A family of lipopolysaccharide binding proteins involved in responses to gram-negative sepsis.
The lipopolysaccharides (LPS) of Gram-negative bacteria initiate potentially fatal processes in many host organisms. Recently published amino acid sequence data suggest that there is a family of LPS binding proteins that may participate in the host response to Gram-negative bacteremia. The first two members of the family to be identified are an LPS binding protein present in serum after an acute phase response in humans, mice, rabbits, and rats and a bactericidal/permeability increasing protein present in the primary granules of human and rabbit neutrophils. LPS binding protein and bactericidal/permeability increasing protein share an ability to bind to LPS, have homologous NH2-terminal amino acid sequences, and are immunologically cross-reactive. Nevertheless, these two molecules differ in their effects on LPS and Gram-negative bacteria, in their sites of biosynthesis, and localization in vivo.
D000210:Acute-Phase Reaction / Q000097:blood; D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins / Q000502:physiology*; D001770:Blood Bactericidal Activity; D001798:Blood Proteins / Q000378:metabolism; D002352:Carrier Proteins / Q000502:physiology*; D003594:Cytoplasmic Granules / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D006090:Gram-Negative Bacteria / Q000502:physiology*; D006801:Humans; D008070:Lipopolysaccharides / Q000378:metabolism / Q000502:physiology*; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000378:metabolism / Q000648:ultrastructure; D010539:Permeability; D011817:Rabbits; D018805:Sepsis / Q000097:blood*; D012689:Sequence Homology, Nucleic Acid
D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins; D001798:Blood Proteins; D002352:Carrier Proteins; D008070:Lipopolysaccharides; D008565:Membrane Proteins; C021623:bactericidal permeability increasing protein