|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
1999-12-6
|
|
pubmed:abstractText |
Human tear lipocalin (TL) is an unusual member of the lipocalin protein family, since it is known to bind a large variety of lipophilic ligands in vivo and acts as a cysteine proteinase inhibitor in vitro. It is suggested to function as a physiological protection factor by scavenging lipophilic potentially harmful compounds. Since protein-protein interaction or macromolecular complexation is a common feature of many lipocalins, we applied phage display technology to identify TL interacting proteins. By panning of a human prostate cDNA phagemid library against purified TL we isolated a thioredoxin (Trx) encoding phage clone. Biochemical analysis revealed that TL indeed interacts with Trx and is reduced by this redox protein. Reduction of the TL-specific disulfide bond is of functional relevance, since the reduced protein shows a nine-fold increase in ligand affinity when tested with retinoic acid as ligand.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/LCN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Lipocalin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Thioredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin,
http://linkedlifedata.com/resource/pubmed/chemical/tear proteins
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
22
|
|
pubmed:volume |
460
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
182-6
|
|
pubmed:dateRevised |
2007-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:10571084-Amino Acid Sequence,
pubmed-meshheading:10571084-Base Sequence,
pubmed-meshheading:10571084-Carrier Proteins,
pubmed-meshheading:10571084-Cloning, Molecular,
pubmed-meshheading:10571084-DNA, Complementary,
pubmed-meshheading:10571084-Disulfides,
pubmed-meshheading:10571084-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10571084-Eye Proteins,
pubmed-meshheading:10571084-Fluorescence,
pubmed-meshheading:10571084-Gene Library,
pubmed-meshheading:10571084-Humans,
pubmed-meshheading:10571084-Ligands,
pubmed-meshheading:10571084-Lipocalin 1,
pubmed-meshheading:10571084-Male,
pubmed-meshheading:10571084-Molecular Sequence Data,
pubmed-meshheading:10571084-Oxidation-Reduction,
pubmed-meshheading:10571084-Protein Binding,
pubmed-meshheading:10571084-Thioredoxins,
pubmed-meshheading:10571084-Tretinoin
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
Phage display reveals a novel interaction of human tear lipocalin and thioredoxin which is relevant for ligand binding.
|
|
pubmed:affiliation |
Institut für Mikrobiologie (Medizinische Fakultät), Universität Innsbruck, Austria. bernhard.redl@uibk.ac.at
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
