Phage display reveals a novel interaction of human tear lipocalin and thioredoxin which is relevant for ligand binding

29Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.

Abstract

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. Copyright (C) 1999 Federation of European Biochemical Societies.

Cite

CITATION STYLE

APA

Redl, B., Merschak, P., Abt, B., & Wojnar, P. (1999). Phage display reveals a novel interaction of human tear lipocalin and thioredoxin which is relevant for ligand binding. FEBS Letters, 460(1), 182–186. https://doi.org/10.1016/S0014-5793(99)01331-9

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free