title: Influence of CD14, LBP and BPI in the monocyte response to LPS of different polysaccharide chain length.
abstract: In this study we examined the involvement of human serum, recombinant lipopolysaccharide binding protein (rLBP), recombinant (r)CD14, CD14 antibodies and recombinant bactericidal permeability-increasing factor (rBPI) in the induction of TNF by Salmonella minnesota LPS of different polysaccharide chain lengths. Soluble rCD14 and rLBP markedly enhanced LPS 6261 TNF production and to a lesser degree also enhanced TNF production from Re 595 LPS and lipid A DP. Addition of anti-CD14 antibodies resulted in nearly complete inhibition of LPS 6261-induced TNF production and partial inhibition of Re 595 LPS and lipid A DP-induced TNF release. The ability of lipid A MP to induce TNF production increased with addition of rCD14. Addition of rLBP or anti-CD14 antibodies had no detectable effect on lipid A MP-induced TNF production. The effect of rBPI was also tested and the results showed that only the TNF-inducing ability from smooth LPS was completely inhibited by rBPI. Recombinant BPI was considerably less effective in inhibiting Re 595 LPS-induced TNF production, and lipid A DP was not affected by rBPI. Our data suggest that the ability of rLBP, rCD14, CD14 antibodies and rBPI to modulate LPS induced TNF production is strongly dependent on the LPS polysaccharide chain length.
authors.affiliation: Institute of Cancer Research and Molecular Biology, University of Trondheim, Norway.
authors.forename: T G
authors.initials: TG
authors.lastname: Jahr
authors.forename: A
authors.initials: A
authors.lastname: Sundan
authors.forename: H S
authors.initials: HS
authors.lastname: Lichenstein
authors.forename: T
authors.initials: T
authors.lastname: Espevik
mesh_terms: D000209:Acute-Phase Proteins; D000911:Antibodies, Monoclonal / Q000276:immunology; D015703:Antigens, CD / Q000276:immunology / Q000494:pharmacology / Q000502:physiology*; D015214:Antigens, Differentiation, Myelomonocytic / Q000276:immunology / Q000494:pharmacology / Q000502:physiology*; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins / Q000494:pharmacology / Q000502:physiology*; D002352:Carrier Proteins / Q000494:pharmacology / Q000502:physiology*; D002460:Cell Line; D016895:Culture Media, Serum-Free; D006801:Humans; D008050:Lipid A / Q000502:physiology; D018950:Lipopolysaccharide Receptors; D008070:Lipopolysaccharides / Q000096:biosynthesis / Q000737:chemistry* / Q000494:pharmacology; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009000:Monocytes / Q000378:metabolism; D011994:Recombinant Proteins / Q000494:pharmacology; D014409:Tumor Necrosis Factor-alpha / Q000096:biosynthesis / Q000187:drug effects; D000099231:Lipopolysaccharide-Binding Protein
chemical_list: D000209:Acute-Phase Proteins; D000911:Antibodies, Monoclonal; D015703:Antigens, CD; D015214:Antigens, Differentiation, Myelomonocytic; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D002352:Carrier Proteins; D016895:Culture Media, Serum-Free; D008050:Lipid A; D018950:Lipopolysaccharide Receptors; D008070:Lipopolysaccharides; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D011994:Recombinant Proteins; D014409:Tumor Necrosis Factor-alpha; D000099231:Lipopolysaccharide-Binding Protein; C021623:bactericidal permeability increasing protein