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Journal of Endotoxin Research
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The LPS receptor generates inflammatory signals from the cell surface

Eicke Latz

University of Massachusetts Medical School, Division of Infectious Diseases, Worcester, Massachusetts, USA, eicke.latz{at}umassmed.edu

Alberto Visintin

University of Massachusetts Medical School, Division of Infectious Diseases, Worcester, Massachusetts, USA

Egil Lien

University of Massachusetts Medical School, Division of Infectious Diseases, Worcester, Massachusetts, USA

Kate A. Fitzgerald

University of Massachusetts Medical School, Division of Infectious Diseases, Worcester, Massachusetts, USA

Terje Espevik

Norwegian University of Science and Technology, Trondheim, Norway

Douglas T. Golenbock

University of Massachusetts Medical School, Division of Infectious Diseases, Worcester, Massachusetts, USA

Bacterial lipopolysaccharides (LPSs) are recognized in mammals by a receptor complex composed of CD14, Toll-like receptor 4 (TLR4), and MD-2. The mechanism of TLR4 function remains to be elucidated. We constructed chimeric TLR molecules C-terminally fused to fluorescent proteins and stably expressed these chimeric constructs in cells. Confocal microscopy revealed TLR4 to be expressed on the plasma membrane and the Golgi apparatus. Time-lapse confocal imaging showed rapid recycling of TLR4/CD14/MD-2 complexes between the Golgi and the plasma membrane. Membrane TLR4 engagement by antibody was sufficient to induce signaling and pharmacological disruption of the Golgi did not affect cellular responses to LPS. Thus, LPS signaling commences after LPS recognition by surface-expressed TLR4 independent of LPS trafficking to the Golgi.

Journal of Endotoxin Research, Vol. 9, No. 6, 375-380 (2003)
DOI: 10.1177/09680519030090061101
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