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- W2102638245 abstract "To generate a recombinant fusion protein (FP) based on the endotoxin-binding domain of bactericidal/permeability-increasing protein (BPI) and the constant domain of IgG and to test its ability to inhibit lipopolysaccharide (LPS)-induced macrophage tumor necrosis factor alpha (TNF-alpha) secretion.A murine macrophage cell line, RAW 264.7, was transfected with a BPI-IgG FP before incubation with LPS. The amount of LPS-induced TNF-alpha protein secreted was measured and compared with that secreted by cells transfected with a control construct.Basic science research laboratory.Secreted TNF-alpha protein concentration.After transfection, RAW 264.7-cell FP expression was detected in cell lysates and supernatants. At each LPS dose tested, cells transfected with the FP gene secreted less TNF-alpha than did cells transfected with a control construct.The FP possesses substantial antiendotoxin activity, as delineated by inhibition of LPS-induced TNF-alpha secretion by murine macrophages transfected with the fusion gene construct. In the future, such FP may be used as a clinical reagent to reduce the morbidity and mortality associated with serious gram-negative bacterial infections in surgical patients." @default.
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- W2102638245 date "1996-11-01" @default.
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- W2102638245 title "Macrophages Expressing a Fusion Protein Derived From Bactericidal/Permeability-Increasing Protein and IgG Are Resistant to Endotoxin" @default.
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- W2102638245 doi "https://doi.org/10.1001/archsurg.1996.01430230055010" @default.
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