Searched for: subject:"Protein%5C%2BBinding"
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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
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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