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음원식,In Soon Choung,A Yeon Kim,Yong Je Lee,Jung Hoon Kang,Jinseu Park,Kil Soo Lee,Hyeok Yil Kwon,최수영 한국분자세포생물학회 2002 Molecules and cells Vol.13 No.2
We previously reported that Tat-Cu,Zn-superoxide dismutase (Tat-SOD) can be directly transduced into mammalian cells across the lipid membrane barrier. To enhance the therapeutic potential of Tat-SOD for the treatment of various disorders that are related to this antioxidant enzyme, the transduction efficacy of Tat-SOD should be heightened. Therefore, we investigated whether copper ion recovery of the fusion protein could enhance the transduction potential of Tat- SOD in cultured HeLa cells. The results showed that the transduction potential of Tat-SOD was markedly enhanced by copper ions, and moderately increased by zinc ions. Compared with Tat-SOD, the Tat-SOD that recovered the copper ion (CR-Tat-SOD) achieved a significant increase in intracellular concentration and enzymatic activity. Therefore, CR-Tat-SOD was transduced into HeLa cells in a rapid saturation manner, but Tat-SOD was shown in a time-dependent manner. With the higher transduction efficacy of CR-Tat-SOD than that of Tat-SOD, the transduced CR-Tat-SOD significantly increased the viability of HeLa cells that were pretreated with paraquat, an intracellular superoxide anion generator. Although the mechanism of the enhanced transduction of Tat-SOD by copper ions is still unanswered, these results indicate that copper ions facilitate the transduction of SOD. These then significantly increase the biological effectiveness of this antioxidant enzyme.
TPA로 유도된 마우스 귀 부종 동물모델에서 소목추출물의 항염증 효과
음원식(Won Sik Eum),이광재(Kwang-Jae Lee),김대원(Dae Won Kim),임순성(Soon Sung Lim),강일준(Il-Jun Kang),박진서(Jinseu Park),최수영(Soo Young Choi) 한국식품영양과학회 2013 한국식품영양과학회지 Vol.42 No.3
본 연구를 통하여 TPA로 유도한 마우스 귀 부종 염증반응에 대한 소목추출물의 항염증 효능과 기전을 확인하였다. 소목추출물은 TPA로 유도한 마우스 귀 부종을 억제하였으며, TPA에 의한 염증관련 단백질인 COX-2 발현 및 cytokine(IL-6, TNF-α 그리고 IL-1β)의 mRNA 발현을 현저히 감소시켰다. 또한 TPA에 의한 NF-κB 및 MAPK의 활성을 억제하였다. 본 연구 결과, 소목추출물은 NF-κB 및 MAPK의 신호전달을 억제함으로서 항염증 효능을 나타내었다. This study investigated the anti-inflammatory effects of extracts from Caesalpinia sappan L. (CSL) on 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced ear edema in mice. Skin inflammation was detected by immunohistochemistry and the protein and mRNA expression levels of cyclooxygenase-2 (COX-2) and cytokines (IL-6, IL-1β and TNF-α) detected by Western blotting and RT-PCR. The activation of nuclear factor-kappa B (NF-κB) and mitogen-activated protein kinase (MAPK) were analyzed by Western blotting. CSL extracts markedly inhibited the TPA-induced expression of COX-2 and pro-inflammatory cytokines. Also, CSL extracts significantly reduced the activation of NF-κB and MAPK. These results suggest that CSL extracts may serve as therapeutic agents against skin diseases related to inflammation.
김승섭,경인구,이미라,김동구,신지영,양진이,이광호,음원식,강정훈 한국유화학회 2014 한국응용과학기술학회지 Vol.31 No.4
노루궁뎅이 버섯균사체(Hericium erinaceum)를 인진쑥(Artemisia capillaris)에 배양하여 조제한 AC-HE 열수 추출물이 생체고분자의 산화적 손상과 세포사멸을 보호할 수 있는 지를 관찰하였다. AC-HE의 항산화 활성을 DPPH radical, ABTS radical, peroxyl radical 소거활성 측정을 통해 알아보았다. 그 결과 DPPH radical 소거활성은 500μg/mL 농도에서 61.73%, ABTS radical 소거활성은 250μg/mL 농도에서 97.39%, peroxyl radical 소거활성은 100μg/mL 농도에서 44.18%로 나타났다. AC-HE은 DNA의 산화적 손상을 효과적으로 억제하였다. 또한 생체고분자물질인 사람의 혈청단백질의 산화적 손상을 억제하였다. 세포에 H2O2를 처리하였을 때 세포생존율에 비하여 발효물을 100μg/mL 농도로 전 처리한 세포생존율은 11.47% 증가했으며, 발효물을 50μg/mL 농도로 처리했을 경우 세포내 ROS의 축적이 유의적으로 감소되었다. 따라서 AC-HE은 항산화 활성뿐만 아니라 산화적 스트레스에 의해 야기되는 세포 독성에 대한 보호 작용이 뛰어난 것으로 사료되었다. The hot water extract from Artemisia capillaris fermented with Hericium erinaceum mycelium (AC-HE) were assessed for the protection against oxidative modification of biological macromolecules and cell death. Antioxidant activity of AC-HE evaluated using 2,2-diphenyl-1-picrylhydrazyl radical, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) radical and peroxyl radical scavenging assays. AC-HE showed 61.73% DPPH radical scavenging activity at 500μg/mL, 97.39% ABTS radical scavenging activity at 250μg/mL, and 44.18% peroxyl radical scavenging activity at 100μg/mL. AC-HE were shown to significantly inhibited DNA strand breakage induced by peroxyl radical. AC-HE also prevented peroxyl radical-mediated human serum albumin modification. AC-HE effectively inhibited H2O2 induced cell death and significantly increased of the 11.47% cell survival at 100μg/mL. AC-HE also decreased intracellular reactive oxygen species (ROS) levels in H2O2-treated cells. The results suggested that AC-HE can contribute to antioxidant and protected cells from oxidative stress-induced cell injury.
Transduced Tat-SOD Fusion Protein Protects Against Ischemic Brain Injury
김대원,최수영,음원식,장상호,김소영,최희순,최수현,안재진,이선화,이길수,한규형,강태천,원무호,강정훈,권오신,조성우,김태윤,박진서 한국분자세포생물학회 2005 Molecules and cells Vol.19 No.1
Reactive oxygen species (ROS) are implicated in reper-fusion injury after transient focal cerebral ischemia. The antioxidant enzyme, Cu,Zn-superoxide dismutase (SOD), is one of the major means by which cells coun-teract the deleterious effects of ROS after ischemia. Re-cently, we reported that when Tat-SOD fusion protein is transduced into pancreatic cells it protects the cells from destruction by relieving oxidative stress in ROS-implicated diabetes (Eum et al., 2004). In the present study, we investigated the protective effects of Tat-SOD fusion protein against neuronal cell death and ischemic insults. When Tat-SOD was added to the culture me-dium of neuronal cells, it rapidly entered the cells and protected them against paraquat-induced cell death. Immunohistochemical analysis revealed that Tat-SOD injected intraperitoneally (i.p.) into mice has access to various tissues including brain neurons. When i.p. in-jected into gerbils, Tat-SOD prevented neuronal cell death in the hippocampus in response to transient fore-brain ischemia. These results suggest that Tat-SOD pro-vides a strategy for therapeutic delivery in various hu-man diseases, including stroke, related to this anti-oxidant enzyme or to ROS.
Ginsenosides Enhance the Transduction of Tat-Superoxide Dismutase into Mammalian Cells and Skin
최수영,김대원,음원식,장상호,Chang Sik Yoon,최희순,Soo Hyun Choi,Young Hoon Kim,So Young Kim,Eun Shil Lee,Nam-In Baek,Hyeok Yil Kwon,Jin Hi Choi,Yoon Chul Choi,Oh-Shin Kwon,조성우,Kyuhyung Han,Kil Soo Lee,Jinseu Park 한국분자세포생물학회 2003 Molecules and cells Vol.16 No.3
박진서,최수영,음원식,장상호,김대원,최희순,Soo Hyun Choi,So Young Kim,Jae Jin An,Sun Hwa Lee,한규형,Jung Hoon Kang,강태천,원무호,Yong Joon Cho,Jin Hi Choi,Tae Yoon Kim 한국분자세포생물학회 2005 Molecules and cells Vol.19 No.2
The human immunodeficiency virus type 1 (HIV-1) Tat protein transduction domain (PTD) is responsible for highly efficient protein transduction across plasma membranes. In a previous study, we showed that Tat- Cu,Zn-superoxide dismutase (Tat-SOD) can be directly transduced into mammalian cells across the lipid membrane barrier. In this study, we fused the human SOD gene with a Tat PTD transduction vector at its N- and/or C-terminus. The fusion proteins (Tat-SOD, SOD-Tat, Tat-SOD-Tat) were purified from Escherichia coli and their ability to enter cells in vitro and in vivo compared by Western blotting and immunohistochemistry. The transduction efficiencies and biological activities of the SOD fusion protein with the Tat PTD at either terminus were equivalent and lower than the fusion protein with the Tat PTD at both termini. The availability of a more efficient SOD fusion protein provides a powerful vehicle for therapy in human diseases related to this anti-oxidant enzyme and to reactive oxygen species.
Tat-mediated Protein Transduction of Human Brain Pyridoxine-5-POxidase into PC12 Cells
최수영,박진서,이선화,이길수,음원식,조성우,원무호,권오신,강태천,Seok-Il Hwang,Soo Hyun Choi,김대원,Jae Jin An,So Young Kim 한국생화학분자생물학회 2006 BMB Reports Vol.39 No.1
Pyridoxine-5-P oxidase catalyses the terminal step in thebiosynthesis of pyridoxal-5-P, the biologically active formof vitamin B6 Which acts as an essential cofactor. Here, ahuman brain pyridoxine-5-P oxidase gene was fused with agene fragment encoding the HIV-1 Tat protein transductiondomain (RKKRRQRRR) in a bacterial expression vectorto produce a genetic in-frame Tat-pyridoxine-5-P oxidasefusion protein. Expressed and purified Tat-pyridoxine-5-Poxidase fusion protein transduced efficiently into PC12cells in a time- and dose-dependent manner when addedexogenously to culture media. Once inside the cells, thetransduced Tat-pyridoxine-5-P oxidase protein showedcatalytic activity and was stable for 48 h. Moreover, theformation of pyridoxal-5-P was increased by adding exogenousTat-pyridoxine-5-P oxidase to media pre-treated with thevitamin B6 precursor pyridoxine. In addition, the intracellularconcentration of pyridoxal-5-P was markedly increasedwhen Tat-pyridoxal kinase was transduced together withTat-pyridoxine-5-P oxidase into cells. These results suggestthat the transduction of Tat-pyridoxine-5-P oxidase fusionprotein presents a means of regulating the level ofpyridoxal-5-P and of replenishing this enzyme in variousneurological disorders related to vitamin B6.
Immunohistochemical Studies of Human Ribosomal Protein S3 (rpS3)
최수영,박진서,원무호,강태천,음원식,김준,최수현,김소영,안재진,이선화,김대원 한국생화학분자생물학회 2006 BMB Reports Vol.39 No.2
The human ribosomal protein S3 (rpS3) was expressed in E. coli using the pET-15b vector and the monoclonal antibodies (mAbs) were produced and characterized. A total of five hybridoma cell lines were established and the antibodies recognized a single band of molecular weight of 3 3 k D a o n i m m u n o b l o t w i t h p u r i f i e d r p S 3 . W h e n t h e purified rpS3 was incubated with the mAbs, the UV endonuclease activity of rpS3 was inhibited up to a maximum of 49%. The binding affinity of mAbs to rpS3 determined by using a biosensor technology showed that they have similar binding affinities. Using the anti-rpS3 antibodies as probes, we investigated the cross-reactivities of various other mammalian brain tissues and cell lines, including human. The immunoreactive bands on Western blots appeared to be the same molecular mass of 33 kDa in all animal species tested. They also appear to be extensively cross-reactive among different organs in rat. These results demonstrated that only one type of immunologically similar rpS3 protein is present in all of the mammalian brain tissues including human. Furthermore, these antibodies were successfully applied in immunohistochemistry in order to detect rpS3 in the gerbil brain tissues. Among the various regions in the brain tissues, the rpS3 positive neurons were predominantly observed in the ependymal cells, hippocampus and substantia nigra pars compacta. The different distributions of rpS3 in brain tissues reply that rpS3 protein may play an important second function in the neuronal cells