• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.10a
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• pp.375-379
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• 2004

Probiotic 활성이 높은 L. acidophilus 30SC의 생존성을 증진시키기 위한 기초자료를 얻고자, 열처리 동안 새로이 발현되는 단백질을 일차원 및 이차원 전기영동을 이용하여 확인하였으며, 세포 모양을 주사전자현미경을 사용하여 관찰하였다. $55^{\circ}C$의 heat shock에는 L. acidphilus 30SC의 사멸이 있는 것으로 나타났다. 나머지 처리구는 $37^{\circ}C$에서 계속 배양한 것과 별다른 차이를 나타내지 않았다. $45^{\circ}C$로 heat shock을 준 경우 $37^{\circ}C$에서 배양한 것과 거의 동일하였다. $55^{\circ}C$에서 15분 heat shock을 준 경우 약 22kDa와 25kDa의 단백질들이 새로이 발현된 것으로 나타났으나, 24 kDa와 27kDa로 추정되는 단백질의 발현정도는 낮았음을 확인하였다. 이차원 전기영동을 실시한 결과, $37^{\circ}C$와 비교할 때 $55^{\circ}C$로 heat shock을 준 경우 새로이 5개의 protein spot을 발견할 수 있었다. 그러나 6개의 단백질 spot은 $55^{\circ}C$ heat shock에서 소실된 것으로 확인되어 추가적인 단백질의 분석이 필요한 것으로 생각되었다.

• BMB Reports
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• v.33 no.4
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• pp.289-293
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• 2000

Annexin I is a 37 kDa member of the annexin family of calcium-dependent phospholipid binding proteins. Annexin I plays regulatory roles in various cellular processes including cell proliferation and differentiation. Recently we found that annexin I is a heat shock protein (HSP) and displays a chaperone-like function. In this paper we investigated the function of annexin I as an ATPase using 1 to 32 amino acids deleted annexin I (${\Delta}-annexin$ I). ${\Delta}-Annexin$ I hydrolyzed ATP as determined by thin layer chromatography. The ability of ATP hydrolysis was inhibited by ADP, GTP and GDP, but not by the AMP, GMP and cAMP. In view of the ATP hydrolyzing function of HSP, the results support the function of annexin I as a HSP.

• The Korean Journal of Physiology and Pharmacology
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• v.16 no.6
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• pp.469-476
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• 2012

2,3,7,8-Tetrachlorodibenzo-p-dioxin (2,3,7,8-TCDD) is an environmental toxicant with a polyhalogenated aromatic hydrocarbon structure and is one of the most toxic man-made chemicals. Exposure to 2,3,7,8-TCDD induces reproductive toxicity, immunotoxicity, and hepatotoxicity. In this study, we evaluated how 2,3,7,8-TCDD-induced hepatotoxicity affect the expression of heat shock proteins and antioxidant enzymes using the real-time polymerase chain reaction (PCR) in rat. 2,3,7,8-TCDD increased heat shock protein (Hsp27, ${\alpha}$-B-crystallin, Mortalin, Hsp105, and Hsp90s) and antioxidant enzymes (SOD-3, GST and catalase) expression after a 1 day exposure in livers of rats, whereas heat shock protein (${\alpha}$-B-crystallin, Hsp90, and GRP78) and antioxidant enzymes (SOD-1, SOD-3, catalase, GST, and GPXs) expression decreased on day 2 and then slowly recovered back to control levels on day 8. These results suggest that heat shock proteins and antioxidant enzymes were induced as protective mechanisms against 2,3,7,8-TCDD induced hepatotoxicity, and that prolonged exposure depressed their levels, which recovered to control levels due to reduced 2,3,7,8-TCDD induced hepatotoxicity.

• Bulletin of the Korean Chemical Society
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• v.33 no.8
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• pp.2508-2512
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• 2012

Cold shock proteins (CSPs) are a family of proteins induced at low temperatures. CSPs bind to single-stranded nucleic acids through the ribonucleoprotein 1 and 2 (RNP 1 and 2) binding motifs. CSPs play an essential role in cold adaptation by regulating transcription and translation via molecular chaperones. The solution nuclear magnetic resonance (NMR) or X-ray crystal structures of several CSPs from various microorganisms have been determined, but structural characteristics of psychrophilic CSPs have not been studied. Therefore, we optimized the purification process to obtain highly pure Lm-Csp and determined the three-dimensional structure model of Lm-Csp by comparative homology modeling using MODELLER on the basis of the solution NMR structure of Bs-CspB. Lm-Csp consists of a ${\beta}$-barrel structure, which includes antiparallel ${\beta}$ strands (G4-N10, F15-I18, V26-H29, A46-D50, and P58-Q64). The template protein, Bs-CspB, shares a similar ${\beta}$ sheet structure and an identical chain fold to Lm-Csp. However, the sheets in Lm-Csp were much shorter than those of Bs-CspB. The Lm-Csp side chains, E2 and R20 form a salt bridge, thus, stabilizing the Lm-Csp structure. To evaluate the contribution of this ionic interaction as well as that of the hydrophobic patch on protein stability, we investigated the secondary structures of wild type and mutant protein (W8, F15, and R20) of Lm-Csp using circular dichroism (CD) spectroscopy. The results showed that solvent-exposed aromatic side chains as well as residues participating in ionic interactions are very important for structural stability. Further studies on the three-dimensional structure and dynamics of Lm-Csp using NMR spectroscopy are required.

• Journal of Life Science
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• v.11 no.5
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• pp.464-469
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• 2001

A gene, dnaK2, encoding a distinct member of the HSP70 family of molecular chaperones is isolated from the halotolerant cyanobactrium Aphanothece halophytica. The dnak2 gene encodes a molecular wight of 68 kDa polypeptide with predicted 616 amino acid residues. The DnaK2 protein has a structural characteristic of bacterial DnaK homologues and shows high similarity to other HSP70/Dank proteins. The danK2 transcripts are hardly detectable at 28$^{\circ}C$ and strongly induced upon heat stress. It is also found that dnaK2 transcript is increased by high-salinity stress even in the absence of heat stress. These results suggest that the DnaK2 protein plays an important role in protecting A. halophytica against damage caused by salt stress at well as heat stress.

• Molecules and Cells
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• v.20 no.3
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• pp.378-384
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• 2005

Estrogen metabolites are carcinogenic. The comparative mitogenic activities of $17{\beta}$-estradiol (E2) and four metabolites, 2-hydroxyestradiol (2-OHE2), 4-hydroxyestradiol (4-OHE2), $16{\alpha}$-hydroxyestrone ($16{\alpha}$-OHE1) and 2-methoxyestradiol (2-ME), were determined in estrogen receptor(ER)-positive MCF-7 human breast cancer cells. Each of the E2 metabolites caused proliferation of the MCF-7 cells, but only E2 and $16{\alpha}$-OHE1 induced a greater than 20-fold increases in transcripts of the progesterone receptor (PR) gene, a classical ER-mediated gene. This suggests that the mitogenic action of E2 and $16{\alpha}$-OHE1 could result from their effects on gene expression via the ER. E2 metabolites altered the expression of E2-regulated proteins including heat shock proteins (Hsps). $16{\alpha}$-OHE1 and 2-ME as well as E2 increased levels of Hsp56, Hsp60, $Hsp90{\alpha}$ and Hsp110 transcripts, and the patterns of these inductions resembled that of PR. Hsp56 and Hsp60 protein levels were increased by all the E2 metabolites. Levels of the transcripts of 3 E2-upregulated proteins (XTP3-transactivated protein A, protein disulfide isomerase-associated 4 protein and stathmin 1) and an E2-downregulated protein (aminoacylase 1) were also affected by the E2 metabolites. These results suggest that the altered expression of Hsps (especially Hsp56 and Hsp60) by E2 metabolites such as E2, $16{\alpha}$-OHE1 and 2-ME could be closely linked to their mitogenic action.

• Genomics & Informatics
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• v.20 no.3
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• pp.33.1-33.17
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• 2022

Nervous necrosis virus (NNV) is a deadly infectious disease that affects several fish species. It has been found that the NNV utilizes grouper heat shock cognate protein 70 (GHSC70) to enter the host cell. Thus, blocking the virus entry by targeting the responsible protein can protect the fishes from disease. The main objective of the study was to evaluate the inhibitory potentiality of 70 compounds of Azadirachta indica (Neem plant) which has been reported to show potential antiviral activity against various pathogens, but activity against the NNV has not yet been reported. The binding affinity of 70 compounds was calculated against the GHSC70 with the docking and molecular dynamics (MD) simulation approaches. Both the docking and MD methods predict 4 (PubChem CID: 14492795, 10134, 5280863, and 11119228) inhibitory compounds that bind strongly with the GHSC70 protein with a binding affinity of -9.7, -9.5, -9.1, and -9.0 kcal/mol, respectively. Also, the ADMET (absorption, distribution, metabolism, excretion, and toxicity) properties of the compounds confirmed the drug-likeness properties. As a result of the investigation, it may be inferred that Neem plant compounds may act as significant inhibitors of viral entry into the host cell. More in-vitro testing is needed to establish their effectiveness.

• Journal of the Korean Magnetic Resonance Society
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• v.23 no.1
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• pp.26-32
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• 2019

${\alpha}B$-crystallin (${\alpha}BC$) is a member of a small heat-shock protein (sHSP) superfamily and plays a predominant role in cellular protein homeostasis network by rescuing misfolded proteins from irreversible aggregation. ${\alpha}BC$ assembles into dynamic and polydisperse high molecular weight complexes containing 12 to 48 monomers; this variable stereochemistry of ${\alpha}BC$ has been linked to quaternary subunit exchange and its chaperone activity. The chaperone activity of ${\alpha}BC$ poses great potential as therapeutic agents for various neurodegenerative diseases. In this mini-review, we briefly outline the recent advancement in structural characterization of ${\alpha}BCs$ and its potential role to inhibit protein misfolding and aggregation in various human diseases. In particular, nuclear magnetic resonance (NMR) spectroscopy and its complimentary techniques have contributed much to elucidate highly-dynamic nature of ${\alpha}BCs$, among which notable advancements are discussed in detail. We highlight the importance of resolving the structural details of various ${\alpha}BC$ oligomers, their quaternary dynamics, and structural heterogeneity.

• Korean Journal of Microbiology
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• v.37 no.3
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• pp.221-227
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• 2001

Heat shock proteins serve as chaperone by preventing the aggregation of denatured proteins and promote survival of pathogens in harsh environments. In bacteria, ethanol shock induced the major chaperone GroEL and DnaK, but in Streptococcus pneumoniae, it induced neither GroEL nor DnaK but alcohol dehydrogenase (ADH). In this study, ADH gene encoding a 104-kDa (p104) protein was identified and characterized. The deduced amino acid sequence of pneumococcal ADH shows homology with other members of the ADH family, and particularly with Entamoeba histolytica ADH2 and E. coli ADH. S. pneumoniae adh is composed of 883 amino acids and its estimated isoelectric point is 6.09. Although ADH is conserved between S. pneumoniae and E. coli, immunoblot analysis employing antisera raised against pneumococcus ADH demonstrated no cross-reactivity with ADH analog in Eschericha coli, Staphylococcus aureus and human HeLa cells. Also secretion of ADH was demonstrated by subcellular fractionation and immunoblot analysis of proteins. These results suggest that S. pneumoniae ADH could be a highly feasible candidate for both diagnostic marker and vaccine.

• Archives of Plastic Surgery
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• v.37 no.4
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• pp.317-322
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• 2010

Purpose: There is no clear evidence of the original cause of hypertrophic scar, and the effective method of treatment is not yet established. Recently the steps of searching in gene and molecular level are proceeding. we are trying to recognize the difference between keratinocytes of hypertrophic scar and normal skin. Then we do support the comprehension of the scar formation mechanism and scar management. Methods: Total RNAs were extracted from cultured keratinocytes from 4 hypertrophic scars and normal skins. The cDNA chips were prepared. A total of 3063 cDNAs from human cDNA library were arrayed. And the scanning data were analyzed. Results: On microarray, heat shock protein, pyruvate kinase, tumor rejection antigen were more than 2 fold intensity genes. Among them, heat shock 70 kd protein showed the strongest intensity difference. Conclusion: In this study, it can be concluded that heat shock proteins play an important role in the process of wound healing and scar formation. This study provides basic biologic information for scar research. The new way of the prevention and treatment of scar formation would be introduced with further investigations.