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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
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pubmed:dateCreated |
1991-1-17
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pubmed:abstractText |
The low density lipoproteins (LDL) from patients with Tangier disease are enriched in triglycerides, 27% of LDL mass versus 7% for normal LDL. To study whether this unique LDL core lipid composition affects the surface disposition of apolipoprotein (apo) B-100, we analyzed the LDL by protease digestion and in competitive radioimmunoassays. Limited proteolytic digestion of Tangier LDL by Staphylococcus aureus V8 protease generated a prominent fragment of 120 kDa (cleavage site at residue 1076), which was not visible in similarly digested normal LDL. In competitive radioimmunoassay, Tangier LDL bound weakly to the apoB-specific monoclonal antibody MB20, compared with control LDL. We localized the MB20 epitope between residues 1031 and 1084 of apoB-100, probably very near residue 1076. DNA sequencing of exon 21 of apoB genomic clones (coding for residues 1014-1084) from a Tangier patient revealed no difference from the normal DNA sequence, thus eliminating a protein polymorphism as a basis for the altered protease sensitivity and antibody binding. When the triglyceride contents of Tangier LDL were reduced to 10% of mass by incubation with normal high density lipoproteins, production of the 120-kDa fragment by proteolysis decreased and MB20 binding increased in affinity, implying a change toward normal conformation of apoB-100. Thus, using two independent techniques, proteolytic digestion and binding of monoclonal antibodies, we have demonstrated an alternative conformation of apoB-100 in the vicinity of residue 1076, which reflects the content of triglycerides in the LDL particle.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein B-100,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins B,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes,
http://linkedlifedata.com/resource/pubmed/chemical/Triglycerides
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20739-46
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1701170-Amino Acid Sequence,
pubmed-meshheading:1701170-Apolipoprotein B-100,
pubmed-meshheading:1701170-Apolipoproteins B,
pubmed-meshheading:1701170-Base Sequence,
pubmed-meshheading:1701170-Cloning, Molecular,
pubmed-meshheading:1701170-DNA,
pubmed-meshheading:1701170-Epitopes,
pubmed-meshheading:1701170-Humans,
pubmed-meshheading:1701170-Introns,
pubmed-meshheading:1701170-Lipoproteins, LDL,
pubmed-meshheading:1701170-Lymphocytes,
pubmed-meshheading:1701170-Molecular Sequence Data,
pubmed-meshheading:1701170-Oligonucleotide Probes,
pubmed-meshheading:1701170-Protein Conformation,
pubmed-meshheading:1701170-Radioimmunoassay,
pubmed-meshheading:1701170-Reference Values,
pubmed-meshheading:1701170-Tangier Disease,
pubmed-meshheading:1701170-Triglycerides
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pubmed:year |
1990
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pubmed:articleTitle |
Conformation of apolipoprotein B-100 in the low density lipoproteins of tangier disease. Identification of localized conformational response to triglyceride content.
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pubmed:affiliation |
Cardiovascular Research Institute, University of California, San Francisco 94143.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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