Abstract
In this study we have compared the binding and degradation of human high density lipoprotein (HDL 3), devoid of apolipoprotein E, by rat intestinal (mucosal) and adrenal cells and by human fibroblasts in culture. Binding of HDL 3 to adrenal and intestinal cells was characterised by saturable, specific processes whereas skin fibroblasts from normal humans did not convincingly demonstrate saturability and had a lower affinity and capacity compared with adrenal and intestinal cells. Post-receptor events also appeared to differ. Cells from the adrenal cortex and gut showed similar binding affinities for HDL 3, but the capacity for binding and for degrading HDL 3 was much higher with intestinal cells. The large amounts of HDL degraded by intestinal cells suggest a specific role for the gut in HDL catabolism, and that, in the rat, intestinal cholesterol may be derived from circulating HDL. Finally, it is suggested that rat adrenal cortical and intestinal mucosal cells possess surface receptors for HDL 3 which differ from the LDL receptor.
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More From: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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