Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-7-18
pubmed:abstractText
The retinol carrier retinol-binding protein (RBP) forms a complex with the thyroid hormone binding protein transthyretin in the plasma of a number of vertebrate species. The interactions of retinoid-RBP complexes, as well as of unliganded RBP, with transthyretin have been investigated by means of fluorescence anisotropy studies. The presence of two independent and equivalent RBP binding sites per transthyretin molecule has been established for proteins purified from species distant in evolution. Although the natural ligand retinol participates in the interaction between retinol-RBP and transthyretin, its binding to RBP is not a prerequisite for protein-protein interaction. The dissociation constants of human transthyretin binding liganded and unliganded forms of human RBP were determined to be: all-trans retinol-RBP, Kd approximately 0.2 microM; apoRBP, Kd approximately 1.2 microM; all-trans retinoic acid-RBP, Kd approximately 0.8 microM; all-trans retinyl methyl ether-RBP, Kd approximately 6 microM. The complex of RBP with the synthetic retinoid fenretinide, which bears the bulky hydroxyphenyl end group, exhibits negligible affinity for transthyretin. The replacement of RBP-bound retinol with synthetic retinoids affects RBP-transthyretin recognition to an extent that appears to be well correlated with the nature and steric hindrance of the groups substituting the retinol hydroxyl group, consistent with their location at the interface between the contact areas of RBP and transthyretin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents, http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Dansyl Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Fenretinide, http://linkedlifedata.com/resource/pubmed/chemical/Prealbumin, http://linkedlifedata.com/resource/pubmed/chemical/Retinoids, http://linkedlifedata.com/resource/pubmed/chemical/Retinol-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Retinol-Binding Proteins, Plasma, http://linkedlifedata.com/resource/pubmed/chemical/Thyroxine, http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin, http://linkedlifedata.com/resource/pubmed/chemical/Vitamin A, http://linkedlifedata.com/resource/pubmed/chemical/apo-retinol-binding protein, human, http://linkedlifedata.com/resource/pubmed/chemical/dansyl chloride, http://linkedlifedata.com/resource/pubmed/chemical/retinyl methyl ether
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
1294
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
48-54
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Retinoid binding to retinol-binding protein and the interference with the interaction with transthyretin.
pubmed:affiliation
Institute of Biochemical Sciences, Science Faculty, University of Parma, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't