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Journal of Lipid Research, Vol 38, 1722-1729, Copyright © 1997 by Lipid Research, Inc.
JC Mamputu, AC Desfaits and G Renier
Lipoprotein lipase (LPL)-mediated lipolysis of very low density lipoprotein
(VLDL) has been demonstrated to increase U937 monocyte adhesion to
endothelial cells. In the present study, we evaluated the ability of LPL to
enhance human monocyte adhesion to bovine aortic endothelial cells (BAEC)
in the absence of exogenous lipoproteins. Exposure of BAEC to 1
microgram/ml LPL at 37 degrees C resulted in a significant increase in
monocyte adhesion over control values. Addition of VLDL in the culture
media further enhanced the LPL effect. A significant increase in monocyte
adhesion was also observed when BAEC were incubated with LPL at 4 degrees
C. Heparin or heparinase treatment of BAEC totally abolished the LPL
stimulatory effect on monocyte adhesion. In addition, incubation of
monocytes with heparinase suppressed the ability of LPL to stimulate
monocyte adhesion to endothelial cells. These treatments also markedly
decreased LPL binding to the monocyte and endothelial cell surfaces. In
contrast to native LPL, heat inactivated or phenylmethylsulfonyl fluoride
(PMSF)-treated LPL did not increase monocyte adhesion to BAEC. Finally,
incubation of LPL in the presence of the 5D2 antibody resulted in a total
suppression of the LPL-induced monocyte adhesion to BAEC. Taken together,
these data demonstrate that LPL activity plays an important role in LPL-
induced monocyte adhesion and that LPL binding to heparan sulfate
proteoglycans expressed on both monocytes and endothelial cells surfaces is
required for the enhanced monocyte adhesion. These results suggest a new
mechanism by which LPL may promote the development of atherosclerosis, that
of facilitating monocyte adhesion to the endothelium.
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Lipoprotein lipase enhances human monocyte adhesion to aortic endothelial cells
Louis-Charles Simard Research Center, Notre-Dame Hospital, Department of Nutrition, University of Montreal, Quebec, Canada.
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