https://scholar.dgist.ac.kr/handle/20.500.11750/295 Tue, 27 Oct 2026 05:15:02 GMT 2026-10-27T05:15:02Z https://scholar.dgist.ac.kr/handle/20.500.11750/60994 Title: A Sulfonamide Intermediate Elicits Therapeutic Effect Against Sepsis by Enhancing Neutrophil Maturation Author(s): Park, Ji Ye; Jeong, Yu Sun; Shin, Myeongsu; Choi, Jiwoo; Shin, Jiwon; Kwon, Leezhi; Lyu, Kanghyun; Jo, Hwangi; Byun, Youngjoo; Koo, JaeHyung; Bae, Yoe-Sik Abstract: Sepsis, a life-threatening condition characterized by systemic inflammation and immune dysregulation, remains a major cause of mortality worldwide. Here, we identify a synthetic sulfonamide intermediate, 1-[5-(2-fluorophenyl)furan-2-yl]-N-(4-methylbenzyl)methanamine (FMM), as a host-directed therapeutic candidate that enhances neutrophil maturation and antimicrobial function via autophagy. In a Pseudomonas aeruginosa-induced sepsis model, FMM administration markedly improved survival and attenuated inflammatory cytokine levels while reducing tissue injury and immune cell apoptosis. Furthermore, FMM promoted bone marrow neutrophil maturation, increased reactive oxygen species generation, and enhanced neutrophil extracellular trap formation. FMM also activated GPCR-mediated G beta gamma-PLC signalling, which triggered intracellular calcium and ERK/p38 phosphorylation. Notably, FMM lacked direct bactericidal activity, suggesting its therapeutic effects are mediated by host immune modulation rather than pathogen targeting. Collectively, these findings demonstrate that FMM exerts potent pharmacological effects on neutrophil function and represents a promising lead compound for developing host-directed immunomodulatory therapies for sepsis. Mon, 31 Aug 2026 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/60994 2026-08-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/58513 Title: Protein–Protein Interactions of Odorant and G Protein-Coupled Receptors: A BRET Analysis Approach Author(s): Choi, Ji Woo; Koo, JaeHyung Abstract: Odorant receptors (ORs), the largest subfamily of G protein-coupled receptors, are pivotal not only for olfactory detection in the nose but also for various biological functions in extra-nasal tissues. The functional characterization of ORs presents significant challenges, especially due to the difficulty of achieving their surface expression in in vitro systems. Research indicates that interactions between ORs and other receptors, as well as OR multimerization, are crucial for their membrane localization and the modulation of signaling pathways. Utilizing the bioluminescence resonance energy transfer (BRET) assay, a technique for investigating protein–protein interactions, our study quantifies the interactions between ORs and various receptors. This approach provides novel insights into OR molecular dynamics, emphasizing the role of OR multimerization. By exploring into these complexities, our work aims to enhance the understanding of cellular signaling mechanisms and promote the development of innovative therapeutic strategies. © The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature 2025. Mon, 31 Mar 2025 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/58513 2025-03-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/58512 Title: Image-Based cAMP Sensor Assay for Analyzing Odorant Receptor Activity Author(s): Choi, Ji Woo; Koo, JaeHyung Abstract: Odorant receptors (ORs), the largest subfamily of G-protein-coupled receptors (GPCRs), are transmembrane proteins essential for olfactory perception. Recent research has revealed their expression in nonolfactory tissues, highlighting their potential as novel drug targets. However, the functional analysis of ORs beyond nasal tissues is constrained by limited availability of suitable ligands. Conventional in vitro methods for studying OR–ligand interactions via cAMP often face challenges in large-scale applications. This protocol introduces an advanced cAMP assay employing the Pink Flamindo sensor, a cAMP fluorescence sensor that normally does not exhibit fluorescence but shows fluorescence when combined with cAMP. This enables the real-time visualization of OR–ligand interactions through an imaging-based method. This technique significantly aids in the deorphanization of ORs. Mon, 31 Mar 2025 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/58512 2025-03-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/58362 Title: Yellow Fluorescent Protein Quenching Assay for Analyzing Odorant Receptor Activity Author(s): Choi, Ji Woo; Koo, JaeHyung Abstract: Odorant receptors (ORs), recognized as the largest subfamily of G protein-coupled receptors (GPCR), are increasingly identified as membrane proteins crucial not only in nasal but also in various extra-nasal biological processes. However, researching the functions of these extra-nasal ORs is challenging due to the limited availability of ligands, posing a significant barrier to comprehensive studies. Large-scale screening with in vitro assays, such as the halide-sensitive yellow fluorescent protein (YFP) quenching assay, is crucial for deorphanizing ORs. This protocol employs the YFP quenching assay to identify OR-ligand interactions, thereby advancing OR deorphanization research. © The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature 2025. Mon, 31 Mar 2025 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/58362 2025-03-31T15:00:00Z