TY - JOUR
T1 - Characterization of human thioredoxin-like-1
T2 - Potential involvement in the cellular response against glucose deprivation
AU - Jiménez, Alberto
AU - Pelto-Huikko, Markku
AU - Gustafsson, Jan Åke
AU - Miranda-Vizuete, Antonio
N1 - Funding Information:
This work was supported by the Swedish Medical Research Council (Projects 03P-14096, 03X-14041, and 13X-10370), the Åke Wibergs Stiftelse, the Karolinska Institutet and Medical Research Fund of Tampere University Hospital. A. Jiménez was supported by a postdoctoral fellowship (EX2003-0390) from the Spanish Ministerio de Educación, Cultura y Deporte. We thank Sergio J. Montaño for excellent technical assistance in the preparation of TXL-1 stable clones and Ulla Jukarainen for technical assistance with in situ hybridizations.
PY - 2006/2/6
Y1 - 2006/2/6
N2 - The thioredoxin system, composed of thioredoxin (Trx) and thioredoxin reductase (TrxR), emerges as one of the most important thiol-based systems involved in the maintenance of the cellular redox balance. Thioredoxin-like-1 (TXL-1) is a highly conserved protein comprising an N-terminal Trx domain and a C-terminal domain of unknown function. Here we show that TXL-1 is a substrate for the cytosolic selenoprotein TrxR-1. In situ hybridization experiments demonstrates high expression of Txl-1 mRNA in various areas of central nervous system and also in some reproductive organs. Glucose deprivation, but not hydrogen peroxide treatment, reduced the levels of endogenous TXL-1 protein in HEK-293 cell line. Conversely, overexpression of TXL-1 protects against glucose deprivation-induced cytotoxicity. Taken together, the finding that Txl-1 mRNA is highly expressed in tissues which use glucose as a primary energy source and the modulation of TXL-1 levels upon glucose deprivation indicate that TXL-1 might be involved in the cellular response to sugar starvation stress.
AB - The thioredoxin system, composed of thioredoxin (Trx) and thioredoxin reductase (TrxR), emerges as one of the most important thiol-based systems involved in the maintenance of the cellular redox balance. Thioredoxin-like-1 (TXL-1) is a highly conserved protein comprising an N-terminal Trx domain and a C-terminal domain of unknown function. Here we show that TXL-1 is a substrate for the cytosolic selenoprotein TrxR-1. In situ hybridization experiments demonstrates high expression of Txl-1 mRNA in various areas of central nervous system and also in some reproductive organs. Glucose deprivation, but not hydrogen peroxide treatment, reduced the levels of endogenous TXL-1 protein in HEK-293 cell line. Conversely, overexpression of TXL-1 protects against glucose deprivation-induced cytotoxicity. Taken together, the finding that Txl-1 mRNA is highly expressed in tissues which use glucose as a primary energy source and the modulation of TXL-1 levels upon glucose deprivation indicate that TXL-1 might be involved in the cellular response to sugar starvation stress.
KW - Cell death
KW - Glucose deprivation
KW - Stress
KW - Thioredoxin
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U2 - 10.1016/j.febslet.2006.01.025
DO - 10.1016/j.febslet.2006.01.025
M3 - Article
C2 - 16438969
AN - SCOPUS:31544452809
SN - 0014-5793
VL - 580
SP - 960
EP - 967
JO - FEBS Letters
JF - FEBS Letters
IS - 3
ER -