© 1997 American Heart Association, Inc.
Articles |
Lipoprotein Lipase Can Function as a Monocyte Adhesion Protein
From the Division of Preventive Medicine and Nutrition, Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY.
Correspondence to Joseph C. Obunike, PhD, Division of Preventive Medicine, BB 906, Department of Medicine, Columbia University, 630 W 168th St, New York, NY 10032.
Abstract Lipoprotein lipase (LPL) is made by several cell
types, including macrophages within the atherosclerotic lesion.
LPL, a dimer of identical subunits, has high affinity for heparin and
cell surface heparan sulfate proteoglycans (HSPGs). Several studies
have shown that cell surface HSPGs can mediate cell binding to adhesion
proteins. Here, we tested whether LPL, by virtue of its HSPG binding,
could mediate monocyte adhesion to surfaces. Monocyte binding to
LPL-coated (1-25 µg/mL) tissue culture plates was 1.4- to 7-fold
higher than that of albumin-treated plastic. Up to 3-fold more
monocytes bound to the subendothelial matrix that had
been pretreated with LPL. LPL also doubled the number of monocytes that
bound to endothelial cells (ECs). Heparinase and
heparitinase treatment of monocytes or incubation of monocytes with
heparin decreased monocyte binding to LPL. Heparinase/heparitinase
treatment of the matrix also abolished the LPL-mediated increase in
monocyte binding. These results suggest that LPL dimers mediate
monocyte binding by forming a "bridge" between matrix and
monocyte surface HSPGs. Inhibition of LPL activity with
tetrahydrolipstatin, a lipase active-site inhibitor, did
not affect the LPL-mediated monocyte binding. To assess whether
specific oligosaccharide sequences in HSPGs mediated monocyte
binding to LPL, competition experiments were performed by using known
HSPG binding proteins. Neither antithrombin nor thrombin inhibited
monocyte binding to LPL. Next, we tested whether integrins were
involved in monocyte binding to LPL. Surprisingly, monocyte binding to
LPL-coated plastic and matrix was inhibited by 
35% via
integrin-binding arginine-glycine–aspartic acid peptides. This result
suggests that monocyte binding to LPL was mediated, in part, by
monocyte cell surface integrins. In summary, our data show that LPL,
which is present on ECs and in the subendothelial
matrix, can augment monocyte adherence. This increase in
monocyte-matrix interaction could promote macrophage
accumulation within arteries.
Key Words: atherosclerosis • heparin • proteoglycans • integrins • artery
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