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Evidence that the Receptor for Soluble CD14:LPS Complexes may not be the Putative Signal‐Transducing Molecule Associated with Membrane‐Bound CD14
Author(s) -
HAZIOT A.,
KATZ I.,
RONG G. W.,
LIN X. Y.,
SILVER J.,
GOYERT S. M.
Publication year - 1997
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1046/j.1365-3083.1997.d01-124.x
Subject(s) - cd14 , receptor , chemistry , membrane , microbiology and biotechnology , molecule , signal (programming language) , biophysics , biology , biochemistry , computer science , organic chemistry , programming language
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 CD14 (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 CD14 with its putative signal‐transducing molecule.