Thioredoxin related protein of 14 kDa (TRP14; also named TXNDC17 for thioredoxin domain-containing protein 17) is a highly conserved and ubiquitously expressed oxidoreductase. It is in parallel with thioredoxin 1 (Trx1, TXN; TXN1) an efficient substrate for the mammalian cytosolic selenoprotein thioredoxin reductase 1 (TrxR1; TXNRD1). However, TRP14 can, in sharp contrast to TXN, not support the activities of ribonucleotide reductase, peroxiredoxins or methionine sulfoxide reductases, thus being unable to directly support cell proliferation or antioxidant defense through these pathways. TRP14 was however shown to efficiently reduce L-cystine, which indirectly can support glutathione synthesis. TRP14 can also suppress NFκB signaling, it was shown to be functionally linked to STAT3 signaling, and it can directly reactivate oxidized phosphotyrosine phosphatase PTP1B. Furthermore, TRP14 can efficiently reduce persulfidated or nitrosylated cysteine residues in many proteins, thereby having the capacity to modulate signaling through hydrogen sulfide or nitric oxide.
Based on this observations my line of research focuses in the characterisation of TRP14 as a unique member of the thioredoxin system and its potential role as dedicated regulator of cellular redox signaling pathways.