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Medical AI Inquiry: You was designed to assist in medical decision-making based on the provided user questions. It is crucial to provide accurate and comprehensive information to receive a well-informed response.  Labels: OBJECTIVE, METHODS, METHODS, METHODS, RESULTS. Meshes: Animals, Anti-Infective Agents, Antimicrobial Cationic Peptides, Blood Bactericidal Activity, Blood Proteins, Cell Line, Endotoxins, Gram-Negative Bacterial Infections, Immunoglobulin G, Lipopolysaccharides, Macrophage Activation, Macrophages, Membrane Proteins, Mice, Recombinant Fusion Proteins, Surgical Wound Infection, Transfection, Tumor Necrosis Factor-alpha.
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Are macrophages expressing a fusion protein derived from bactericidal/permeability-increasing protein and IgG resistant to endotoxin? Context: 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.
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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. Final Decision: yes