Lymphocyte Signaling

Thioredoxin is a small redox protein found in many eukaryotes and prokaryotes. A pair of cysteines within a highly conserved, active site sequence can be oxidized to form a disulfide bond which is then reduced by thioredoxin reductase (1). Multiple forms of thioredoxin have been identified, including cytosolic thioredoxin 1 (Trx1) and mitochondrial thioredoxin 2 (Trx2). Thioredoxin participates in many cellular processes including redox signaling, response to oxidative stress and protein reduction (1). A potential role of thioredoxin in human disorders such as cancer, aging and heart disease is currently under investigation (2). Thioredoxin can play a key role in cancer progression, as it acts as a negative regulator of the proapoptotic kinase ASK1 (3) Changes in thioredoxin expression have been associated with meningococcal septic shock and acute lung injury (4,5).

1. Watson, W.H. et al. (2004) Toxicol. Sci. 78, 3-14.
2. Burke-Gaffney, A. et al. (2005) Trends Pharmacol. Sci. 26, 398-404.
3. Saitoh, M. et al. (1998) EMBO J. 17, 2596-2606.
4. Callister, M.E. et al. (2007) Intensive Care Med. 33, 364-367.
5. Callister, M.E. et al. (2006) Thorax 61, 521-527.

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Thioredoxin 1 Blocking Peptide

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