Searched for: subject:"Protein%5C%2BBinding"
(1 - 5 of 5)
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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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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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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Lombardi, P. (author), Mulder, M. (author), van der Boom, H. (author), Frants, R.R. (author), Havekes, L.M. (author), Gaubius Instituut TNO (author)
Binding studies at 37 °C showed that lipoprotein lipase-treated very low density lipoproteins (LPL-VLDL) and very low density lipoproteins (VLDL), once taken up via the low density lipoprotein (LDL) receptor, are poorly degraded by HepG2 cells as compared with LDL. Determination of the initial endocytotic rate for LPL-VLDL and VLDL as compared...
article 1993
Searched for: subject:"Protein%5C%2BBinding"
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