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J Biol Chem, Vol. 273, Issue 52, 35355-35361, December 25, 1998
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From the Departments of An initial event in atherosclerosis
is the retention of lipoproteins within the intima of the vessel wall.
The co-localization of apolipoprotein (apo) B and proteoglycans within
lesions has suggested that retention is due to lipoprotein interaction
with these highly electronegative glycoconjugates. Both apoB100- and apoB48-containing lipoproteins, i.e. low density
lipoproteins (LDLs) and chylomicron remnants, are atherogenic. This
suggests that retention is due to determinants in the initial 48% of
apoB. To test this, the interaction of an apoB fragment (apoB17), and apoB48- and apoB100- containing lipoproteins with heparin,
subendothelial matrix, and artery wall purified proteoglycans was
studied. ApoB100-containing LDL from humans and human apoB transgenic
mice and apoB48-containing LDLs from apoE knockout mice were used.
Despite the lack of the carboxyl-terminal 52% of apoB, the apoB48-LDL
bound to heparin-affinity gel as well as did apoB100-LDL. An
NH2-terminal fragment containing 17% of full-length apoB
was made using a recombinant adenovirus; apoB17 bound to heparin as
well as did LDL. Monoclonal antibodies against the
NH2-terminal region of apoB decreased apoB100 LDL binding
to heparin, whereas antibodies against the LDL receptor-binding region
did not alter LDL-heparin interaction. The role of the NH2-terminal region of apoB in LDL interaction with matrix
molecules was also assessed. Media containing apoB17 decreased LDL
binding to subendothelial matrix by 42%. Moreover, removal of the
apoB17 by immunoprecipitation abrogated the inhibitory effect of these media. Antibodies to the NH2-terminal region decreased LDL
binding to matrix and dermatan sulfate proteoglycans. Purified apoB17 effectively competed for binding of LDL to artery derived decorin and
to subendothelial matrix. Thus, despite the presence of multiple basic
amino acids near the LDL receptor-binding domain of LDL, the
NH2-terminal region of apoB is sufficient for the
interaction of lipoproteins with glycoconjugates produced by
endothelial and smooth muscle cells. The presence of a
proteoglycan-binding site in the NH2-terminal region of
apoB may explain why apoB48- and apoB100-containing lipoproteins are
equally atherogenic.
Medicine and ** Microbiology,
Columbia University College of Physicians & Surgeons,
New York, New York 10032, the ¶ Department of Pathology, Wake
Forest University School of Medicine, Winston Salem, North Carolina
27157, and the Scripps Research Institute, La Jolla, California
92037
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