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Structure and function of lipopolysaccharide binding-protein

Academic Article
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Overview

authors

  • Schumann, R. R.
  • Leong, S. R.
  • Flaggs, G. W.
  • Gray, P. W.
  • Wright, S. D.
  • Mathison, J. C.
  • Tobias, Peter
  • Ulevitch, Richard

publication date

  • September 1990

journal

  • Science  Journal

abstract

  • 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.

subject areas

  • Acute-Phase Proteins
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blood Proteins
  • Carrier Proteins
  • Gene Library
  • Humans
  • Kinetics
  • Lipid A
  • Lipopolysaccharides
  • Male
  • Membrane Glycoproteins
  • Molecular Sequence Data
  • Oligonucleotide Probes
  • Rabbits
  • Sequence Homology, Nucleic Acid
  • Sheep
  • Staphylococcus aureus
  • Tumor Necrosis Factor-alpha
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.2402637

PubMed ID

  • 2402637
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Additional Document Info

start page

  • 1429

end page

  • 1431

volume

  • 249

issue

  • 4975

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