| First Author | Schumann RR | Year | 1990 |
| Journal | Science | Volume | 249 |
| Issue | 4975 | Pages | 1429-31 |
| PubMed ID | 2402637 | Mgi Jnum | J:44234 |
| Mgi Id | MGI:1099609 | Doi | 10.1126/science.2402637 |
| Citation | Schumann RR, et al. (1990) Structure and function of lipopolysaccharide binding protein. Science 249(4975):1429-31 |
| abstractText | 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. |
