Characterization and catabolism of rat very high density lipoproteins. 1985

W H Därr, and E E Windler, and K U Stephan, and A K Walli, and H Greten

A previously unrecognized lipoprotein of very high density was isolated from rat serum. During zonal ultracentrifugation of whole serum or of fractions from Sepharose 4B chromatography, a peak comigrating with a peak of cholesterol was found between the typical high density lipoproteins and the residual serum proteins. Centrifugation of chylomicrons, very low density lipoproteins, and high density lipoproteins, radio-iodinated in their lipid and protein moieties and mixed with serum, did not yield this peak. The pooled fractions contained about 85% protein. The remainder was lipid comprising cholesteryl esters, free cholesterol, triglycerides, phosphatidylcholine, and sphingomyelin. Polyacrylamide gel electrophoresis revealed bands in the region of apolipoproteins E and C as the major components. The composition suggested a lipoprotein, and this was substantiated by electron microscopy which showed particles with a mean diameter of 150 A. Their average hydrated density was 1.23 g/ml and the apparent molecular weight was 1.35 X 10(6). These very high density lipoproteins are characterized by a rapid catabolism as compared to high density lipoproteins. Within 10 min, 84% and 70% of intravenously injected 125I-labeled very high density lipoproteins were removed from plasma of male and female rats, respectively, and did not appear to be converted to lipoproteins of a different density class. Ninety-five percent of the removed 125I was recovered in the liver and the radioactivity per gram of tissue was also highest for the liver. Accordingly, the rate of clearance of 125I-labeled very high density lipoproteins was markedly reduced in functionally eviscerated rats. Radioautography revealed that most of the silver grains representing very high density lipoproteins were associated with hepatocytes and only about 1% was found over v. Kupffer cells. Uptake and degradation by freshly isolated rat hepatocytes were mediated by a saturable and specific binding site. Composition and metabolic pathway are compatible with a function of very high density lipoproteins in the transport of protein and lipids to the liver.

UI MeSH Term Description Entries
D008075 Lipoproteins, HDL A class of lipoproteins of small size (4-13 nm) and dense (greater than 1.063 g/ml) particles. HDL lipoproteins, synthesized in the liver without a lipid core, accumulate cholesterol esters from peripheral tissues and transport them to the liver for re-utilization or elimination from the body (the reverse cholesterol transport). Their major protein component is APOLIPOPROTEIN A-I. HDL also shuttle APOLIPOPROTEINS C and APOLIPOPROTEINS E to and from triglyceride-rich lipoproteins during their catabolism. HDL plasma level has been inversely correlated with the risk of cardiovascular diseases. High Density Lipoprotein,High-Density Lipoprotein,High-Density Lipoproteins,alpha-Lipoprotein,alpha-Lipoproteins,Heavy Lipoproteins,alpha-1 Lipoprotein,Density Lipoprotein, High,HDL Lipoproteins,High Density Lipoproteins,Lipoprotein, High Density,Lipoprotein, High-Density,Lipoproteins, Heavy,Lipoproteins, High-Density,alpha Lipoprotein,alpha Lipoproteins
D008297 Male Males
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D011919 Rats, Inbred Strains Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding. August Rats,Inbred Rat Strains,Inbred Strain of Rat,Inbred Strain of Rats,Inbred Strains of Rats,Rat, Inbred Strain,August Rat,Inbred Rat Strain,Inbred Strain Rat,Inbred Strain Rats,Inbred Strains Rat,Inbred Strains Rats,Rat Inbred Strain,Rat Inbred Strains,Rat Strain, Inbred,Rat Strains, Inbred,Rat, August,Rat, Inbred Strains,Rats Inbred Strain,Rats Inbred Strains,Rats, August,Rats, Inbred Strain,Strain Rat, Inbred,Strain Rats, Inbred,Strain, Inbred Rat,Strains, Inbred Rat
D002845 Chromatography Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts. Chromatographies
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D005260 Female Females
D006498 Hepatectomy Excision of all or part of the liver. (Dorland, 28th ed) Hepatectomies
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001053 Apolipoproteins Protein components on the surface of LIPOPROTEINS. They form a layer surrounding the hydrophobic lipid core. There are several classes of apolipoproteins with each playing a different role in lipid transport and LIPID METABOLISM. These proteins are synthesized mainly in the LIVER and the INTESTINES. Apolipoprotein

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