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( Yong Song Gho ) 대한간학회 2016 춘·추계 학술대회 (KASL) Vol.2016 No.1
Communication between cells and environment is an essential process in living organisms. The secretion of extracellular vesicles, also known as exosomes and microvesicles is a universal cellular process occurring from simple organisms to complex multicellular organisms, including humans. Throughout evolution, both prokaryotic and eukaryotic cells have adapted to manipulate extracellular vesicles for intercellular communication via outer membrane vesicles in the case of Gram-negative bacteria and ectosomes (also known as microvesicles) or exosomes in eukaryotic cells. Recent progress in this area has revealed that extracellular vesicles play multiple roles in intercellular and interspecies communication, suggesting that extracellular vesicles are NanoCosmos, i.e., extracellular organelles that play diverse roles in intercellular communication (http://evpedia.info). This presentation focuses on the comprehensive aspects of mammalian and bacterial extracellular vesicles including components, biogenesis, and diverse functions that should facilitate further applications, especially to develop diagnostic tools, liver regeneration, and therapeutics including our recent progress in novel exosome-mimetic technology for targeted delivery of chemotherapeutics and siRNA as well as for adjuvant-free, non-toxic vaccine delivery system against bacterial infection.
Naphthazarin Derivatives (Ⅶ): Antitumor Action against ICR Mice Bearing Ascitic S-180 Cells
Song, Gyu-Yong,Kim, Yong,You, Young-Jae,Gho, Hoon,Ahn, Byung-Zun The Pharmaceutical Society of Korea 2001 Archives of Pharmacal Research Vol.24 No.1
Various analogues of 5,8-dimethoxy-1,4-naphthoquinone (DMNQ) such as 2- or 6-(1-hydro-xyiminoalkyl)-DMNQs were prepared and evaluated for the antitumor action. (1-Hydroxyiminoalkyl)-DMNQ derivatives expressed greater antitumor action than (1 -hydroxyalkyl)- or acyl-DMNQ derivatives. Moreover, 6-(1-hydroxyiminoalkyl)-DMNQ derivatives expressed higher anti-tumor action than 2-sudstituted ones, suggestive of a steric effect. Some of 6-(1-propyloxyalkyl)-DMNQ derivatives with an alkyl group of butyl to octyl moiety showed T/C values of > 400 %.
고초균에서 3 - 메칠아데닌 DNA 글아이코실라아제의 분리 및 특성
고용송,한범희,양철학 ( Yong Song Gho,Bom He Han,Chul Hak Yang ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.3
An inducible enzyme which releases primarily 3-methyladenine from alkylated DNA was partially purified from Bacillus subtilis by using DEAE-cellulose and DNA-cellulose chromatography and designated as 3-methyladenine DNA glycosylase. It released 3-methyl-adenine and 7-methylguanine from DNA methylated with N-methyl-N-nitrosourea (MNU). 3-methyladenine (3-meA) was released 30 times faster than 7-methylguanine (7-meG). No detectable amount of O^6-methylguanine (O^6-meG) was released. The glycosylase activity was inhibited by neither free 3-meA nor 7-meG but was stimulated by spermidine. Apparent molecular weight was 30,000 on SDS polyacrylamide gel electrophoresis and 23,000 on Sephadex G-100 gel filtration. Its pI was 4.7 on column electrofocusing. Unlike the 3-methyladenine DNA glycosylases in Escherichia coli, no evidence for the presence of two different enzymes was found. The enzyme exhibited a preference for double-stranded alkylated DNA to the single stranded one. Apparent K_m for substrate DNA was 5.15×10^(-8)M. Addition of 1 mM EDTA slightly decreased the activity. Addition of 2 mM Mg^(2+) and Ca^(2+) stimulated base release, while 2 mM Co^(2+) and Mn^(2+) inhibited it. Optimum pH for the enzyme reaction was pH 6.7-7.5. The enzyme activity was quite sensitive to temperature and had a sharp optimum at 37℃. The enzyme was inactivated by N-ethylmaleimide and p-chloromercuribenzoate which was known as a sulfhydryl reagents.
Purification and Characterization of 3-Methyladenine DNA Glycosylase from Bacillus Subtilis
고용송,한범희,양철학,Gho, Yong-Song,Han, Bom-Ie,Yang, Chul-Hak 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.3
알킬화된 DNA로부터 주로 3-메칠아데닌을 제거하는 유발성 효소를 고초균으로부터 DEAE-셀루로오즈와 DNA-셀루로오즈 크로마토그래피법을 사용하여 부분적으로 분리하고 이를 3-메칠아데닌 DNA 글라이코실라아제로 명명하였다. 이 효소는 N-메칠-N-니트로소유리아로 메칠화된 DNA 기질로부터 3-메칠아데닌과 3-메칠구아닌을 제거하였다. 이 때 3-메칠아데닌은 7-메칠구아닌 보다 30배나 빨리 제거되었다. 이 효소는 $O^6$-메칠구아닌은 제거시키지 못하였다. 이 효소의 활동도는 3-메칠아데닌이나 7-메칠구아닌에 의해 방해되지는 않았으며 스퍼미딘에 의해 그 활동도가 증가되었다. 이 효소의 분자량은 SDS 아크릴아미드 젤 전기영동법에 의하면 30,000 정도이었고, 셰파덱스 G-100의 젤 여과법에 따르면 23,000으로 나타났다. 효소의 등전점은 등전초점화 콜럼에서 4.7로 나타났다. 두개의 3-메칠아데닌 DNA 글라이코실라아제가 존재하는 대장균과는 달리 고초균에는 한 형태의 효소만 존재함을 확인하였다. 또한 고초균 3-메칠아데닌 DNA 보다 겹가닥 알킬화된 DNA를 선호하였다. 기질을 알킬화된 DNA를 사용했을 때 $K_m$값은 $5.15{\times}10^{-8}M$이었다. 1 mM의 EDTA 존재하에 효소의 활동도는 약간 감소하였고 2mM $Mg^{2+}$와 $Ca^{2+}$의 존재하에 베이스의 제거가 증가되는 한편 2mM의 $Co^{2+}$와 $Mn^{2+}$은 효소의 활동도를 방해하였다. 이 효소반응의 pH 적정점은 pH6.7-7.5이었고 온도에 대해 특히 민감하였고 $37^{\circ}C$에서 예민한 적정점을 나타내었다. 이 효소는 썰퍼하이드릴 그룹에 반응하는 N-메칠말레이미드와 p-클로로머큐리벤조에 의해 불활성화되었다. An inducible enzyme which releases primarily 3-methyladenine from alkylated DNA was partially purified from Bacillus subtilis by using DEAE-cellulose and DNA-cellulose chromatography and designated as 3-methyladenine DNA glycosylase. It released 3-methyl-adenine and 7-methylguanine from DNA methylated with N-methyl-N-nitrosourea (MNU). 3-methyladenine (3-meA) was released 30 times faster than 7-methylguanine (7-meG). No detectable amount of $O^6$-methylguanine ($O^6$-meG) was released. The glycosylase activity was inhibited by neither free 3-meA nor 7-meG but was stimulated by spermidine. Apparent molecular weight was 30,000 on SDS polyacrylamide gel electrophoresis and 23,000 on Sephadex G-100 gel filtration. Its pI was 4.7 on column electrofocusing. Unlike the 3-methyladenine DNA glycosylases in Escherichia coli, no evidence for the presence of two different enzymes was found. The enzyme exhibited a preference for double-stranded alkylated DNA to the single stranded one. Apparent $K_m$ for substrate DNA was $5.15{\times}10^{-8}M$. Addition of 1 mM EDTA slightly decreased the activity. Addition of 2 mM $Mg^{2+}$ and $Ca^{2+}$ stimulated base release, while 2 mM $Co^{2+}$ and $Mn^{2+}$ inhibited it. Optimum pH for the enzyme reaction was pH 6.7-7.5. The enzyme activity was quite sensitive to temperature and had a sharp optimum at $37^{\circ}C$. The enzyme was inactivated by N-ethylmaleimide and p-chloromercuribenzoate which was known as a sulfhydryl reagents.
Proteome analysis of outer membrane vesicles from a clinical<i>Acinetobacter baumannii</i>isolate
Kwon, Sang-Oh,Gho, Yong Song,Lee, Je Chul,Kim, Seung Il Oxford University Press 2009 FEMS microbiology letters Vol.297 No.2
<P>The secretion of outer membrane vesicles (OMVs) is one of the major mechanisms by which Gram-negative bacteria deliver effector molecules to host cells. Acinetobacter baumannii is an important opportunistic pathogen in hospital-acquired infections, but the secretion system for effector molecules to induce host cell damage has not been characterized. In the present study, we investigated the secretion of OMVs from a clinical A. baumannii isolate and analyzed the comprehensive proteome of A. baumannii-derived OMVs. Acinetobacter baumannii secreted OMVs into the extracellular milieu during in vitro growth. Using 1-DE and LC-MS/MS protein identification and assignment analysis, 132 different proteins associated with OMVs were identified. These proteins were derived from outer membranes (n=26), periplasmic space (n=6), inner membranes (n=8), cytoplasm (n=43), and unknown localization or multiple localization sites (n=49) according to the cell location prediction programs. Among the proteins associated with OMVs, a potent cytotoxic molecule, outer membrane protein A, was highly enriched and several putative virulence-associated proteins were also identified. These results suggest that OMVs from A. baumannii are an important vehicle designed to deliver effector molecules to host cells.</P>