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혈관형성 조절물질 탐색을 위한 제브라피쉬 동물모델의 이용
소주훈,최태영,권병목,김철희 충남대학교 생물공학연구소 2004 생물공학연구지 Vol.10 No.2
The zebrafish (Danio rerio) is now the prominent vertebrate model system for clarification of the roles of specific genes and signaling pathways in development. Zebrafish embryos provide many advantages for experimental and genetic analysis of vascular development. In this study we describe the use of zebrafish model system for the experimental study of angiogenesis. We established several technical methods to define cellular and molecular alterations in vascular development; whole-mount in situ hybridization, microangiography, and alkaline phosphatase staining. We also introduced the overexpression experiments by using in vitro-transcribed synthetic mRNAs and vascular-specific gene promoters. For the gene knock-down analyses, we challenged morpholino antisense oligonucleotide system. With these efforts, the zebrafish might be used as a powerful tool for the screening of effective angiogenic factors.
RHOMBENONE : FARNESYL PROTEIN TRANSFERASE INHIBITOR FROM THE LEAVES OF HEDERA RHOMBEA BEAN
Kwon, Byoung-Mog,Lee, Seung-Ho,Kim, Kyung-Sook,Lee, Ihn-Rhan,Lee, Un Chul,Hong, Su-Hyung,Bok, Song-Hae 梨花女子大學校 藥學硏究所 1998 藥學硏究論文集 Vol.- No.7
Rhombenone, a new dammarane analogue containing an 25-oxo, which inhibits farnesyl protein transferase (FPTase), was isolated from the leaves of Hedera rhombea Bean. Additional related dammaranes were also evaluated for FPTase inhibition.
Kwon, Byoung Mog,Bae, Yun Soo,Han, Mi Young,Park, Young Mee,Yoo, Ji Yun,Lee, Sang Seop,Lee, Kyung Im,Jeong, Moon Jin 생화학분자생물학회 1998 BMB Reports Vol.34 No.6
In the present study, an in vitro ELISA system to assess the interaction between Src homology (SH)2 domains and phosphotyrosine that contain peptides was established using purified GST-conjugated SH2 proteins and synthetic biotinylated phosphotyrosine that contain oligopeptides. The SH2 domains bound the relevant phosphopeptides that were immobilized in the streptavidin-coated microtiter plate in a highly specific and dose-dependent manner. The epidermal growth factor receptor (EGFR)-, T antigen (T Ag)-, and platelet-derived growth factor receptor (PDGFR)-derived phosphopeptides interacted with the growth factor receptor binding protein (Grb)2/ SH2, Lck/SH2, and phosphatidyl inositol 3-kinase (PI3K) p85/SH2, respectively. No cross-reactions were observed. Competitive inhibition experiments showed that a short phosphopeptide of only four amino acids was long enough to determine the binding specificity. Optimal concentrations of the GST-SH2 fusion protein and phosphopeptide in this new ELISA system for screening the binding blockers were chosen at 2nM and 500nM, respectively. When two candidate compounds were tested in our ELISA system, they specifically inhibited the Lck/ SH2 and/or p85/SH2 binding to the relevant phosphopeptides. Our results indicate that this ELISA system could be used as an easy screening method for the discovery of specific binding blockers of protein-protein interactions via SH2 domains.
Synthesis and In Vitro Cytotoxicity of Cinnamaldehydes to Human Solid Tumor Cells
Kwon, Byoung-Mog,Lee, Seung-Ho,Choi, Sang-Un,Park, Sung-Hee,Lee, Chong-Ock,Cho, Young-Kwon,Sung, Nack-Do,Bok, Song-Hae 忠南大學校 癌共同硏究所 1998 癌共同硏究所 硏究誌 Vol.2 No.1
Cinnamaldehydes and related compounds were synthesized from various cinnamic acids based on the 2'-hydroxycinnamaldehyde isolated from the bark of Cinnamomum cassia Blume. The cytotoxicity to human solid tumor cells such as AS49, SK-OV-3, SK-MEL-2, XF498 and HCT1 5 were measured. Cinnamic acid, cinnamates and cinnamyl alcohols did not show any cytotoxicity against the human tumor cells. Cinnamaldehydes and realted compounds were resistant to AS49 cell line up to 15 μg/ml. In contrast, HCT15 and SK-MEL-2 cells were much sensitive to these cinnamaldehyde analogues which showed ED_(50) values 0.63~8.1 μg/ml. Cytotoxicity of the saturated aldehydes was much weak compared to their unsaturated aldehydes. From these studies, it was found that the key functional group of the cinnamaldehyde-related compounds in the antitumor activity is the propenal group.
Kwon, Byoung-Mog,Cohen, Scot,Myers, Andrew G. 충남대학교 약학대학 의약품개발연구소 1993 藥學論文集 Vol.9 No.-
The rate of reaction of chlicheamiciny Ⅰ with 2-aminoethanethioⅠ at pH=7.4 in the presence of DNA was found to be approximately one order of magnitude greater than the rate in the absence of DNA. This result is consistent with the hypothesis of base catalysis of thiol activation by DNA. The products from reactions in the presence of DNA were different than from reactions in the absence of DNA. A speculative rational is that chlicheamicin is activated while bound to DNA and affords a different product distribution than calicheamiciny Ⅰactivated free in solution.
Synthesis and In Vitro Cytotoxicity of Cinnamaldehydes to Human Solid Tumor Cells
Kwon, Byoung-Mog,Lee, Seung-Ho,Choi, Sang Un,Park, Sung Hee,Lee, Chong Ock,Cho, Young-Kwon,Sung, Nack-Do,Bok, Song-Hae 충남대학교 생물공학연구소 1999 생물공학연구지 Vol.7 No.-
Cinnamaldehydes and related compounds were synthesized from various cinnamic acids based on the 2'-hydroxycinnamaldehyde isolated from the bark of Cinnamomum cassia Blume. The cytotoxicity to human solid tumor cells such as A549, SK-OV-3, SK-MEL-2, XF498 and HCT15 were measured Cinnamic acid, cinnamates and cinnamyl alcohols did not show any cytotoxicity against the human tumor cells. Cinnamaldehydes and realted compounds were resistant to A549 cell line up to 15 ㎍/ml. In contrast, HCT15 and SK-MEL-2 cells were much sensitive to these cinnamaldehyde analogues which showed ED_50 values 0.63∼8.1 ㎍/ml. Cytotoxicity of the saturated aldehydes was much weak compared to their unsaturated aldehydes. From these studies, it was found that the key functional group of the cinnamaldehyde-related compounds in the antitumor activity is the propenal group.
2'-Hydroxycinnamaldehyde from Stem Bark of Cinnamomum cassia
Kwon, Byoung-Mog,Cho, Young-Kwon,Lee, Seung-Ho,Nam, Ji-Youn,Bok, Song-Hae,Chun, Soo-Kyoung,Kim, Jeong-Ah,Lee, Ihn-Rhan 梨花女子大學校 藥學硏究所 1997 藥學硏究論文集 Vol.- No.6
2'-Hydroxycinnamaldehyde, which inhibits farnesyl-protein transferase (FPTase), has been isolated from the stem bark of Cinnamomum cassia Blume. The biologically active agent in the extract has been purified by silica column chromatography and HPLC. The structure of the isolated compound was elucidated on the basis of 500㎒ NMR experiments.