Evidence that the Receptor for Soluble CD14:LPS Complexes may not be the Putative Signal-Transducing Molecule Associated with Membrane-Bound CD14.

Autor: Haziot, A., Katz, I., Rong, G. W., Lin, X. Y., Silver, J., Goyert, S. M.
Předmět:
Zdroj: Scandinavian Journal of Immunology; Sep1997, Vol. 46 Issue 3, p242-245, 4p, 2 Graphs
Abstrakt: Membrane-bound CD14 acts as a receptor for lipopolysaccharide (LPS) on monocytes/macrophages and neutrophils. Studies have suggested that the activation of monocytes/macrophages by the binding of LPS to membrane-bound CD14 may require the association of a signal-transducing molecule with membrane-bound CD14. The observation that non-CD14 expressing cells, such as endothelial cells, can nevertheless be activated by a complex of LPS and a soluble form of CD 14 (sCD14) suggests that the receptor for this complex may be identical to the signal transducing molecule associated with membrane-bound CD14. The studies described show that two CD14-specific MoAb are able to block the LPS-induced activation of endothelial cells but do not affect the response of monocytes to LPS. This suggests that the interaction of the sCD14:LPS complex with endothelial cells is distinct from the interaction of membrane-bound CD 14 with its putative signal-transducing molecule. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index