English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/38909
Title: Selenoprotein TRXR-1 and GSR-1 are essential for removal of old cuticle during molting in Caenorhabditis elegans
Authors: Stenvall, Jörgen; Fierro-González, Juan Carlos; Swoboda, Peter; Cacho-Valadez, Briseida; Arnér, Elias S. J.; Miranda-Vizuete, Antonio; Tuck, Simon
Keywords: Blotting
Caenorhabditis elegans
Glutathione reductase
Peptide elongation factors
Thioredoxin-disulfide reductase
Issue Date: 18-Jan-2011
Publisher: National Academy of Sciences (U.S.)
Citation: Proceedings of the National Academy of Sciences of the USA 108(3): 1064-1069 (2011)
Abstract: Selenoproteins, in particular thioredoxin reductase, have been implicated in countering oxidative damage occurring during aging but the molecular functions of these proteins have not been extensively investigated in different animal models. Here we demonstrate that TRXR-1 thioredoxin reductase, the sole selenoprotein in Caenorhabditis elegans, does not protect against acute oxidative stress but functions instead together with GSR-1 glutathione reductase to promote the removal of old cuticle during molting. We show that the oxidation state of disulfide groups in the cuticle is tightly regulated during the molting cycle, and that when trxr-1 and gsr-1 function is reduced, disulfide groups in the cuticle remain oxidized. A selenocysteine-to-cysteine TRXR-1 mutant fails to rescue molting defects. Furthermore, worms lacking SELB-1, the C. elegans homolog of Escherichia coli SelB or mammalian EFsec, a translation elongation factor known to be specific for selenocysteine in E. coli, fail to incorporate selenocysteine, and display the same phenotype as those lacking trxr-1. Thus, TRXR-1 function in the reduction of old cuticle is strictly selenocysteine dependent in the nematode. Exogenously supplied reduced glutathione reduces disulfide groups in the cuticle and induces apolysis, the separation of old and new cuticle, strongly suggesting that molting involves the regulated reduction of cuticle components driven by TRXR-1 and GSR-1. Using dauer larvae, we demonstrate that aged worms have a decreased capacity to molt, and decreased expression of GSR-1. Together, our results establish a function for the selenoprotein TRXR-1 and GSR-1 in the removal of old cuticle from the surface of epidermal cells.
Description: 6 páginas, 5 figuras.-- et al.
Publisher version (URL): http://dx.doi.org/10.1073/pnas.1006328108
URI: http://hdl.handle.net/10261/38909
DOI: 10.1073/pnas.1006328108
ISSN: 0027-8424
E-ISSN: 1091-6490
References: PMID:21199936
Appears in Collections:(IBIS) Artículos
(CABD) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record

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