Rate and equilibrium constants for binding of apo-E HDLc (a cholesterol-induced lipoprotein) and low density lipoproteins to human fibroblasts: Evidence for multiple receptor binding of apo-E HDLc
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چکیده
منابع مشابه
Two independent lipoprotein receptors on hepatic membranes of dog, swine, and man. Apo-B,E and apo-E receptors.
We have reported previously that canine livers possess two distinct lipoprotein receptors, an apoprotein (apo)-B,E receptor capable of binding the apo-B-containing low density lipoproteins (LDL) and the apo-E-containing cholesterol-induced high density lipoproteins (HDLc), and an apo-E receptor capable of binding apo-E HDLc but not LDL. Both the apo-B,E and apo-E receptors were found on the liv...
متن کاملStudy of the Binding of Iron and Indium to Human Serum Apo-Transferrin
Indium is a heavy metal belonging to group IIIa. It is believed that indium may interfere with iron metabolism from the sites of absorption, transportation, utilization and storage in the cells. The present investigation was established to study and compare the binding of iron and indium to human apo-transferrin (apo-tf). Pure human apo-tf was used and the binding activity of iron and indium, a...
متن کاملAcetoacetylated lipoproteins used to distinguish fibroblasts from macrophages in vitro by fluorescence microscopy.
We have developed a procedure for labeling lipoproteins with the fluorescent probe 3,3'-dioctadecylindocarbocyanine (Dil) and have used Dil-labeled native and acetoacetylated lipoproteins to differentiate macrophages from fibroblasts in mixed cell culture. Lipoproteins labeled with this probe were suitable for the direct viewing of their binding and internalization by cells in vitro. The labeli...
متن کاملApo A-i and Apo E Interaction: beyond Lipoproteins
Apolipoproteins (Apo) A-I, A-II, A-IV, and E possess repeated amphipathic helical regions with the same genomic structure and are members of a multigene family that probably evolved from a common ancestral gene [1]. These apolipoproteins play pivotal roles in lipid transport and lipoprotein metabolism, and their carboxyl-terminal domain is critical for lipid binding [2]. The purpose of this com...
متن کاملApoprotein (E--A-II) complex of human plasma lipoproteins. II. Receptor binding activity of a high density lipoprotein subfraction modulated by the apo(E--A-II) complex.
Normal human high density lipoproteins (HDL) of the d = 1.063 to 1.125 ultracentrifugal fraction can be separated by Geon-Pevikon block electrophoresis into two subclasses, HDL-I and HDL-II. HDL-I, characterized by the presence of the E apoprotein and the apo(E-A-II) complex along with the A-I and A-II apoproteins, accounted for most, if not all, of the high affinity binding of the human HDL (d...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1979
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.76.5.2311