Apolipoprotein E-binding proteins isolated from dog and human liver. 1988

U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
Medizinische Kernklinik and Poliklinik, Universitätskrankenhaus Eppendorf, Hamburg, Federal Republic of Germany.

Chylomicron remnant catabolism appears to be mediated by apolipoprotein (apo) E binding to hepatic lipoprotein receptors. Previously, the apo B,E(LDL) receptor and a unique apo E-binding protein (referred to as the apo E receptor) were isolated from solubilized canine and human livers. In the present study, the apo E-binding fraction was further characterized and found to contain at least three proteins, all of which bind apo E-containing lipoproteins with high affinity. The 56-kDa band was found to contain the alpha- and beta-subunits of F1-ATPase, presumably derived from mitochondrial membranes. In addition, an apo E-binding protein with an apparent Mr approximately equal to 59,000 was identified. The 59-kDa protein displays calcium-independent binding on ligand blots, but displays both calcium-dependent and -independent binding in assays performed with detergent-solubilized protein. The 59-kDa protein recognized lipid-free as well as lipid-bound apo E in ligand blots, and also bound apo E-2, apo E-3, and apo E-4 in a comparable way. Monoclonal antibodies produced against the 59-kDa protein did not react with the 56-kDa proteins. Normal human liver, as well as the liver of a patient lacking the apo B,E(LDL) receptor, possessed the 56-kDa and 59-kDa proteins. These data indicate that liver cells possess at least three proteins, in addition to the apo B,E(LDL) receptor, that bind apo E-containing lipoproteins with high affinity. The physiological role of these proteins in apo E metabolism remains to be determined.

UI MeSH Term Description Entries
D007118 Immunoassay A technique using antibodies for identifying or quantifying a substance. Usually the substance being studied serves as antigen both in antibody production and in measurement of antibody by the test substance. Immunochromatographic Assay,Assay, Immunochromatographic,Assays, Immunochromatographic,Immunoassays,Immunochromatographic Assays
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011956 Receptors, Cell Surface Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands. Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D002847 Chromatography, Agarose A method of gel filtration chromatography using agarose, the non-ionic component of agar, for the separation of compounds with molecular weights up to several million. Chromatography, Sepharose,Agarose Chromatography,Sepharose Chromatography,Agarose Chromatographies,Chromatographies, Agarose,Chromatographies, Sepharose,Sepharose Chromatographies
D002848 Chromatography, DEAE-Cellulose A type of ion exchange chromatography using diethylaminoethyl cellulose (DEAE-CELLULOSE) as a positively charged resin. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) DEAE-Cellulose Chromatography,Chromatography, DEAE Cellulose,DEAE Cellulose Chromatography
D002914 Chylomicrons A class of lipoproteins that carry dietary CHOLESTEROL and TRIGLYCERIDES from the SMALL INTESTINE to the tissues. Their density (0.93-1.006 g/ml) is the same as that of VERY-LOW-DENSITY LIPOPROTEINS. Chylomicron

Related Publications

U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
September 1988, Biochimica et biophysica acta,
U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
October 1983, The Journal of biological chemistry,
U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
June 1984, Scandinavian journal of gastroenterology,
U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
June 1994, Journal of biochemistry,
U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
July 1984, Biochimica et biophysica acta,
U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
April 1981, The Journal of biological chemistry,
U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
March 1986, The Journal of biological chemistry,
U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
February 1986, The Journal of biological chemistry,
U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
April 1996, Experimental neurology,
U Beisiegel, and W Weber, and J R Havinga, and G Ihrke, and D Y Hui, and M E Wernette-Hammond, and C W Turck, and T L Innerarity, and R W Mahley
May 1986, Biochimie,
Copied contents to your clipboard!