Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
 ...
PMID:Characterization of human thioredoxin-like-1: potential involvement in the cellular response against glucose deprivation. 1643 69

Yeasts are equipped with several putative single-domain thioredoxins located in different subcellular compartments. However, additional proteins containing thioredoxin domains are also encoded by the yeast genomes as described for mammals and other eukaryotic organisms. We report here the characterization of the fission yeast orthologue thioredoxin-like 1 (txl1(+)), which has been previously identified in mammals. Similarly to the human protein, the fission yeast Txl1 is a two-domain protein comprising an N-terminal thioredoxin-like domain and a C-terminal domain of unknown function. Many other yeasts and fungi species contain homologues of txl1(+); however, there is no evidence of txl1(+) orthologues in either Saccharomyces cerevisiae or plants. Txl1 is found in both the nucleus and the cytoplasm of Schizosaccharomyces pombe cells and exhibits a strong reducing activity coupled to thioredoxin reductase. In humans, TXL1 expression is induced by glucose deprivation and overexpression of TXL1 confers resistance against this stress. In contrast, a Sz. pombe Deltatxl1 mutant was not affected in the response against glucose starvation but the Deltatxl1 mutant strain showed a clear hypersensitivity to alkyl hydroperoxide. The mRNA levels of txl1(+) in a h20 strain did not change in response to any oxidative insult (hydrogen peroxide or alkyl hydroperoxide) and the overexpression of an integrated copy of the wild-type txl1(+) gene did not confer a significant increased resistance against alkyl hydroperoxide. Overall, these results indicate that the Txl1 role in the cellular detoxification of alkyl hydroperoxide is exerted through a constitutive transcription of txl1(+).
 ...
PMID:The txl1+ gene from Schizosaccharomyces pombe encodes a new thioredoxin-like 1 protein that participates in the antioxidant defence against tert-butyl hydroperoxide. 1747 1