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* Department of Medicine, University of California, San Diego, La Jolla, CA 92093
College of Medicine, Asan Medical Center, University of Ulsan, Seoul
1 To whom correspondence should be addressed. e-mail: 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 the 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 chemokine receptor CCR2 and intact chemokine-to-integrin signaling was necessary. However, the activation of CCR2 with monocyte chemoattractant protein-1 not only stimulated the integrins preexisting on the cell surface, but 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.
Abbreviations: Bt2cAMP, dibutyryl-cAMP; [Ca2+]i, intracellular calcium concentration; HUVEC, human umbilical vein endothelial cell; MCP-1, monocyte chemoattractant protein-1; PE, phycoerythrin; TBARS, thiobarbituric acid-reactive substances
Supplementary key words adhesion protein • atherosclerosis • CCR2 • integrin • monocyte recruitment
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