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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1989-6-30
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pubmed:abstractText |
We studied binding of T4 to the lipid-complexed apolipoproteins (apo) of high density lipoproteins (HDL), the major lipoprotein carrier of thyroid hormones in human plasma, and to lipid-free apoA-I. HDL isolated from fresh normal plasma by ultracentrifugation (density, 1.063-1.210 g/mL) was photoaffinity labeled with [3,5-(125)I]T4 and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Two bands corresponding to apoA-I (28.3K) and apoC-II or apoC-III (8.6-9.2K) were seen, and their radioactivity decreased by 50-60% when labeled in the presence of 1 mumol/L T4. Photoaffinity labeling of isolated apoA-I also was demonstrated and was decreased 74% by 1 mumol/L T4, suggesting a higher affinity of the lipid-free protein for T4. T4 binding of isolated apoA-I was optimal at pH 7-8, reached a maximum after 1 h at 23 C, and decreased after incubation at 37 C. Scatchard analysis revealed a single T4-binding site with a Ka of 7.5 x 10(7) L/mol at 23 C, pH 8.2. The potency of T4 analogs as inhibitors of T4 binding to isolated apoA-I was L-T4 = D-T4 = triiodothyroacetic acid = L-rT3 much greater than L-T3 much greater than L-thyronine. The binding of T4 to apoA-I was reduced by known inhibitors of T4 binding to serum proteins (diclofenac = mefenamic acid = furosemide = 8-anilinonaphthalene sulfonic acid much greater than dilantin greater than heparin greater than barbital) and by lipids (unsaturated fatty acids greater than cholesterol = cholesterol esters = phospholipids greater than saturated fatty acids = diglycerides = triglycerides). We conclude that the binding of T4 to HDL is mediated by a specific interaction of the hormone with apoA-I and with apoC-II and/or apoC-III. Since the lipid constituents of HDL inhibit T4 binding to apoA-I, the HDL subfraction in plasma that carries most of the HDL-bound T4 should be one with a low lipid content.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein A-I,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins A,
http://linkedlifedata.com/resource/pubmed/chemical/Diclofenac,
http://linkedlifedata.com/resource/pubmed/chemical/Furosemide,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, VLDL,
http://linkedlifedata.com/resource/pubmed/chemical/Mefenamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroid Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroxine,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroxine-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-972X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
68
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1067-72
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2498379-Apolipoprotein A-I,
pubmed-meshheading:2498379-Apolipoproteins A,
pubmed-meshheading:2498379-Autoradiography,
pubmed-meshheading:2498379-Binding Sites,
pubmed-meshheading:2498379-Diclofenac,
pubmed-meshheading:2498379-Furosemide,
pubmed-meshheading:2498379-Lipoproteins, HDL,
pubmed-meshheading:2498379-Lipoproteins, VLDL,
pubmed-meshheading:2498379-Mefenamic Acid,
pubmed-meshheading:2498379-Temperature,
pubmed-meshheading:2498379-Thyroid Hormones,
pubmed-meshheading:2498379-Thyroxine,
pubmed-meshheading:2498379-Thyroxine-Binding Proteins,
pubmed-meshheading:2498379-Time Factors
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pubmed:year |
1989
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pubmed:articleTitle |
Characterization of the binding of thyroxine to high density lipoproteins and apolipoproteins A-I.
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pubmed:affiliation |
Clinical Endocrinology Branch, National Institute of Diabetes, Digestive and Kidney Diseases, Bethesda, Maryland 20892.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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