Keio University · Medicine
Professor Koichi Fukunaga's research lab focuses on the identification and characterization of endogenous lipid mediators that resolve acute inflammation, particularly in critical illnesses such as acute lung injury (ALI) and severe viral infections like COVID-19. The lab investigates bioactive lipid pathways—such as the metabolism of presqualene diphosphate to presqualene monophosphate—and their roles in regulating immune cell function and inflammation resolution. Using integrative approaches combining experimental disease models, lipidomics, and human genetic studies, the lab aims to uncover novel therapeutic targets for inflammatory and infectious diseases.
Figures are computed from collected data and may differ slightly.
Acute lung injury (ALI) is a severe illness with excess mortality and no specific therapy. In its early exudative phase, neutrophil activation and accumulation in the lung lead to hypoxemia, widespread tissue damage, and respiratory failure. In clinical trials, inhibition of proinflammatory mediators has not proven effective. In this study, we pursued a new investigative strategy that emphasizes mediators promoting resolution from lung injury. A new spontaneously resolving experimental murine mo
Host genetics is a key determinant of COVID-19 outcomes. Previously, the COVID-19 Host Genetics Initiative genome-wide association study used common variants to identify multiple loci associated with COVID-19 outcomes. However, variants with the largest impact on COVID-19 outcomes are expected to be rare in the population. Hence, studying rare variants may provide additional insights into disease susceptibility and pathogenesis, thereby informing therapeutics development. Here, we combined whole
Presqualene diphosphate (PSDP) is a bioactive lipid that rapidly remodels to presqualene monophosphate (PSMP) upon cell activation (Levy, B. D., Petasis, N. A., and Serhan, C. N. (1997) Nature 389, 985-990). Here, we have identified and characterized a phosphatase that converts PSDP to PSMP. Unlike the related polyisoprenyl phosphate farnesyl diphosphate (FDP), PSDP was not a substrate for type 2 lipid phosphate phosphohydrolases. PSDP phosphatase activity was identified in activated human neutr
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