Lipoprotein lipase-enhanced binding of lipoprotein(a) [Lp(a)] to heparan sulfate is improved by apolipoprotein E (apoE) saturation: secretion-capture process of apoE is a possible route for the catabolism of Lp(a)

Metabolism: Clinical and Experimental
H H van BarlingenT W de Bruin

Abstract

Recently, it has been recognized that cell-bound heparan sulfate (HS) proteoglycans (HSPG) are able to bind and subsequently initiate degradation of lipoproteins. Two mediators of lipoprotein catabolism, both with HS binding capacity, lipoprotein lipase (LPL) and apolipoprotein E (apoE), are involved in this process. This mechanism is known as the secretion-capture process of apoE. Lipoprotein(a) [Lp(a)] was shown to have a strong binding capacity to cell-associated HSPG. This binding capacity was increased by LPL addition. We investigated the effects of recombinant apoE (r-apoE) enrichment of Lp(a) on the binding to HS. Lp(a), isolated by ultracentrifugation and gel filtration, was incubated with r-apoE and reisolated by ultracentrifugation, resulting in r-apoE-enriched Lp(a). ApoE-enriched Lp(a) and control Lp(a) were coated to microtiter plates. The capacity to bind biotin-conjugated HS (b-HS) in the presence or absence of inactivated bovine LPL was studied. R-apoE-enriched Lp(a) showed increased b-HS binding capacity versus control Lp(a). Addition of LPL resulted in an increased b-HS binding capacity of both control and r-apoE-enriched Lp(a). To investigate whether binding of Lp(a) to endothelial cell HSPG occurred in vivo,...Continue Reading

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Citations

Apr 9, 1999·Arteriosclerosis, Thrombosis, and Vascular Biology·V MooserP Nicod
Jul 14, 2005·Chemical Reviews·John M Whitelock, Renato V Iozzo
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