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Papers In Press, published online ahead of print May 1, 2003
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Medicine, University of California, San Diego, La Jolla, CA 92093
Corresponding Author: oquehenberger{at}ucsd.edu
In the present study we investigated the mechanisms by which plasma lipoproteins modulate the integrin-dependent adhesion properties of monocytes. LDL induced the expression of monocyte CD11b in vitro as well as in vivo via intracellular signaling mechanisms involving calcium transients. The effect on CD11b transcription was specific for native LDL and was blocked by a neutralizing anti-LDL receptor antibody. Neither oxidized LDL nor HDL had any effect on CD11b expression. Although LDL stimulated CD11b surface expression, the integrins were not activated. To initiate the CD11b-specific adhesion to the endothelium, the engagement of CCR2 and intact chemokine-to-integrin signaling were necessary. However, the activation of CCR2 with monocyte chemoattractant protein-1 not only stimulated the integrins pre-existing on the cell surface but it also increased the number of CD11b molecules on the cell surface. This was particularly pronounced in THP-1 cells after treatment with LDL. In a previous study we showed that LDL induces the expression of CCR2 in monocytes. We conclude that this may be the underlying cause of the enhanced chemokine effect on CD11b expression and activation observed with these cells.
Revised on April 2, 2003
Accepted on April 29, 2003
Low density lipoprotein activates signaling pathways leading to an increase in cytosolic free calcium and stimulation of CD11b expression in monocytes
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