• Proceedings of the Korean Society of Precision Engineering Conference
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• 2007.06a
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• pp.675-676
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• 2007

• Journal of the Korean Society of Food Science and Nutrition
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• v.32 no.3
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• pp.428-436
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• 2003

Epidemiological studies have observed a negative association between increased consumption of green and yellow vegetables and cancer incidence. These vegetables contain carotenoids, which are reported to exhibit anticarcinogenic effects. Overexpression of ErbB2 and ErbB3 genes is a frequent event in several human cancers. The present study was performed to determine whether $\alpha$-carotene, $\beta$-carotene, lutein, or lycopene inhibits cell growth and to assess such an effect is related to changes in the levels of the ErbB receptor family and tile ErbB3 receptor signaling pathway in HT-29 cells. HT-29 cells were cultured in serum-free medium in the presence of various concentrations (0~100 $\mu$M) of the individual carotenoids. $\alpha$ -Carotene and lycopene significantly inhibited cell growth in a dose-dependent manner, whereas lutein slightly inhibited cell growth and $\beta$-carotene increased cell growth. Lycopene is more potent than $\alpha$ -carotene in inhibiting HT-29 cell growth. Lycopene inhibited DNA synthesis and induced apoptosis of HT-29 cells. The ErbB3 ligand heregulin (HRG) increased cell growth but did not prevent the lycopene-induced inhibition of cell growth. Lycopene decreased ErbB2 protein levels in a dose-dependent manner. Immunoprecipitation/Western blot studies revealed that lycopene inhibited HRG-induced phosphorylation of ErbB3, recruitment of the 985 regulatory subunit of phosphatidylinositol 3-kinase (PI3K) to the ErbB3 receptor, and phosphorylation of Akt. These results indicate that downregulation of ErbB2/ErbB3/PI3K/Akt signaling may be one of the mechanisms by which lycopene inhibits HT-29 cell pro-liferation and induces apoptosis.

• Journal of the Korean Magnetics Society
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• v.7 no.5
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• pp.250-257
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• 1997

The microstructure and magnetic properties of Fe-Nb-B-N thin film alloys, which produced by rf magnetron sputtering method in $Ar+N_2$ mixed gas atmosphere, were investigated. The $Fe_{70}Nb_{14}B_{11}N_5$ films, annealed at 59$0^{\circ}C$, exhibit soft magnetic properties: $4{\pi}M_s=16.5kG$ , $H_c=0.13Oe$ and ${\mu}_{eff}$ (1~10 MHz)=5, 000. The frequency stability of the Fe-Nb-B-N films has also been found to be good up to 10 MHz. The Fe-Nb-B-N thin film alloys annealed at 59$0^{\circ}C$ consist of three phase; fine crystalline $\alpha$-Fe phase with grain size of about 5~10 nm, Nb-B rich amorphous phase and Nb-nitride precipitates with the size of less than 3 nm. Annealed Fe-Nb-B films have two phases; $\alpha$-Fe grains with the size of about 10 nm and Nb-B rich amorphous phase. The addition of N decreased $\alpha$-Fe grain size due to the precipitation of NbN. The good magnetic properties of the Fe-Nb-B-N film alloys are due to fine $\alpha$-Fe grains resulting from the precipitation of NbN.

• Journal of Life Science
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• v.32 no.6
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• pp.421-429
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• 2022

The expression of interleukin-1α (IL-1α) is elevated in monocytic cells, such as monocytes and macro-phages, within atherosclerotic arteries, yet the cellular molecules involved in cytokine upregulation remain unclear. Because peptidoglycan (PG), a major component of gram-positive bacterial cell walls, is detected within the inflammatory cell-rich regions of atheromatous plaques, it was investigated if PG contributes to IL-1α expression in monocytes/macrophages. Exposure of THP-1 monocytic cells to PG resulted in elevated levels of IL-1α gene transcripts and increased secretion of IL-1α protein. The transcription and secretion of IL-1α were abrogated by OxPAPC, an inhibitor of TLR2/4, but not by polymyxin B that inhibits lipopolysaccharide-induced TLR4 activation. To understand the molecular mechanisms of the inflammatory responses due to bacterial pathogen-associated molecular patterns (PAMPs) in diseased arteries, we attempted to determine the cellular factors involved in the PG-induced upregulation of IL-1α expression. Pharmacological inhibition of cell signaling pathways with LY294002 (a PI3K inhibitor), Akti IV (an inhibitor of Akt activation), rapamycin (an mTOR inhibitor), U0126 (a MEK inhibitor), SB202190 (a p38 MAPK inhibitor), SP6001250 (a JNK inhibitor), and DPI (a NOX inhibitor) also significantly attenuated the PG-mediated expression of IL-1α. These results suggest that PG induces the monocytic or macrophagic expression of IL-1α, thereby contributing to vascular inflammation, via multiple signaling molecules, including TLR2, PI3K/Akt/mTOR, and MAPKs.

• Proceedings of the Korean Society of Precision Engineering Conference
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• 2013.05a
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• pp.349-350
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• 2013

• Proceedings of the Korean Society of Precision Engineering Conference
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• 2010.05a
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• pp.565-566
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• 2010

• The Journal of Korean Institute of Communications and Information Sciences
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• v.25 no.7B
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• pp.1282-1291
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• 2000

기존의 LQ-서보형 PI 설계방법은 보드선도 상에서 저주파와 고주파 영역에서의 루프전단함수의 특이값 일치에 기이한 설계상의 문제를 가지고 있다. 이러한 점을 해결하기 위해 역 최적제어와 볼록형 최적화기법에 기초한 새로운 설계 방법을 제안하고자 한다.

• Proceedings of the Korean Society of Plant Pathology Conference
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• 2002.11a
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• pp.81.1-81
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• 2002

• Bulletin of the Korean Chemical Society
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• v.25 no.6
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• pp.924-926
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• 2004

• The Korean Journal of Food And Nutrition
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• v.15 no.2
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• pp.104-111
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• 2002

The peptidyl prolyl sis-trans isomerase (PPIase, EC 5.2.1.8) from bacillus stearothermophilus was extracted from the cells treated with by lysozyme. PPIase was purified from the cell extracts by heat treatment, ammonium sulfate precipitation, ion exchange chromatography and finally gel filtration, sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE). The molecular weight of the purified PPIase was estimated as 18kDa by SDS-PAGE. The 39 amino acid residues from the N-terminus were determined by the protein sequencer. The enzyme showed the optimum pH at 8.0 and was stable at the range of pH 7.0∼8.0. The enzyme was considerably stable after heat treatment at 60$\^{C}$ for 30minutes, and the enzyme was quite stable up to 65$\^{C}$. The presence of the PPIase in the refolding solution accelerated the isomerization rate of the assay peptide. PPIase gene of Bacillus stearothermophilus was screened from a genomic library by plaque hybridization using the A-l primer as a probe. A PPIase positive plaque contained a 3.0kb insert of the chromosomal DNA. A 3.0kb fragment was subcloned into pUC18, resulting pPI-40. A DNA fragment encoding the N-terminal portion of the PPIase in pPI-40 was amplified by polymerase chain reaction(PCR) method using the A-1 and B-2 primers. The amplified fragment was cloned into the Sma I site of pUC18 and recombinant plasmid was designated as pSN-18. The nucleotide sequence of 167bp fragment was determined. The deduced amino acid sequence of PPIase was completely matched with the determined N-terminal amino acid sequence of PPIase B. stearothermophilus.