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Science 21 September 1990:
Vol. 249. no. 4975, pp. 1429 - 1431
DOI: 10.1126/science.2402637

Articles

Science, Vol 249, Issue 4975, 1429-1431
Copyright © 1990 by American Association for the Advancement of Science


articles

Structure and function of lipopolysaccharide binding protein

RR Schumann, Leong SR, GW Flaggs, PW Gray, SD Wright, JC Mathison, PS Tobias, and RJ Ulevitch

Department of Immunology, Research Institute of Scripps Clinic, La Jolla, CA 92037.

The primary structure of lipopolysaccharide binding protein (LBP), a trace plasma protein that binds to the lipid A moiety of bacterial lipopolysaccharides (LPSs), was deduced by sequencing cloned complementary DNA. LBP shares sequence identity with another LPS binding protein found in granulocytes, bactericidal/permeability-increasing protein, and with cholesterol ester transport protein of the plasma. LBP may control the response to LPS under physiologic conditions by forming high-affinity complexes with LPS that bind to monocytes and macrophages, which then secrete tumor necrosis factor. The identification of this pathway for LPS-induced monocyte stimulation may aid in the development of treatments for diseases in which Gram-negative sepsis or endotoxemia are involved.


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   Abstract »    Full Text »    PDF »
Identification of meningococcal LPS as a major monocyte activator in IL-10 depleted shock plasmas and CSF by blocking the CD14-TLR4 receptor complex.
A. Bjerre, B. Brusletto, R. Ovstebo, G. B. Joo, P. Kierulf, and P. Brandtzaeg (2003)
Innate Immunity 9, 155-163
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The role of membrane-bound LBP, endotoxin aggregates, and the MaxiK channel in LPS-induced cell activation.
M. Muller, O. Scheel, B. Lindner, T. Gutsmann, and U. Seydel (2003)
Innate Immunity 9, 181-186
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Elevation of Basal Intracellular Calcium as a Central Element in the Activation of Brain Macrophages (Microglia): Suppression of Receptor-Evoked Calcium Signaling and Control of Release Function.
A. Hoffmann, O. Kann, C. Ohlemeyer, U.-K. Hanisch, and H. Kettenmann (2003)
J. Neurosci. 23, 4410-4419
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Characterization of a Single Nucleotide Polymorphism in the Lipopolysaccharide Binding Protein and Its Association with Sepsis.
R. C. Barber and G. E. O'Keefe (2003)
Am. J. Respir. Crit. Care Med. 167, 1316-1320
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Lipoteichoic Acid (LTA) of Streptococcus pneumoniae and Staphylococcus aureus Activates Immune Cells via Toll-like Receptor (TLR)-2, Lipopolysaccharide-binding Protein (LBP), and CD14, whereas TLR-4 and MD-2 Are Not Inv