Searched for: subject:"Protein%5C%2BBinding"
(1 - 7 of 7)
document
Westerterp, M. (author), Berbée, J.F.P. (author), Delsing, D.J.M. (author), Jong, M.C. (author), Gijbels, M.J.J. (author), Dahlmans, V.E.H. (author), Offerman, E.H. (author), Romijn, J.A. (author), Havekes, L.M. (author), Rensen, P.C.N. (author), TNO Kwaliteit van Leven (author)
Mice that overexpress human apolipoprotein C-I (apoC-I) homozygously (APOC1+/+ mice) are protected against obesity and show cutaneous abnormalities. Although these effects can result from our previous observation that apoC-I inhibits FFA generation by LPL, we have also found that apoC-I impairs the uptake of a FFA analog in adipose tissue. In...
article 2007
document
Gaubius Instituut TNO (author), Tacken, P.J. (author), de Beer, F. (author), van Vark, L.C. (author), Havekes, L.M. (author), Hofker, M.H. (author), van Dijk, K.W. (author)
The apolipoprotein (apo)E receptor 2 (apoER2) is a recently cloned member of the low-density lipoprotein (LDL) receptor (LDLR) family, showing a high homology with both the LDLR and the very-low-density lipoprotein (VLDL) receptor (VLDLR). In the present study, the binding characteristics of the apoER2 with respect to apoE and lipoprotein lipase...
article 2000
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Gaubius instituut TNO (author), Jong, M.C. (author), Willems-van Dijk, K. (author), Dahlmans, V.E.H. (author), van der Boom, H. (author), Kobayashi, K. (author), Oka, K. (author), Siest, G. (author), Chan, L. (author), Hofker, M.H. (author), Havekes, L.M. (author)
We have shown previously that human apolipoprotein (apo)Cl transgenic mice exhibit hyperlipidaemia, due primarily to an impaired clearance of very-low-density lipoprotein (VLDL) particles from the circulation. In the absence of at least the low-density-lipoprotein receptor (LDLR), it was shown that APOCI overexpression in transgenic mice...
article 1999
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de Man, F.H.A.F. (author), de Beer, F. (author), van der Laarse, A. (author), Smelt, A.H.M. (author), Havekes, L.M. (author), Gaubius Instituut TNO (author)
An in vitro assay to study lipolysis of very low density lipoproteins (VLDL) by heparan sulfate proteoglycan (HSPG-bound lipoprotein lipase (LPL) was developed. Optimal conditions for VLDL lipolysis by HSPG-bound LPL were obtained by incubating plastic wells with 0.5 μg HSPG and 1.5 μg LPL, subsequently. Control experiments with heparinase...
article 1997
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Gaubius instituut TNO (author), Hendriks, W.L. (author), van der Boom, H. (author), van Vark, L.C. (author), Havekes, L.M. (author)
Lipoprotein lipase (LPL) stimulates the uptake of low-density lipoprotein (LDL) and very-low-density lipoprotein (VLDL) in different cell types, including macrophages, through bridging of LPL between lipoproteins and extracellular heparan sulphate proteoglycans (HSPG). Because macrophages produce LPL and because modified lipoproteins are present...
article 1996
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Mulder, M. (author), Lombardi, P. (author), Jansen, H. (author), van Berkel, T.J.C. (author), Frants, R.R. (author), Havekes, L.M. (author), Gaubius Instituut TNO (author)
It has previously been shown that lipoprotein lipase (LPL) enhances the binding of low density lipoproteins (LDL) and very low density lipoproteins (VLDL) to HepG2 cells and fibroblasts, up to 80-fold. This increase in binding is LDL receptor-independent and is due to a bridging of LPL between extracellular heparan sulfate proteoglycans (HSPG)...
article 1993
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Gaubius instituut TNO (author), Havekes, L. (author), van Hinsbergh, V. (author), Kempen, H.J. (author), Emeis, J. (author)
The human hepatoma cell line Hep G2 was studied with respect to metabolism of human low-density lipoprotein (LDL). The Hep G2 cells bind, take up and degrade human LDL with a high-affinity saturable and with a low-affinity non-saturable component. The high-affinity binding possesses a K(D) of 25 nM-LDL and a maximal amount of binding of about 70...
article 1983
Searched for: subject:"Protein%5C%2BBinding"
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