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J. Biol. Chem., Vol. 276, Issue 29, 26916-26922, July 20, 2001
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From the Lipoprotein lipase (LPL) efficiently mediates the
binding of lipoprotein particles to lipoprotein receptors and to
proteoglycans at cell surfaces and in the extracellular matrix. It has
been proposed that LPL increases the retention of atherogenic
lipoproteins in the vessel wall and mediates the uptake of lipoproteins
in cells, thereby promoting lipid accumulation and plaque formation. We
investigated the interaction between LPL and low density lipoproteins (LDLs) with special reference to the protein-protein interaction between LPL and apolipoprotein B (apoB). Chemical modification of
lysines and arginines in apoB or mutation of its main proteoglycan binding site did not abolish the interaction of LDL with LPL as shown
by surface plasmon resonance (SPR) and by experiments with THP-I
macrophages. Recombinant LDL with either apoB100 or apoB48 bound with
similar affinity. In contrast, partial delipidation of LDL markedly
decreased binding to LPL. In cell culture experiments, phosphatidylcholine-containing liposomes competed efficiently with LDL
for binding to LPL. Each LDL particle bound several (up to 15) LPL
dimers as determined by SPR and by experiments with THP-I
macrophages. A recombinant NH2-terminal fragment of
apoB (apoB17) bound with low affinity to LPL as shown by SPR, but this interaction was completely abolished by partial delipidation of apoB17.
We conclude that the LPL-apoB interaction is not significant in
bridging LDL to cell surfaces and matrix components; the main interaction is between LPL and the LDL lipids.
Binding of Low Density Lipoproteins to Lipoprotein Lipase Is
Dependent on Lipids but Not on Apolipoprotein B*
§,
,, Wallenberg Laboratory, Göteborg
University, S-41345 Göteborg, Sweden, the ¶ Department of
Medical Biosciences, Umeå University, S-90187 Umeå, Sweden, the
National Institute of Chemical Physics and Biophysics, 12618 Tallinn, Estonia, and the ** Division of Cardiovascular Genetics,
Department of Medicine, The Rayne Institute, University College,
WC1E6JJ London, United Kingdom
*
This work was supported by Swedish Medical Research Council
Grants 12563 and 12203, The Swedish Foundation for Strategic Research, The Swedish Heart-Lung Foundation, The Swedish Royal Academy of Sciences, and the Estonian Science Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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