https://scholar.dgist.ac.kr/handle/20.500.11750/888 2026-06-03T20:56:11Z https://scholar.dgist.ac.kr/handle/20.500.11750/60356 Title: SLIT2 as a key regulator and therapeutic target in liver injury Author(s): Choi, Yongwon; Choi, Jae-ho; Lee, Young-Sam; Jeong, Jinju; Kang, Eunho; Park, So-hyun; Lee, Young-kyoung; Park, Soon-sang; Kang, Hee-young; Kim, Young-hwa; Park, Tae-jun Abstract: Drug-induced liver injury accounts for approximately 10% of acute hepatitis and up to 50% of acute liver failure. Despite its clinical significance, treatment remains largely limited to cessation of the offending agent. SLIT/ROBO signaling, known for roles in organ development, angiogenesis, leukocyte migration, and cancer metastasis, has demonstrated protective effects against various organ damage. In mouse models of liver injury induced by acetaminophen (APAP), thioacetamide, bile duct ligation, and serum from patients with toxic liver disease, Slit2 expression significantly increases, while Slit1 and Slit3 remain unchanged. Liver-specific Slit2 knockdown exacerbates liver injury, whereas recombinant SLIT2 alleviates liver damage by reducing oxidative stress via CYP2E1 downregulation and suppressing inflammation through nuclear factor κB inhibition. Notably, among ROBO receptors, only ROBO4 was induced in hepatocytes after APAP exposure. ROBO4 knockdown eliminates the hepatoprotective effects of SLIT2, highlighting the importance of SLIT2/BOBO4 signaling in toxic liver injury. Furthermore, the novel Slit2-derived peptide 5 (SP5), designed from the ROBO4-binding LRR2 domain, significantly reduces liver damage and inflammation. Notably, both recombinant SLIT2 and SP5 confer hepatoprotection even when administered 24 h after APAP challenge. These findings suggest that SLIT2/ROBO4-targeted therapies may offer a promising approach for preventing fulminant hepatitis in the context of toxic liver injury. 2026-03-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/59989 Title: Hydrogen Evolution via Oxygen Tolerant [NiFe]-Hydrogenase Immobilized on TiO2 Nanotubes Author(s): Kim, Hwapyong; Kim, Ki Nam; Lee, Sang-Hyeon; Nam, Chang-Hoon; Lee, Young-Sam; In, Su-Il Abstract: [FeFe]-hydrogenase has been of great interest due to its high enzymatic activity for hydrogen evolution reactions (HERs). However, the big challenge of [FeFe]-hydrogenase is a significant performance degradation in aerobic conditions. On the other hand, [NiFe]-hydrogenase of E. coli has an oxygen tolerant property. Therefore, using [NiFe]-hydrogenase is an effective solution to avoid performance degradation in aerobic conditions. Herein, we extracted [NiFe]-hydrogenases from E. coli and immobilized them on the TiO2 nanotube (TNT) electrode prepared by pyrrole-based electropolymerization for application in aerobic conditions. As a result, we can confirm that [NiFe]-hydrogenases coated TNT electrode demonstrates the increased HER activity underaerobic condition than control samples in in-vitro activity test using methylene viologen and linear sweep voltammetry. 2025-12-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/57687 Title: The In vitro reconstituted the lens-specific intermediate filament with filensin and phakinin replicates the genotype-phenotype correlation for cataracts Author(s): Jeong, Jinju; Kwon, Mi Kyung; Nam, Yongho; Lee, Chang-Hun; Lee, Young-Sam Abstract: The intermediate filaments (IFs) family is one of the cyto-skeletons that regulate cell shape, size, stiffness, and movement. Unlike other cytoskeletons such as actin and tubulin, alpha-helical linear proteins of the IFs family constitute filament formation, which can be classified in six types depending on their assembly mechanisms. Filensin and phakinin, which are classified into the type-VI IFs, are only expressed in lens fiber cells and are composed of the lens-specific IFs. However, it is unclear how filensin and phakinin constitute filaments and have an impact on lens properties. Here, we studied the in vitro molecular assembly of human filensin and phakinin to identify the structural and functional relationships. We reconstituted the co-assembled filaments with human recombinant filensin and phakinin and determined its stoichiometry as the ratio of one-to-one. Filensin and phakinin filaments interacted with alpha-crystallin and assembled to make a beeded structure detected by the sedimentation assay and TEM. Moreover, the cataract disease mutant phakinin E233del caused short filaments and reduced resistance against heat and shear stress. We further showed that the alpha-helical rod domains in each protein are involved in the interaction between two proteins, and the intrinsically disordered head and tail domains regulates filament extension. Overall, we determined the molecular interaction in the lens-IFs, which confers the crystalline lens with stability against physical stress. These results suggest that the impaired integrity of the IF can lead to age-related diseases like cataracts and presbyopia. 2024-03-24T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/57310 Title: Brief guide to senescence assays using cultured mammalian cells Author(s): Kang, Eunseok; Kang, Chanhee; Lee, Young-Sam; Lee, Seung-Jae V. Abstract: Cellular senescence is a crucial biological process associated with organismal aging and many chronic diseases. Here, we present a brief guide to mammalian senescence assays, including the measurement of cell cycle arrest, change in cellular morphology, senescence-associated β-galactosidase (SA-β-gal) staining, and the expression of senescence-associated secretory phenotype (SASP). This work will be useful for biologists with minimum expertise in cellular senescence assays. © 2024 The Author(s) 2024-08-31T15:00:00Z