Hsp70 family임을 확인할 수 있었다 RgHsp70 mRNA는 간과 두신 조직에서 높은 발현을 보였으며, 48시간 동안 수온별(21, 18, 15 및 $12^{\circ}C$) 노출 후 간 조직에서 대조구인 $21^{\circ}C$보다 $12^{\circ}C$에서 발현이 증가함을 확인하였다. 본 연구에서는, 수온이 하강함에 따라 RgHsp70 mRNA 발현에 주요한 영향을 미치는 것으로 보아, 수온변화에 따른 스트레스로 인해 발현의 변화를 나타내는 주요 스트레스성 단백질임을 확인할 수 있었다.

• 한국양식학회:학술대회논문집
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• 한국양식학회 2005년도 춘계학술발표대회 논문요약집
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• pp.104-105
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• 2005

• Journal of Animal Science and Technology
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• 제65권4호
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• pp.683-697
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• 2023

The threat posed by increased surface temperatures worldwide has attracted the attention of researchers to the reaction of animals to heat stress. Spermatogenesis in animals such as stallions is a temperature-dependent process, ideally occurring at temperatures slightly below the core body temperature. Thus, proper thermoregulation is essential, especially because stallion spermatogenesis and the resulting spermatozoa are negatively affected by increased testicular temperature. Consequently, the failure of thermoregulation resulting in heat stress may diminish sperm quality and increase the likelihood of stallion infertility. In this review, we emphasize upon the impact of heat stress on spermatogenesis and the somatic and germ cells and describe the subsequent testicular alterations. In addition, we explore the functions and molecular responses of heat shock proteins, including HSP60, HSP70, HSP90, and HSP105, in heat-induced stress conditions. Finally, we discuss the use of various therapies to alleviate heat stress-induced reproductive harm by modulating distinct signaling pathways.

• 대한의생명과학회지
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• 제9권2호
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• pp.105-110
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• 2003

Ankyrins are a ubiquitously expressed family of intracellular adaptor proteins involved in targeting diverse proteins to specialized membrane domains in both the plasma membrane and the endoplasmic reticulum. Canonical ankyrins are 190-220 kDa proteins expressed in most tissues and cell types and comprise a membrane-binding domain (MBD) of 24 ANK repeats, a spectrin-binding domain, a death domain and a C-terminal domain. Rescue studies with ankyrin-B/G chimeras have identified the C-terminal domain of ankyrin-B as the defining domain in specifying ankyrin-B activity, but the function of C-terminal domain of ankyrin-B is, however, not known. We report here that the C-terminal domain of ankyrin-B is capable of interacting with the C-terminal Region of Hsp40. The Hsps are induced not only by heat shock but also by various other environmental stresses. Hsps are also expressed constitutively at normal growth temperatures and have basic and indispensable functions in the life cycle of proteins as molecular chaperones, as well as playing a role in protecting cells from the deleterious stresses. The binding sites required in the interaction between C-terminal domain of ankyrin-B and C-terminal region of Hsp40 were characterized using the yeast two-hybrid system and GST-pull down assay. The interaction between ankyrin-B and Hsp40 represents the first direct evidence of ankyrin's role as chaperones.

• Asian Pacific Journal of Cancer Prevention
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• 제13권5호
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• pp.2185-2191
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• 2012

Background: Prevalence of Barrett's esophagus (BE) in Luoyang, China, has not been reported, and its pathogenesis is controversial. The aim of this study was therefore to investigate the prevalence of BE and its underlying factors in the city of Luoyang. Method: This was a prospective study in one center. Many patients were analyzed using endoscopy who showed upper gastrointestinal symptoms between August 2006 and June 2007. In addition, the effect of apoptosis-related proteins and heat shock proteins upon BE's pathogenesis were also investigated by an immunohistochemical protocol. Results: Prevalence of BE was at 4.55% and the mean age of those affected was about 10 years older than for esophagitis. Typical reflux symptoms were significantly lower than with esophagitis, whereas signs of caspase-3 and HSP105 elevation were significantly higher. Expression of TERT, HSP70 and $HSP90{\alpha}$ in BE cases was significantly lower than in esophagitis. However, there was no statistical difference between the two groups in expression of HSP27. Conclusions: The prevalence of BE is high in Luoyang, which could result from esophagitis despite typical reflux symptoms being relatively uncommon. Initiation and development of BE might be the result of accelerated proliferation, apoptosis and differentiation of original cells to intestinal epithelium.

• 생명과학회지
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• 제24권2호
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• pp.105-111
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• 2014

본 연구의 목적은 말의 열충격 단백질 유전자의 특성을 구명하고 말의 각 조직과 운동 전과 후 혈액에서 열충격 단백질 유전자의 발현량을 분석함에 있다. 이전의 연구를 통해, 대표적인 경주마인 더러브렛의 혈액과 골격근에서 운동 전, 후 RNA-sequencing을 통해 차등발현유전자 분석을 실시하고, 본 연구를 위해 운동 전과 후에 차등 발현된 유전자 중, 열충격 단백질 유전자(HspH1, Hsp90${\alpha}$, Hsp70)를 선택하였다. 세 개의 열충격 단백질 유전자는 각각의 혈액이나 근육에서 운동 전에 비해 후에 발현이 증가된 것으로 확인됐다. 본 연구팀은 선정된 유전자에 대한 검증과 분석을 위해, 말의 조직별 RT-PCR 분석과 운동시간별 백혈구에서 real time qPCR 분석을 실시하였다. 그 결과 말의 각 조직(갑상선, 결장, 골격근, 맹장, 신장, 심장, 척수, 폐)에서 세 개의 열충격 단백질 유전자 mRNA가 모두 존재함을 알 수 있었다. 또한, 말의 운동 시간 별 혈액에서 mRNA를 추출하여 열충격 단백질의 운동 시간에 따른 발현 양상 분석을 실시한 결과, 운동 전에 비해 운동 120분 후 열충격 단백질 유전자의 발현량이 증가함을 확인하였다. 이러한 결과는 인간과 다른 동물 실험의 결과와 일치하며, 열충격 단백질 유전자 전사 조절기작이 종간에 보존이 되어왔음을 시사한다. 또한, 운동에 따른 열충격 단백질 유전자의 발현 양상과 운동 수행 및 회복 기작간의 상관관계에 대한 추가적인 연구가 필요함을 제안하는 바이다.

• 대한한방내과학회지
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• 제25권4호
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• pp.105-116
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• 2004

Objective : In this study, we used the aged bilateral common carotid artery occlusion (BCAO) rats were used to measure the effect of Bupleuri Radix (Si-Ho) on the brain ischemic injury, because aging is an important factor in storke, Method : The brian ischemic injury was induced by temporary closing of carotids on both sides in a low blood pressure state. Bupleuri Radix (Si-Ho) was orally administered in 18-month-old BCAO rats. Result : The Ischemic Damaged Hippocampus and HSP expression were analyzed by the immunohistochemical staining and the result were as follows: 1. The low numbers of pyramid cells in the hippocampus CA1 area for the ischemically injured experimental group rose to numbers simillar to those of the control group. 2. The thin neuronal cell layer in the hippocampus CA1 area for the ischemically injured experimental group returned to thickness simillar to those of the control group. 3. The normalized optical density of HSP70 expression was suppressed in CA2, DG and CA1 expression was significantly suppressed in the experimental group compared to the control group. Conclusion : These results suggested that Bupleuri Radix (Si-Ho) has a neuroprotective effect by reducing neural cell injury in the initial ischemic state.

• BMB Reports
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• 제45권6호
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• pp.331-336
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• 2012

The retinoid-related orphan nuclear receptor gamma ($ROR{\gamma}$) plays critical roles in regulation of development, immunity and metabolism. As transcription factor usually forms a protein complex to function, thus capturing and dissecting of the $ROR{\gamma}$ protein complex will be helpful for exploring the mechanisms underlying those functions. After construction of the recombinant tandem affinity purification (TAP) plasmid, pMSCVpuro $ROR{\gamma}$-CTAP(SG), the nuclear localization of $ROR{\gamma}$-CTAP(SG) fusion protein was verified. Following isolation of $ROR{\gamma}$ protein complex by TAP strategy, seven candidate interacting proteins were identified. Finally, the heat shock protein 90 (HSP90) and receptor-interacting protein 140 (RIP140) were confirmed to interplay with $ROR{\gamma}$ by co-immunoprecipitation. Interference of HSP90 or/and RIP140 genes resulted in dramatically decreased expression of CYP2C8 gene, the $ROR{\gamma}$ target gene. Data from this study demonstrate that HSP90 and RIP140 proteins interact with $ROR{\gamma}$ protein in a complex format and function as co-activators in the $ROR{\gamma}$-mediated regulatory processes of HepG2 cells.

• 한국자기공명학회논문지
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• 제19권3호
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• pp.99-105
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• 2015

Hsp33 is a prokaryotic molecular chaperon that exerts a holdase activity upon response to an oxidative stress at raised temperature. In particular, intramolecular disulfide bond formation between the four conserved cysteines that bind a zinc ion in reduced state is known to be critically associated with the redox sensing. Here we report the backbone NMR assignment results of the half-oxidized Hsp33, where only two of the four cysteines form an intramolecular disulfide bond. Almost all of the resolved peaks could be unambiguously assigned, although the total assignments extent reached just about 50%. Majority of the missing assignments could be attributed to a significant spectral collapse, largely due to the oxidation-induced unfolding of the C-terminal redox-switch domain. These results support two previous suggestions: conformational change in the first oxidation step is localized mainly in the C-terminal zinc-binding domain, and the half-oxidized form would be still inactive. However, some additional regions appeared to be potentially changed from the reduced state, which suggest that the half-oxidized conformation would be an intermediate state that is more labile to heat and/or further oxidation.