NDLI: Familial defective apolipoprotein B-100: low density lipoproteins with abnormal receptor binding.

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Familial defective apolipoprotein B-100: low density lipoproteins with abnormal receptor binding.

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Familial defective apolipoprotein B-100: low density lipoproteins with abnormal receptor binding.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Krauss, R. M. Innerarity, T. L. Weisgraber, K. H. Mahley, R. W. Vega, G. L. Grundy, S. M. Arnold, K. S.
Description	Author Affiliation: Innerarity TL ( Gladstone Foundation Laboratories for Cardiovascular Disease, University of California, San Francisco 94140-0608.);
Abstract	Previous in vivo turnover studies suggested that retarded clearance of low density lipoproteins (LDL) from the plasma of some hypercholesterolemic patients is due to LDL with defective receptor binding. The present study examined this postulate directly by receptor binding experiments. The LDL from a hypercholesterolemic patient (G.R.) displayed a reduced ability to bind to the LDL receptors on normal human fibroblasts. The G.R. LDL possessed 32% of normal receptor binding activity (approximately equal to 9.3 micrograms of G.R. LDL per ml were required to displace 50% of 125I-labeled normal LDL, vs. approximately equal to 3.0 micrograms of normal LDL per ml). Likewise, the G.R. LDL were much less effective than normal LDL in competing with 125I-labeled normal LDL for cellular uptake and degradation and in stimulating intracellular cholesteryl ester synthesis. The defect in LDL binding appears to be due to a genetic abnormality of apolipoprotein B-100: two brothers of the proband possess LDL defective in receptor binding, whereas a third brother and the proband's son have normally binding LDL. Further, the defect in receptor binding does not appear to be associated with an abnormal lipid composition or structure of the LDL: the chemical and physical properties of the particles were normal, and partial delipidation of the LDL did not alter receptor binding activity. Normal and abnormal LDL subpopulations were partially separated from plasma of two subjects by density-gradient ultracentrifugation, a finding consistent with the presence of a normal and a mutant allele. The affected family members appear to be heterozygous for this disorder, which has been designated familial defective apolipoprotein B-100. These studies indicate that the defective receptor binding results in inefficient clearance of LDL and the hypercholesterolemia observed in these patients.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	19
Volume Number	84
Language	English
Publisher	National Academy of Sciences
Publisher Date	1987-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Apolipoproteins B Genetics Receptors, LDL Metabolism Apolipoprotein B-100 Blood Cells, Cultured Fibroblasts Hyperlipoproteinemia Type II Infant Kinetics Lipoproteins, LDL Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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