English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/24663
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:

Divergent expression of type 2 deiodinase and the putative thyroxine-binding protein p29, in rat brain, suggests that they are functionally unrelated proteins

AutorMontero-Pedrazuela, Ana ; Bernal, Juan ; Guadaño-Ferraz, Ana
Fecha de publicaciónmar-2003
EditorEndocrine Society
CitaciónEndocrinology 144(3): 1045-1052 (2003)
ResumenDeiodinases (D1, D2, and D3) are selenoproteins involved in thyroid hormone metabolism. Generation of the active hormone T3, from T4, is carried out by D1 and D2, whereas D3 degrades both hormones. The identity of the cloned D2 as a selenoprotein is well supported by biochemical and physiological data. However, an alternative view has proposed that type 2 deiodinase is a nonselenoprotein complex containing a putative T4 binding subunit called p29, with an almost identity in sequence with the Dickkopf protein Dkk3. To explore a possible functional relationship between p29 and D2, we have compared their mRNA expression patterns in the rat brain. In brain, parenchyma p29 was expressed in neurons. High expression levels were found in all the regions of the blood-cerebrospinal fluid (CSF) barrier. p29 was present in different types of cells than D2, with the exception of the tanycytes. Our data do not support that p29 has a functional relationship with D2. On the other hand, expression of p29 in the blood-CSF barrier suggests that it might be involved in T4 transport to and from the CSF, but further studies are needed to substantiate this hypothesis.
Descripción8 pages, 4 figures.
Versión del editorhttp://dx.doi.org/10.1210/en.2002-220823
Aparece en las colecciones: (IIBM) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Mostrar el registro completo

Artículos relacionados:

NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.