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김운기,Ok-Ju Sul,곽정숙,Hye-Young Hur,Anne M. Latour,Beverly H. Koller,권병세,Choon-Soo Jeong 생화학분자생물학회 2010 Experimental and molecular medicine Vol.42 No.12
Tumor necrosis factor receptor-related 2 (TR2, HVEM or TNFRSF-14) plays an important role in immune responses,however, the mechanisms regulating its expression are unclear. To understand the control of TR2gene expression, we studied the upstream region of the gene. Gel supershift assays revealed inducible binding of nuclear factor of activated T cells (NFAT)to a putative NFAT site within the TR2 promoter. Furthermore, cotransfection of a dominant negative NFAT construct, or siRNA for NFAT, resulted in increased expression of a TR2 reporter gene. Our findings demonstrate that NFAT negatively regulates TR2expression in activated T cells.
Overexpression of developmentally regulated GTP-binding protein-2 increases bone loss
Ke, Ke,Sul, Ok-Joo,Kim, Woon-Ki,Lee, Mi-Hyun,Ko, Myung-Seok,Suh, Jae-Hee,Kim, Hyun-Ju,Kim, Shin-Yoon,Park, Jeong-Woo,Choi, Hye-Seon American Physiological Society 2013 AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND M Vol.304 No.7
<P>The developmentally regulated GTP-binding protein-2 (DRG2) is a novel subclass of GTP-binding proteins. Many functional characteristics of osteoclasts (OC) are associated with small GTPases. We hypothesized that DRG2 affects bone mass via modulating OC activity. Using DRG2 transgenic mice, we investigated the role of DRG2 in bone remodeling. DRG2 overexpression caused a decrease in bone mass and an increase in the number and activity of OC in vivo. DRG2 overexpression increased fusion, spreading, survival, and resorption activity of OC in vitro<I>.</I> Downregulation of DRG2 by siRNA decreased fusion, spreading, and survival of OC, supporting the observations found in DRG2 transgenic OC. Transgenic mature OCs were larger, with actin rings and higher ERK, Akt, Rac1 and Rho activities than wild-type OCs. Inhibition of these proteins abolished the effects of DRG2 on formation of large OCs with actin rings, implying that DRG2 affects cytoskeleton reorganization in a Rac1/Rho/ERK/Akt-dependent manner. In summary, DRG2 is associated with survival and cytoskeleton organization of OC under influence of macrophage colony-stimulating factor, and its overexpression leads to elevated bone resorptive activity of OC, resulting in bone loss.</P>
Cellulose 분해효소를 분비하는 Trichoderma sp. C-4
손영준,설옥주,정대균,한인섭,최윤재,정춘수 한국산업미생물학회 1997 한국미생물·생명공학회지 Vol.25 No.4
분해중인 볏짚으로부터 cellulase를 분비하는 곰팡이 C-4를 분리하였다. 분리된 균주의 형태적 배양적 특성을 조사한 결과 Trichoderma sp.로 분류되어 Trichoderma sp. C-4라고 명명하였다. 균을 Mandels 배지에서 6일동안 28℃에서 진탕배양한 후 배양액에 분비된 효소의 활성을 조사한 결과 CMCase 활성은 8.2 U/㎖(28.1 U/㎎), Avicelase활성은 0.75 U/㎖(2.58 U/㎎), β-glucosidase활성은 1.67 U/㎖(5.68 U/㎎)로 나타났다. 균배양 및 효소유도의 최적조건은 28℃, pH 6.2였다. 조효소는 50℃, pH 5.0에서 안정하였다. 1mM의 CsCl, LiCl, MgCl_2, CoCl_2에 대하여 CMCase활성이 영향받지 않았다. Trypsin과 chymotrypsin(2% w/w)에 의하여 10분 동안 30%의 활성이 상실되엇으나 그 후 60분 동안 더 이상의 활성 감소는 없었다. Rumen fluid에 대하여 24시간 동안 비교적 안정하였고, rumen fluid에 존재하는 효소와 CMC 및 Avicel에 대하여 각각 130% 및 118%의 상승효과를 나타내었다. During the screening of cellulase producing microorganisms, a fungal strain C-4 was selected from etiolated leaves. Based on taxonomic studies, the fungus could be classified as a strain of Trichoderma sp. When the strain C-4 was cultured in Mandel's media at 28℃ for 6 days, the enzyme activities detected in broth were as follows: 8.2 U/㎖ (28.1 U/㎎) of CMCase activity, 0.75 U/㎖ (2.58 U/㎎) of Avicelase activity, 1.67 U/㎖ (5.68 U/㎎) of β-glucosidase activity. The optimum pH for enzyme induction was 6.2. The crude enzyme retained 100% of its original CMCase activity at 50℃ for 1 hr (pH 5.0), and at 4℃ for 24 hrs (pH 5.0). There was no effect on the CMCase activity in the presence of 1 mM of CsCl, LiCl, MgCl_2 and FeCl_2, respectively. When the crude enzyme was treated with trypsin and chymotrypsin (2% w/w) for 10 minutes, the remaining CMCase activity was 70%, but there was no further loss of activity for 60 minutes treatment at 30℃. The crude enzyme showed the synergism with rumen fluid for the hydrolysis of Avicel and CMC by 118% and 130%, respectively.
새로운 섬유소분해 균주 Trichoderma sp. C-4에서 분리한 Endoglucanase (F-I-III)에 대한 연구
설옥주,정대균,한인섭,정춘수,Sul Ok Ju,Chung Dae Kyun,Han In Seob,Jeong Choon Soo 한국미생물학회 2005 미생물학회지 Vol.41 No.1
One of the endoglucanases, F-I-III, was purified from the culture filtrate of T. sp. C-4 through procedures including chromatography on Sephacryl S-200, DEAE-Sepharose A-50, and Chromatofocusing on Mono-P (FPLC). The molecular weight of the enzyme was determined to be about 56,000 Da by SDS-PAGE, and pI of 4.9 by analytical isoelectric focusing. F-I-III showed the highest enzyme activity at $55^{\circ}C$, and the pH optimum of the enzyme was 5.0. There was no loss of activity when the enzyme was incubated at $50^{\circ}C$ for 24 hours. The specific activity of the enzyme F-I-III toward the CMC was 315.4 U/mg. The Km value for $PNPG_2$ of F-I-III was 2.69 mM. N-terminal sequence of F-I-III was analyzed to be QPGTSTPEVHPKKLTTYK. It showed $95\%$ of homology to that of EGI from T. reesei. The presence of some metal ions (1 mM) had only a little effect on CMCase activity. The treatment of the reducing agents resulted in the increase of endoglucanase activity. 국내에서 분리된 우수섬유소분해 균주인 Trichodema sp. C-4가 생성하는 endoglucanase 중하나를 $(NH_4)_2SO_4$ 침전, Sephacryl S-200 gel filtration, DEAE-Sepharose A-50 ion exchange, Mono-P chromatofocusing (EPLC)의 단계로 정제하고 이를 F-I-III라 명명하였다. 분리된 효소 F-I-III는 분자량 56,000Da, 둥전점 4.9로 측정된 단일 단백질이었다. F-I-III는 $55^{\circ}C$에서 가장 높은 활성을 보였으며, pH 5.0이 반응 최적 조건이었다. $50^{\circ}C$에서 24시간 동안 안정하였으며, pH 4-7의 범위에서 안정하였다. CMC에 대한 비활성은 315.4U/mg 이었으며, PNPG2에 대한 Km 값은 2.69 mM이었다. 이 효소는 같은 균주에서 분리한 다른 endoglucanase와 exoglucanase를 섞었을 때 결정형 섬유소인 Avicel분해에 대한 상승효과를 보였다. $Mg^{2+},\;CO^{2+},\;Fe^{2+},\;Ca^{2+},\;CS^+,\;Li^+$ 등의 이온은 1 mM의 농도에서 효소의 활성에 큰 영향을 미치지 않았고, 1 mM의 환원제 (cystein, EDIA, \beta-mercaptoethanol, dithiothreitol(DTT), L-ascorbic acid)들은 효소의 활성을 증가시켰다. E-I-III의 N-말단 서열을 분석하여 QPGTSTPEVHPKKLTTYK의 서열을 얻었다. 이는 Trichodema reesei의 endoglucanase인 EGI과 $95\%$의 유사도를나타내었다. 분리된 효소 F-I-III는 높은 비활성을 가지고 있어서 활용가치가 높을 것으로 사료되었다.
김운기,Jin-Soo Park,Ok-Ju Sul,Jae-Hee Seo,최범규,Hee-Young Park,Anne M. Latour,Beverly H. Koller,권병세,Choon-Soo Jeong 한국분자세포생물학회 2011 Molecules and cells Vol.31 No.2
Previous work has suggested that the LIGHT-TR2 costimulatory pathway plays a role in the acute and chronic stages of dextran sulfate sodium (DSS)-induced colitis [Steinberg et al. (2008); Wang et al. (2005)]. To clarify the role of TNFR-related 2 (TR2) signaling in the maintenance of intestinal homeostasis, we generated a TR2 knock-out (KO) mouse. Using DSS to induce colitis, we compared the colitic symptoms and pathological changes in wild type (WT) and TR2 KO mice, and the production of cytokines by the diseased colons. We also studied the role of TR2 in suppressing innate and adaptive immunity in the DSS model. TR2 deficient mice were characterized by reduced symptoms of intestinal inflammation compared with wildtype mice, and reduced production of cytokines. We therefore generated a monoclonal antibody against mouse TR2 which was specific to TR2 and capable of blocking TR2 signals. With this antibody, we demonstrated that antagonizing TR2 during the development of DSS-induced colitis reduced the symptoms of inflammation. Our findings suggest that TR2 is an important mediator in colitis, and may serve as a therapeutic target in inflammatory bowel disease.
Kim, Seok-Hyung,Lee, Ok-Jun,Kwon, Ju-Lee,Kim, Jin Man,Sul, Hae-Joung,Song, Kyu Sang,Kim, Kyung-Hee Potamitis Press 2015 Anticancer research Vol.35 No.7
<P>To investigate whether differential expression of Yes-associated protein (YAP) and 관-catenin is important in gastric carcinogenesis.</P>
Kim, Woon-Ki,Sul, Ok-Ju,Kwak, Jung-Sook,Hur, Hye-Young,Latour, Anne M.,Koller, Beverly H.,Kwon, Byoung-S.,Jeong, Choon-Soo Korean Society for Biochemistry and Molecular Bion 2010 Experimental and molecular medicine Vol.42 No.12
Tumor necrosis factor receptor-related 2 (TR2, HVEM or TNFRSF-14) plays an important role in immune responses, however, the mechanisms regulating its expression are unclear. To understand the control of TR2 gene expression, we studied the upstream region of the gene. Gel supershift assays revealed inducible binding of nuclear factor of activated T cells (NFAT) to a putative NFAT site within the TR2 promoter. Furthermore, cotransfection of a dominant negative NFAT construct, or siRNA for NFAT, resulted in increased expression of a TR2 reporter gene. Our findings demonstrate that NFAT negatively regulates TR2 expression in activated T cells.
Ke, Ke,Kim, Woon-Ki,Sul, Ok-Joo,Phan, Van Tien,Lee, Mi-Hyun,Kim, Hyun-Ju,Kim, Shin-Yoon,Choi, Hye-Seon American Physiological Society 2012 AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND M Vol.303 No.11
<P>The aim of the present study was to evaluate the effect of fibrinogen on number and function of osteoclasts (OC) consequently resulting in bone loss. It was hypothesized that the enhanced level of released fibrinogen due to loss of ovarian function caused bone loss by acting on OCs. Bone loss was induced by ovariectomy (OVX) in mice and analyzed by micro-CT. The effect of fibrinogen on OCs was evaluated by tartrate-resistant acid phosphatase, annexin V, actin staining, pit formation observed on dentine slices, and Western blotting. Exogenous fibrinogen increased OC survival, actin ring formation, and bone resorption in vitro. The effect of fibrinogen was dependent on β(3)-integrin, which is a marker for mature OCs. Fibrinogen induced the activation of transforming oncogene from Ak strain (Akt), Ras-related C3 botulinum toxin substrate 1 (Rac1), and Rho family of GTPase (Rho) and the degradation of the Bcl-2 interacting mediator of cell death (Bim) in a manner similar to macrophage colony-stimulating factor (M-CSF). OVX increased plasma fibrinogen and serum M-CSF together with elevated actin ring formation and bone loss. The increased fibrinogen level due to loss of ovarian function may contribute, at least partly, to bone loss through the enhanced number and activity of OCs.</P>