• 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.

• Korean Journal of Oriental Medicine
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• v.13 no.1 s.19
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• pp.153-160
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• 2007

In the post-genome era, analysis of the cellular transcriptome using microarray or the cellular proteome using a 2-D gel electrophoresis and MALDI-TOF mass spectrometry are most widely used. Stroke is one of the most important causes of death along with cancer and cardiac disease. When pathological change of cells in developed from cerebral ischemia accompanied by stroke administration of neuroprotective drugs before stroke can decreases the degeneration of neuronal cells. The purpose of the present study was to assess the neuroprotective effect and protein expression after administration of P004, middle cerebral artery model of cerebral ischemia in rats. SD rats were subjected to middle cerebral artery occlusion. P004 (1,000 mg/kg) was administered 2 times at 0, 90 minutes after middle cerebral artery occlusion (MCAo). Rats were killed at 48 hours, and infarct area and volume were determined by histology and computerized image analysis. We investigated the protein expression profile on the global ischemia induced by MCAo. This proteomic analysis enable us to identify several proteins differently expressed in infarct brain tissue. The aims of this study were to do investigation comparing the neuroprotection activities of P004 and to understand the mechanism of acted as neuroprotective drug.

• Journal of Microbiology and Biotechnology
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• v.22 no.4
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• pp.470-478
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• 2012

Recent genome comparisons of E. coli B and K-12 strains have indicated that the makeup of the cell envelopes in these two strains is quite different. Therefore, we analyzed and compared the envelope proteomes of E. coli BL21(DE3) and MG1655. A total of 165 protein spots, including 62 nonredundant proteins, were unambiguously identified by two-dimensional gel electrophoresis and mass spectrometry. Of these, 43 proteins were conserved between the two strains, whereas 4 and 16 strain-specific proteins were identified only in E. coli BL21(DE3) and MG1655, respectively. Additionally, 24 proteins showed more than 2-fold differences in intensities between the B and K-12 strains. The reference envelope proteome maps showed that E. coli envelope mainly contained channel proteins and lipoproteins. Interesting proteomic observations between the two strains were as follows: (i) B produced more OmpF porin with a larger pore size than K-12, indicating an increase in the membrane permeability; (ii) B produced higher amounts of lipoproteins, which facilitates the assembly of outer membrane ${\beta}$-barrel proteins; and (iii) motility- (FliC) and chemotaxis-related proteins (CheA and CheW) were detected only in K-12, which showed that E. coli B is restricted with regard to migration under unfavorable conditions. These differences may influence the permeability and integrity of the cell envelope, showing that E. coli B may be more susceptible than K-12 to certain stress conditions. Thus, these findings suggest that E. coli K-12 and its derivatives will be more favorable strains in certain biotechnological applications, such as cell surface display or membrane engineering studies.

• Bulletin of the Korean Chemical Society
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• v.28 no.9
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• pp.1499-1509
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• 2007

Proteomic analyses of synaptic vesicle fraction from rat brain have been performed for the better understanding of vesicle regulation and signal transmission. Two different approaches were applied to identify proteins in synaptic vesicle fraction. First, the isolated synaptic vesicle proteins were treated with trypsin, and the resulting peptides were analyzed using a high-pressure capillary reversed phase liquid chromatography/tandem mass spectrometry (cRPLC/MS/MS). Alternatively, proteins were separated by two-dimensional gel electrophoresis (2DE) and identified by matrix-assisted laser desorption ionization mass spectrometry (MALDI-TOF/MS). Total 18 and 52 proteins were identified from cRPLC/MS-MS and 2DE-MALDI-TOF-MS analysis, respectively. Among them only 2 proteins were identified by both methods. Of the proteins identified, 70% were soluble proteins and 30% were membrane proteins. They were categorized by their functions in vesicle trafficking and biogenesis, energy metabolism, signal transduction, transport and unknown functions. Among them, 27 proteins were not previously reported as synaptic proteins. The cellular functions of unknown proteins were estimated from the analysis of domain structure, expression profile and predicted interaction partners.

• The KIPS Transactions:PartD
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• v.12D no.5 s.101
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• pp.719-728
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• 2005

2-dimensional electrophoresis(2DE) is a separation technique to identify proteins contained in a sample. However, the image is very sensitive to its experimental conditions as well as the quality of scanning. In order to adjust the possible variation of spots in a particular image, a user should manually annotate landmark spots on each gel image to analyze the spots of different images together. However, this operation is an error-prone and tedious job. This thesis develops an automated method of extracting the landmark spots of an image based on landmark profile. The landmark profile is created by clustering the previously identified landmarks of sample images of the same type. The profile contains the various properties of clusters identified for each landmark. When the landmarks of a new image need to be fount all the candidate spots of each landmark are first identified by examining the properties of its clusters. Subsequently, all the landmark spots of the new image are collectively found by the well-known optimization algorithm $A^*$. The performance of this method is illustrated by various experiments on real 2DE images of mouse's brain-tissues.