Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
26
|
| pubmed:dateCreated |
1991-10-21
|
| pubmed:abstractText |
The sterol binding specificity of rat recombinant liver fatty acid binding protein (L-FABP) and intestinal fatty acid binding protein (I-FABP) was characterized with [3H]cholesterol and a fluorescent sterol analog dehydroergosterol. Ligand binding analysis, fluorescence spectroscopy, and activation of microsomal acyl-CoA:cholesterol acyltransferase activity showed that L-FABP-bound sterols. 1) Lipidex-1000 assay showed a dissociation constant Kd = 0.78 +/- 0.18 microM and stoichiometry of 0.47 +/- 0.16 mol/mol for [3H]cholesterol binding to L-PABP. 2) With [3H]cholesterol/phosphatidylcholine liposomes, the cholesterol binding parameters for L-FABP were Kd = 1.53 +/- 0.28 microM and stoichiometry 0.83 +/- 0.07 mol/mol. 3) L-FABP interaction with dehydroergosterol altered the fluorescence intensity and polarization of dehydroergosterol. Dehydroergosterol bound to L-FABP with Kd = 0.37 microM and a stoichiometry of 0.83 mol/mol. 4) Cholesterol and dehydroergosterol decreased L-FABP tyrosine lifetime. Dehydroergosterol binding produced sensitized emission of bound dehydroergosterol with longer lifetime.5) L-FABP bound two cis-parinaric acid molecules/molecule of protein. Cholesterol displaced one of these bound cis-parinaric acids. 6) L-FABP enhanced acyl-CoA:cholesterol acyltransferase in a concentration-dependent manner. In contrast, these assays indicated that I-FABP did not bind sterols. Thus, L-FABP appears able to bind 1 mol of cholesterol/mol of L-FABP, the L-FABP sterol binding site is equivalent to one of the two fatty acid binding sites, and L-FABP stimulates acyl-CoA:cholesterol acyltransferase by transfer of cholesterol.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Ergosterol,
http://linkedlifedata.com/resource/pubmed/chemical/Fabp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Fabp1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Fabp7 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sterol O-Acyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/dehydroergosterol
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
266
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
17180-6
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:1894612-Animals,
pubmed-meshheading:1894612-Binding Sites,
pubmed-meshheading:1894612-Carrier Proteins,
pubmed-meshheading:1894612-Cholesterol,
pubmed-meshheading:1894612-Ergosterol,
pubmed-meshheading:1894612-Fatty Acid-Binding Proteins,
pubmed-meshheading:1894612-Fatty Acids,
pubmed-meshheading:1894612-Fluorescence Polarization,
pubmed-meshheading:1894612-Intestines,
pubmed-meshheading:1894612-Liposomes,
pubmed-meshheading:1894612-Liver,
pubmed-meshheading:1894612-Neoplasm Proteins,
pubmed-meshheading:1894612-Nerve Tissue Proteins,
pubmed-meshheading:1894612-Rats,
pubmed-meshheading:1894612-Recombinant Proteins,
pubmed-meshheading:1894612-Spectrometry, Fluorescence,
pubmed-meshheading:1894612-Sterol O-Acyltransferase,
pubmed-meshheading:1894612-Tyrosine
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
Selective binding of cholesterol by recombinant fatty acid binding proteins.
|
| pubmed:affiliation |
Department of Pharmacology and Cell Biophysics, University of Cincinnati Medical Center, Ohio 45276-0004.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|