The role of thioredoxin reductase 1 in melanoma metabolism and metastasis

2015 ◽  
Vol 28 (6) ◽  
pp. 685-695 ◽  
Author(s):  
Pamela B. Cassidy ◽  
Matthew Honeggar ◽  
Robyn L. Poerschke ◽  
Karen White ◽  
Scott R. Florell ◽  
...  
Keyword(s):  
Thioredoxin Reductase ◽  
Thioredoxin Reductase 1

scholarly journals System-wide identification and prioritization of enzyme substrates by thermal analysis

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Amir Ata Saei ◽  
Christian M. Beusch ◽  
Pierre Sabatier ◽  
Juan Astorga Wells ◽  
Hassan Gharibi ◽  
...  
Keyword(s):  
Thermal Analysis ◽  
Thioredoxin Reductase ◽  
Structural Level ◽  
Post Translational Modification ◽  
Post Translational Modifications ◽  
Enzyme Substrate ◽  
Thioredoxin Reductase 1 ◽  
Enzyme Substrates ◽  
Substrate Proteins

AbstractDespite the immense importance of enzyme–substrate reactions, there is a lack of general and unbiased tools for identifying and prioritizing substrate proteins that are modified by the enzyme on the structural level. Here we describe a high-throughput unbiased proteomics method called System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA). The approach assumes that the enzymatic post-translational modification of substrate proteins is likely to change their thermal stability. In our proof-of-concept studies, SIESTA successfully identifies several known and novel substrate candidates for selenoprotein thioredoxin reductase 1, protein kinase B (AKT1) and poly-(ADP-ribose) polymerase-10 systems. Wider application of SIESTA can enhance our understanding of the role of enzymes in homeostasis and disease, opening opportunities to investigate the effect of post-translational modifications on signal transduction and facilitate drug discovery.

scholarly journals The Yin and Yang of Nrf2-Regulated Selenoproteins in Carcinogenesis

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Regina Brigelius-Flohé ◽  
Mike Müller ◽  
Doris Lippmann ◽  
Anna Patricia Kipp
Keyword(s):  
Cancer Cells ◽  
Thioredoxin Reductase ◽  
Selenium Deficiency ◽  
Related Factor ◽  
Cellular Defense ◽  
Thioredoxin Reductase 1 ◽  
Cancer Initiation ◽  
Yin And Yang ◽  
Support Tumor Growth

The NF-E2-related factor-2 (Nrf2) is a transcription factor which regulates the major cellular defense systems and thereby contributes to the prevention of many diseases including cancer. Selenium deficiency is associated with a higher cancer risk making also this essential trace element a promising candidate for cancer prevention. Two selenoproteins, thioredoxin reductase-1 (TrxR1) and glutathione peroxidase-2 (GPx2), are targets for Nrf2. Selenium deficiency activates Nrf2 as does a TrxR1 knockout making a synergism between both systems plausible. Although this might hold true for healthy cells, the interplay may turn into the opposite in cancer cells. The induction of the detoxifying and antioxidant enzymes by Nrf2 will make cancer cells chemoresistant and will protect them against oxidative damage. The essential role of TrxR1 in maintaining proliferation makes its upregulation in cancer cells detrimental. The anti-inflammatory potential of GPx2 will help to inhibit cancer initiation and inflammation-triggered promotion, but its growth supporting potential will also support tumor growth. This paper considers beneficial and adverse consequences of the activation of Nrf2 and the selenoproteins which appear to depend on the cancer stage.

Protective role of thioredoxin reductase 1 in cadmium-induced DNA damage

2012 ◽  
Vol 8 (3) ◽  
pp. 289-295 ◽  
Author(s):  
Jee Yeon Park ◽  
Young Ju Lee ◽  
Preeyaporn Koedrith ◽  
Young Rok Seo
Keyword(s):  
Dna Damage ◽  
Thioredoxin Reductase ◽  
Protective Role ◽  
Thioredoxin Reductase 1

scholarly journals System-wide identification and prioritization of enzyme substrates by thermal analysis (SIESTA)

2018 ◽  
Author(s):  
Amir Ata Saei ◽  
Christian M. Beusch ◽  
Pierre Sabatier ◽  
Juan Astorga Wells ◽  
Alexey Chernobrovkin ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Thermal Analysis ◽  
Protein Kinase B ◽  
Thioredoxin Reductase ◽  
Post Translational Modification ◽  
Enzyme Substrate ◽  
Thioredoxin Reductase 1 ◽  
Enzyme Substrates ◽  
Substrate Proteins

AbstractDespite the immense importance of enzyme-substrate reactions, there is a lack of generic and unbiased tools for identifying and prioritizing substrate proteins which are modulated in the structural and functional levels through modification. Here we describe a high-throughput unbiased proteomic method called System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA). The approach assumes that enzymatic post-translational modification of substrate proteins might change their thermal stability. SIESTA successfully identifies several known and novel substrate candidates for selenoprotein thioredoxin reductase 1, protein kinase B (AKT1) and poly-(ADP-ribose) polymerase-10 systems in up to a depth of 7179 proteins. Wider application of SIESTA can enhance our understanding of the role of enzymes in homeostasis and disease, open new opportunities in investigating the effect of PTMs on signal transduction, and facilitate drug discovery.

6537 POSTER Selenite mediated cytotoxcicity in human lung cancer and the role of Thioredoxin reductase 1

2007 ◽  
Vol 5 (4) ◽  
pp. 369
Author(s):  
A.P. Fernandes ◽  
M. Selenius ◽  
A. Capitanio ◽  
O. Brodin ◽  
M. Björnstedt ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Human Lung ◽  
Thioredoxin Reductase ◽  
Human Lung Cancer ◽  
Thioredoxin Reductase 1
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