Abstract
A recombinant (r) NH2-terminal fragment of bactericidal/permeability-increasing protein, rBPI23, was shown to inhibit murine macrophage nitric oxide (NO) production elicited by lipopolysaccharide (LPS) plus interferon-gamma (IFN-gamma). Normal mouse plasma amplified NO synthesis (measured as NO2- release) at LPS concentrations of 1-10 ng/mL, and antibody to the plasma LPS-binding protein (LBP) partially inhibited NO2- release in the presence of normal mouse plasma. rBPI23 (1 microgram/mL) effectively inhibited LPS-dependent NO2- release in the presence or absence of normal mouse plasma. Fifty percent inhibition of IFN-gamma/LPS-elicited NO2- production or of binding of fluoresceinated LPS was obtained with approximately 0.2 microgram/mL rBPI23. These results provide a basis for studies of rBPI23 effects on NO synthase activity in murine models of gram-negative sepsis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antimicrobial Cationic Peptides
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Blood Bactericidal Activity / drug effects*
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Blood Proteins / pharmacology*
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Cells, Cultured
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Dose-Response Relationship, Drug
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Female
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Interferon-gamma / pharmacology
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Leishmania enriettii / physiology
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Lipopolysaccharides / metabolism
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Lipopolysaccharides / pharmacology*
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Macrophage Activation
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Macrophages / drug effects
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Macrophages / immunology
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Macrophages / metabolism*
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Macrophages / parasitology
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Membrane Proteins*
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Mice
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Mice, Inbred CBA
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Nitric Oxide / biosynthesis*
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Permeability
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Recombinant Proteins / pharmacology
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Tumor Necrosis Factor-alpha / biosynthesis
Substances
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Antimicrobial Cationic Peptides
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Blood Proteins
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Lipopolysaccharides
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Membrane Proteins
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Recombinant Proteins
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Tumor Necrosis Factor-alpha
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bactericidal permeability increasing protein
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Nitric Oxide
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Interferon-gamma