Title
Binding of β-VLDL to heparan sulfate proteoglycans requires lipoprotein lipase, whereas apoE only modulates binding affinity
Author
de Beer, F.
Hendriks, W.L.
van Vark, L.C.
Kamerling, S.W.A.
van Dijk, K.W.
Hofker, M.H.
Smelt, A.H.M.
Havekes, L.M.
Gaubius instituut TNO
Publication year
1999
Abstract
The binding of β-VLDL to heparan sulfate proteoglycans (HSPG) has been reported to be stimulated by both apoE and lipoprotein lipase (LPL). In the present study we investigated the effect of the isoform and the amount of apoE per particle, as well as the role of LPL on the binding of β-VLDL to HSPG. Therefore, we isolated β-VLDL from transgenic mice, expressing either APOE*2(Arg158→Cys) or APOE*3-Leiden (E2-VLDL and E3Leiden-VLDL, respectively), as well as from apoE-deficient mice containing no apoE at all (Enull-VLDL). In the absence of LPL, the binding affinity and maximal binding capacity of all β-VLDL samples for HSPG-coated microtiter plates was very low. Addition of LPL to this cell-free system resulted in a 12- to 55-fold increase in the binding affinity and a 7- to 15-fold increase in the maximal binding capacity (B(max)). In the presence of LPL, the association constant (K(a)) tended to increase in the order Enull-VLDL
Subject
Biology
β-VLDL
apoE
Heparan sulfate proteoglycans
Lipoprotein lipase
Animals
Apolipoprotein E2
Apolipoprotein E3
Apolipoproteins E
Arteriosclerosis
Binding, Competitive
Cell Line
Cholesterol, VLDL
Heparan Sulfate Proteoglycans
Iodine Radioisotopes
Lipoprotein Lipase
Macrophages
Mice
Mice, Knockout
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DOI
https://doi.org/10.1161/01.atv.19.3.633
TNO identifier
234960
ISSN
1079-5642
Source
Arteriosclerosis, Thrombosis, and Vascular Biology, 19 (3), 633-637
Document type
article