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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1999-6-7
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pubmed:abstractText |
Apo B-100 of LDL can bind to both the LDL receptor and megalin, but the molecular interactions of apo B-100 with these 2 receptors are not completely understood. Naturally occurring mutant forms of apo B may be a source of valuable information on these interactions. Apo B-70.5 is uniquely useful because it contains the NH2-terminal portion of apo B-100, that includes only one of the two putative LDL receptor-binding sites (site A). The lipoprotein containing apo B-70. 5 (Lp B-70.5) was purified from apo B-100/apo B-70.5 heterozygotes by sequential ultracentrifugation combined with immunoaffinity chromatography. Cell culture experiments, ligand blot analysis, and in vivo studies all consistently showed that Lp B-70.5 is not recognized by the LDL receptor. The kidney was identified as a major organ in catabolism of Lp B-70.5 in New Zealand white rabbits. Autoradiographic analysis revealed that renal proximal tubular cells selectively removed Lp B-70.5. On ligand blotting of renal cortical membranes, Lp B-70.5 bound only to megalin. The ability of megalin to mediate cellular endocytosis of Lp B-70.5 was confirmed using retinoic acid/dibutyryl cAMP-treated F9 cells. This study suggests that the putative LDL receptor-binding site A on apo B-100 might not by itself be a functional binding domain and that the apo B-binding sites recognized by the LDL receptor and by megalin may be different. Moreover, megalin may play an important role in renal catabolism of apo B truncations, including apo B-70.5.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10330424-1301956,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10330424-13252080,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10330424-98070
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9738
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1419-30
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10330424-Animals,
pubmed-meshheading:10330424-Apolipoprotein B-100,
pubmed-meshheading:10330424-Apolipoproteins B,
pubmed-meshheading:10330424-Autoradiography,
pubmed-meshheading:10330424-Binding, Competitive,
pubmed-meshheading:10330424-Binding Sites,
pubmed-meshheading:10330424-Cell Line,
pubmed-meshheading:10330424-Heymann Nephritis Antigenic Complex,
pubmed-meshheading:10330424-Humans,
pubmed-meshheading:10330424-Kidney,
pubmed-meshheading:10330424-Membrane Glycoproteins,
pubmed-meshheading:10330424-Peptide Fragments,
pubmed-meshheading:10330424-Rabbits,
pubmed-meshheading:10330424-Receptors, LDL,
pubmed-meshheading:10330424-Transfection
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pubmed:year |
1999
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pubmed:articleTitle |
Truncated apo B-70.5-containing lipoproteins bind to megalin but not the LDL receptor.
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pubmed:affiliation |
Division of Atherosclerosis, Lipid Research and Nutrition, Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA. zchen@imgate.wustl.edu
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pubmed:publicationType |
Journal Article
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