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Joung, Dae-Ki,Mun, Su-Hyun,Lee, Kuang-Shim,Kang, Ok-Hwa,Choi, Jang-Gi,Kim, Sung-Bae,Gong, Ryong,Chong, Myong-Soo,Kim, Youn-Chul,Lee, Dong-Sung,Shin, Dong-Won,Kwon, Dong-Yeul Hindawi Publishing Corporation 2014 Evidence-based Complementary and Alternative Medic Vol.2014 No.-
<P>Tectorigenin (TTR) is an O-methylated isoflavone derived from the rhizome of <I>Belamacanda chinensis</I> (L.) DC. It is known to perform a wide spectrum of biological activities such as antioxidant, anti-inflammatory, anti-tumor. The aim of this study is to examine the mechanism of antibacterial activity of TTR against methicillin-resistant <I>Staphylococcus aureus</I> (MRSA). The anti-MRSA activity of TTR was analyzed in combination assays with detergent, ATPase inhibitors, and peptidoglycan (PGN) derived from <I>S. aureus</I>. Transmission electron microscopy (TEM) was used to monitor survival characteristics and changes in <I>S. aureus</I> morphology. The MIC values of TTR against all the tested strains were 125 <I><I>μ</I></I>g/mL. The OD(600) of each suspension treated with a combination of Triton X-100, DCCD, and NaN<SUB>3</SUB> with TTR (1/10 × MIC) had been reduced from 68% to 80%, compared to the TTR alone. At a concentration of 125 <I><I>μ</I></I>g/mL, PGN blocked antibacterial activity of TTR. This study indicates that anti-MRSA action of TTR is closely related to cytoplasmic membrane permeability and ABC transporter, and PGN at 125 <I><I>μ</I></I>g/mL directly bind to and inhibit TTR at 62.5 <I><I>μ</I></I>g/mL. These results can be important indication in study on antimicrobial activity mechanism against multidrug resistant strains.</P>
JOUNG, DAE-KI,CHOI, SUNG-HOON,KANG, OK-HWA,KIM, SUNG-BAE,MUN, SU-HYUN,SEO, YUN-SOO,KANG, DA-HYE,GONG, RYONG,SHIN, DONG-WON,KIM, YOUN-CHUL,KWON, DONG-YEUL SPANDIDOS PUBLICATIONS 2015 MOLECULAR MEDICINE REPORTS Vol.12 No.1
<P>Methicillin-resistant Staphylococcus aureus (MRSA) infection is a serious clinical problem worldwide. The aim of the present study was to examine the antimicrobial activity of oxyresveratrol (ORV) against MRSA. The antimicrobial activity of ORV was evaluated against three strains of MRSA and one methicillin-susceptible S. aureus (MSSA) strain using a minimal inhibitory concentration (MIC) assay, MTT colorimetric assay, checkerboard dilution test and time-kill assay. The MIC of ORV for all strains was moderate at 125 ?g/ml. Of note, the antimicrobial activity and fractional inhibitory concentration index values of ORV were markedly increased in the presence of a non-growth inhibitory dose of certain antibiotics. Time-kill curves revealed that a combination of ORV with ciprofloxacin or with gentamicin reduced bacterial counts to below the lowest detectable limit after 24 h. These effective combinations may be used as potential antimicrobial regimens for use in the management of MRSA.</P>
Inactivation of Brain myo-Inositol Monophosphate Phosphatase by Pyridoxal-5`-Phosphate
( Dae Won Kim ),( Joung Woo Hong ),( Won Sik Eum ),( Hee Soon Choi ),( Soo Hyun Choi ),( So Young Kim ),( Byung Ryong Lee ),( Jae Jin An ),( Sun Hwa Lee ),( Seung Ree Lee ),( Oh Shin Kwon ),( Hyeok Yi 생화학분자생물학회 2005 BMB Reports Vol.38 No.1
Myo-inositol monophosphate phosphatase (IMPP) is a key enzyme in the phosphoinositide cell-signaling system. This study found that incubating the 1MPP from a porcine brain with pyridoxal-5`-phosphate (PLP) resulted in a time-dependent enzymatic inactivation. Spectral evidence showed that the inactivation proceeds via the formation of a Schiff`s base with the amino groups of the enzyme. After the sodium borohydride reduction of the inactivated enzyme, it was observed that 1.8 mol phosphopyridoxyl residues per mole of the enzyme dimer were incorporated. The substrate, myo-inositol-l-phosphate, protected the enzyme against inactivation by PLP. After tryptic digestion of the enzyme modified with PLP, a radioactive peptide absorbing at 210 nm was isolated by reverse-phase HPLC. Amino acid sequencing of the peptide identified a portion of the PLP-binding site as being the region containing the sequence L-Q-V-S-Q-Q-E-D-I-T-X, where X indicates that phenylthiohydantoin amino acid could not be assigned. However, the result of amino acid composition of the peptide indicated that the missing residue could be designated as a phosphopyridoxyl lysine. This suggests that the catalytic function of IMPP is modulated by the binding of PLP to a specific lysyl residue at or near its substrate-binding site of the protein.
메틸수은으로 손상된 골모세포에 대한 NMDA 수용체길항제의 영향
하대호,양현웅,이종화,이강창 대한동의생리학회,대한동의병리학회 2003 동의생리병리학회지 Vol.17 No.2
In order to elucidate the mechanism between cytotoxicity of methhylmercuric chloride(MMC) and oxygen radicals in cultured osteoblasts of neonatal mouse, cell viability was measured by MTT assay in osteoblasts treated with 1 ~ 50 μM MMC for 30 hours. And also, the protective effect of N-methyl D-aspartate(NMDA) receptor antagonist, D-2-amino-5-phosphovaleric acid(APV) was examined by cell viability in these cultures. Cell viability was significantly decreased in dose dependency after exposure of 30μM MMC to cultured osteoblasts for 30 hours. Protective effect of APV against MMC-mediated toxicity was very effective in these cultures. From above the results, it suggests that MMC is toxic in cultured mouse osteoblasts and NMDA receptor antagonist such as APV is effective in blocking the osteotoxicity induced by MMC.
Kim, Dae-Won,Eum, Won-Sik,Choi, Hee-Soon,Kim, So-Young,An, Jae-Jin,Lee, Sun-Hwa,Sohn, Eun-Joung,Hwang, Seok-Il,Kwon, Oh-Shin,Kang, Tae-Cheon,Won, Moo-Ho,Cho, Sung-Woo,Lee, Kil-Soo,Park, Jin-Seu,Choi, Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.6
We cloned and expressed human pyridoxal-5'-phosphate (PLP) phosphatase, the coenzymatically active form of vitamin $B_6$, in Escherichia coli using pET15b vector. Monoclonal antibodies (mAb) were generated against purified human brain PLP phosphatase in mice, and four antibodies recognizing different epitopes were obtained, one of which inhibited PLP phosphatase. The binding affinities of these four mAbs to PLP phosphatase, as determined using biosensor technology, showed that they had similar binding affinities. Using the anti-PLP phosphatase antibodies as probes, we investigated their cross-reactivities in various mammalian and human tissues and cell lines. The immunoreactive bands obtained on Western blots had molecular masses of ca. 33 kDa. Similarly fractionated extracts of several mammalian cell lines all produced a single band of molecular mass 33 kDa. We believe that these PLP phosphatase mAbs could be used as valuable immunodiagnostic reagents for the detection, identification, and characterization of various neurological diseases related to vitamin $B_6$ abnormalities.
이종화 ( Joung Hwa Lee ),양현웅 ( Hyun Woong Yang ),이강창 ( Kang Chang Lee ),박상면 ( Sang Myeon Park ),김상수 ( Sang Su Kim ),서부일 ( Bu Il Seo ),강영성 ( Young Seung Kang ),김성수 ( Seung Soo Kim ),황대룡 ( Dae Ryoung Hwang 대한본초학회 2003 大韓本草學會誌 Vol.18 No.1
N/A Objectives : To clarify the myocardial toxicity of FeSO_4 in cultured rat myocardial cells, toxic effect was measured by MTT assay. Methods : Myocardial cells were incubated for 12hours in the media containing 10~80㎛ concentrations of FeSO_4. And also, the protective effect of Alli Macrostemi Bulbus(AMB) was measured in these cultures. Results : Cell viability was remarkably decreased in a dose- and time-dependent manners when cultured myocardial cells were exposed to 40 ㎛ FeSO_4 for 12hours. In the cytoprotective effect of AMB on FeSO_4-induced cytotoxicity, AMB blocked the FeSO_4-induced myotoxicity in these cultures. Conclusions : From the above results, it is suggested that FeSO_4 is toxic on cultured rat myocardial cells and AMB is effective in the prevention of FeSO_4-induced myocardial toxicity.
The Zanthoxylum schinifolium seed oil modulates immune function under the biological safety level
Seo, Joung-Wook,Park, Dae-Hun,Li, Yong-Chun,Kang, Hur-Je,Xu, Hong De,Kim, Young-Jin,Lee, Jong-Hwa,Lee, Myung-Sup,Lee, In Chul,Lee, Yun Lyul,Ahn, Jae-Bum,Cho, Soon-Chang,Lee, Min-Jae 대한독성유전단백체학회 2012 Molecular & cellular toxicology Vol.10 No.1
Zanthoxylum schinifolium (Z. schinifolium) and the seed oil of Z. schinifolium has been widely used as culinary applications and traditional medicine for epigastric pain in Korea, China, and several Asia nations and the components or extracts of Z. schinifolium have been reported to have pharmaceutical effects such as anti-platelet aggregation, inhibitory activities against monoamine oxidase, antioxidant and anticancer activities, and anti-inflammatory activity. In this study we got the results that 200 mg/kg/day seed oil of Z. schinifolium oral administration for 13 weeks enhances most immune-related cells and is biologically safe. However as B cell population was increased by Z. schinifolium seed oil administration but B cell function was not changed by that, ultimately we deduced that Z. schinifolium seed oil doesn't have the modulation effect about B cell. To evaluate the biological safety of repeated Z. schinifolium seed oil administration the index of biological safety such as CBC, hematological enzymes, and especially histopathological morphologies was measured but no changes related with Z. schinifolium seed oil administration had been shown. Conclusively Z. schinifolium seed oil is one of the safe candidates to modulate immunity.
Inactivation of Brain myo-Inositol Monophosphate Phosphatase by Pyridoxal-5'-Phosphate
Kim, Dae-Won,Hong, Joung-Woo,Eum, Won-Sik,Choi, Hee-Soon,Choi, Soo-Hyun,Kim, So-Young,Lee, Byung-Ryong,An, Jae-Jin,Lee, Sun-Hwa,Lee, Seung-Ree,Kwon, Oh-Shin,Kwon, Hyeok-Yil,Cho, Sung-Woo,Lee, Kil-Soo Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.1
Myo-inositol monophosphate phosphatase (IMPP) is a key enzyme in the phosphoinositide cell-signaling system. This study found that incubating the IMPP from a porcine brain with pyridoxal-5'-phosphate (PLP) resulted in a time-dependent enzymatic inactivation. Spectral evidence showed that the inactivation proceeds via the formation of a Schiff's base with the amino groups of the enzyme. After the sodium borohydride reduction of the inactivated enzyme, it was observed that 1.8 mol phosphopyridoxyl residues per mole of the enzyme dimer were incorporated. The substrate, myo-inositol-1-phosphate, protected the enzyme against inactivation by PLP. After tryptic digestion of the enzyme modified with PLP, a radioactive peptide absorbing at 210 nm was isolated by reverse-phase HPLC. Amino acid sequencing of the peptide identified a portion of the PLP-binding site as being the region containing the sequence L-Q-V-S-Q-Q-E-D-I-T-X, where X indicates that phenylthiohydantoin amino acid could not be assigned. However, the result of amino acid composition of the peptide indicated that the missing residue could be designated as a phosphopyridoxyl lysine. This suggests that the catalytic function of IMPP is modulated by the binding of PLP to a specific lysyl residue at or near its substrate-binding site of the protein.