https://scholar.dgist.ac.kr/handle/20.500.11750/329 2026-08-10T13:48:49Z https://scholar.dgist.ac.kr/handle/20.500.11750/60581 Title: IL-2 표면 발현 세포외 소포체를 유효성분으로 포함하는 암 질환 예방 또는 치료용 조성물 Author(s): 예경무; 정도경; 백문창 Abstract: The present invention relates to a composition for preventing or treating cancer, the composition containing IL-2 surface expression-extracellular vesicles as an active ingredient. According to the present invention, immune cells, in which useful cytokines have been expressed on the cell surface, and extracellular vesicles, preferably small extracellular vesicles (sEV), which are derived from the immune cells and have useful cytokines expressed on the surface were prepared using a lentiviral vector containing a cytokine-linker-a PDGF receptor transmembrane domain, and it was found that the extracellular vesicles increased proliferation and activity of cytotoxic T cells thereby increasing anti-cancer immune efficacy. Thus, the extracellular vesicles having the efficacy can be usefully utilized as a pharmaceutical composition for preventing or treating cancer, a pharmaceutical composition for co-administration with an anticancer drug, or a composition for delivering a drug or a physiologically active material. https://scholar.dgist.ac.kr/handle/20.500.11750/60574 Title: 비만의 예방 또는 치료용 약학 조성물 Author(s): 오병무; 정영태 Abstract: 본 발명은 비만의 예방 또는 치료용 약학 조성물 또는 식품 조성물에 관한 것으로, 본 발명은 Keap1 유전자가 제거된 NK세포를 포함하여, 체중, 장기 무게, 지방 조직 무게, 혈청지오티(AST), 혈청지피티(ALT), 혈중 콜레스테롤(TCHOL) 또는 저밀도지단백(LDL)을 현저히 낮출 수 있다. 따라서, 본 발명의 Keap1 유전자가 제거된 NK세포를 포함하는 조성물은 대상의 체중 조절에 용이하게 사용될 수 있어, 미용, 축산, 의료 분야 등에 유용하게 사용될 수 있으며, 특히 비만 및 이의 동반진단의 개선, 예방 및 치료를 위한 식품 첨가물, 건강기능식품 및 치료제 분야 등에 유용하게 사용될 수 있다. https://scholar.dgist.ac.kr/handle/20.500.11750/60550 Title: Constitutive DUSP2 expression enhances lymphoid cell proliferation by activating CDK1 and promotes lymphomagenesis Author(s): Qian, Yu; Panaampon, Jutatip; Chapuy, Bjoern; Zhang, Xueyan; Zhao, Xiujuan; Wang, Zhe; Zhang, Pengfei; Payungwong, Tongchai; Zhang, Aretina; Ke, Qiang; Zhong, Jing; Yuan, Ping; Zhang, Lei; Hong, Min; Choi, Il-Kyu; Guan, Jiankun; Calado, Dinis Pedro; Rodig, Scott; Pozdnyakova, Olga; Rajewsky, Klaus; Godinho, Susana A.; Jirawatnotai, Siwanon; Wu, Hao; Shipp, Margaret A.; Dougan, Stephanie K.; Zhang, Baochun Abstract: DUSP2 is known as a nuclear dual-specificity phosphatase, highly restricted to immune cells. Its expression is induced by antigenic and mitogenic stimuli and has been implicated in immune cell differentiation and functions. However, its role in immune cell mitotic proliferation and hematologic malignancies has not been rigorously examined. Here, we show DUSP2 is highly expressed in human B-cell, T cell, and other hematologic malignancies. Ablating DUSP2 expression in lymphoma cell lines decreases growth and viability. In mice, transgenic Dusp2 expression promotes B-cell and T cell proliferation, and malignant transformation. Mechanistically, DUSP2 promotes cell cycle progression by activating CDK1 through dephosphorylation at inhibitory Tyr15 and Thr14, which is mediated not by its own phosphatase activity, but instead by a structural motif that recruits CDC25 phosphatases. This work reveals an unexpected oncogenic role for DUSP2 in lymphoid malignancies and the function of a structural motif, which represents an appealing target site for therapeutic intervention. 2026-06-30T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/60516 Title: Expression and purification of the ectodomain of erythropoietin receptor fused to mCitrine or mTFP1 fluorescent protein in Escherichia coli Author(s): 강은호; Ashim Janbolat; Ji, Sangho; Han, Min Ae; Yu, Wookyung; Kim, Sung Jae; Hong, Eunmi; Moon, Cheil; Lee, Chang-Hun Abstract: The erythropoietin receptor (EPOR) is a single-pass transmembrane protein that homo-dimerizes upon binding with its renal ligand erythropoietin (EPO) to trigger downstream signaling. Its extracellular ectodomain mediates ligand binding. Therefore, a fusion protein of the EPOR ectodomain can be useful for various in vitro assays, such as a binding assay with an EPO-like peptide, if overexpressed in Escherichia coli (E.coli). In this study, we hypothesized that fusion proteins of the EPOR ectodomain with mCitrine or mTFP1, expressed in bacteria, could enable in vitro Fo & uml;rster resonance energy transfer experiments. Two fusion proteins, EPOR-mCitrine and EPORmTFP1, were overexpressed in E. coli but obtained as inclusion bodies. Urea solubilization and stepwise dialysis yielded soluble fusion proteins. Circular dichroism spectroscopy revealed that EPOR-mCitrine had greater secondary structure content than EPOR-mTFP1. When combined with recombinant human EPO, the hydrodynamic radius of EPOR-mCitrine changed, as measured using dynamic light scattering, confirming binding. This interaction was further validated using isothermal titration calorimetry. We propose that bacterially produced EPOR-mCitrine is a useful in vitro tool for measuring EPO binding. 2026-06-30T15:00:00Z