English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/66387
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Photoaffinity labeling of the uncoupling protein UCP1 with retinoic acid: ubiquinone favors binding

AuthorsTomás, Paula; Ledesma, Amalia ; Rial, Eduardo
KeywordsUncoupling protein
retinoic acid
photoaffinity labeling
Issue DateAug-2002
CitationFEBS Letters, 526 (1-3) : 63-65 (2002)
AbstractRetinoic acid is a potent activator of the uncoupling protein-1 (UCP1) both at the gene and mitochondrial level. Irradiation with ultraviolet light can be used to directly photolabel proteins with retinoic acid. The procedure has been applied to investigate its interaction with UCP1 isolated from brown adipose tissue mitochondria. All-trans-retinoic acid binds to UCP1 with high affinity and the labeling is only partially protected by guanosine diphosphate. Ubiquinone (UQ) has been described to be an obligatory cofactor for uncoupling protein function and we demonstrate that it greatly increases the affinity of UCP1 for retinoic acid. Data support the notion of a direct interaction between UQ and retinoic acid
Description3 páginas, 3 figuras -- PAGS nros. 63-65
Publisher version (URL)http://dx.doi.org/10.1016/S0014-5793(02)03116-2
Appears in Collections:(CIB) Artículos
Files in This Item:
File Description SizeFormat 
restringido.pdf21,67 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.