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J Biol Chem, Vol. 273, Issue 26, 15985-15992, June 26, 1998
From the Departments of This study evaluated whether human
monocyte-derived macrophages synthesize specific types of proteoglycans
with lipoprotein-binding capability that could contribute to lipid
retention in the arterial wall. After labeling with either
[35S]SO4 or
[35S]methionine, macrophages secreted a high molecular
mass proteoglycan, with glycosaminoglycan chains of ~18 kDa and core
protein bands of ~100 and 55 kDa. Both core protein bands were
recognized by an antibody to PG-100, an antibody that recognizes the
proteoglycan form of macrophage colony-stimulating factor
(PG-100/PG-MCSF). The interaction between PG-100/PG-MCSF and low
density lipoproteins (LDL) was examined by gel mobility shift. In this
system, PG-100/PG-MCSF was resolved further into two forms. The two
forms had the same core proteins but differed in their overall size and
glycosaminoglycan content. The larger form contained glycosaminoglycan
chains that were entirely chondroitin ABC lyase-sensitive, whereas the
smaller form contained chains that were sensitive to both chondroitin ABC lyase and heparinase. Both forms bound native LDL with high affinity, but the larger form bound LDL with higher affinity than the
smaller form. The glycosaminoglycan chains of PG-100/PG-MCSF, but not
the core proteins, were responsible for binding to native LDL. Mildly
oxidized LDL and methyl-LDL, which have an electrophoretic charge
similar to that of native LDL, also bound PG-100/PG-MCSF. In contrast,
extensively oxidized LDL and acetyl-LDL, which are more electronegative
than native LDL, did not bind to either form of PG-100/PG-MCSF. The
demonstration of two forms of human monocyte-derived macrophage
PG-100/PG-MCSF which bind LDL may represent an additional role for
macrophages in the extracellular trapping of lipoproteins in
atherosclerosis.
Human Monocyte-derived Macrophages Secrete Two Forms of
Proteoglycan-Macrophage Colony-stimulating Factor That Differ in
Their Ability to Bind Low Density Lipoproteins
,,, and Pathology and
§ Medicine, University of Washington,
Seattle, Washington 98195
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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