2009
DOI: 10.1074/mcp.m800580-mcp200
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Elucidation of Thioredoxin Target Protein Networks in Mouse

Abstract: Thioredoxin 1 (Trx1) is a key redox modulator that is functionally conserved across a wide range of species, including plants, bacteria, and mammals. Using a conserved CXXC motif, Trx1 catalyzes the reduction of cysteine disulfides and S-nitrosothiols. In contrast to small molecular reductants such as glutathione and cysteine that can reduce a wide range of oxidized proteins, Trx1 reduces only selected proteins via specific protein-protein interaction. Trx1 has been shown to regulate numerous signal transducti… Show more

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Cited by 72 publications
(69 citation statements)
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“…A proteomic analysis of oxidized cardiac proteins reduced by Trx showed many metabolic proteins, suggesting that Trx may play an important role in preventing metabolic dysfunction. 47 The importance of Trx in the heart was investigated using transgenic mice overexpressing a cardiac-specific dominant-negative (Cys32Ser/Cys35Ser) Trx1 mutant. 48 These mice had increased oxidative stress and left ventricular (LV) hypertrophy (LVH) compared with wild-type animals under basal conditions, which was further potentiated after chronic pressure overload, whereas overexpression of wild-type Trx1 had the opposite effect.…”
Section: Thioredoxinmentioning
confidence: 99%
“…A proteomic analysis of oxidized cardiac proteins reduced by Trx showed many metabolic proteins, suggesting that Trx may play an important role in preventing metabolic dysfunction. 47 The importance of Trx in the heart was investigated using transgenic mice overexpressing a cardiac-specific dominant-negative (Cys32Ser/Cys35Ser) Trx1 mutant. 48 These mice had increased oxidative stress and left ventricular (LV) hypertrophy (LVH) compared with wild-type animals under basal conditions, which was further potentiated after chronic pressure overload, whereas overexpression of wild-type Trx1 had the opposite effect.…”
Section: Thioredoxinmentioning
confidence: 99%
“…In addition to being a cytosolic disulfide reductase in the cytosol, Trx1 also translocates to the nucleus and regulates the functions of specific nuclear proteins (2), including nuclear factor B (NFB) (13), activator protein 1 (13), and histone deacetylase 4 (14). In contrast to the broad understanding of Trx1 in regulating cytosolic signal transduction pathways (15)(16)(17), the significance of Trx1 in the nucleus is well documented but poorly understood (18), perhaps because of the relatively transient association of Trx1 with its targets and the relatively low levels of nuclear targets.…”
mentioning
confidence: 99%
“…In the past, proteomics approaches have been used to identify Trx1 targets. Fu et al used the isotope-coded affinity tag approach and identified more than 50 cardiac Trx1 targets from a transgenic mouse model overexpressing Trx1 (15). More recently, Benhar et al coupled the biotin switch technique with stable isotope labeling by amino acids in cell culture (SILAC) to identify 46 substrates of Trx1-mediated denitrosylation (19).…”
mentioning
confidence: 99%
“…81 Also other mammalian class A J-proteins, DNAJA2 (nematode DNJ-19) and DNJA3 (nematode DNJ-10), seem to be regulated by TRX1. 88 As oxidative stress accompanies aging and neurodegenerative diseases, it has been speculated that the inactivation of this class of J-proteins may contribute to the increasing imbalance of proteostasis during aging and disease. 81 Other chaperone family members were also reported to harbor oxidative-sensitive cysteines, such as HSP-1 (e.g., protein folding and dissaggregation 87 ), CCT-4 (subunit of TCP/TriC complex, e.g.…”
Section: Redox-regulation Of Chaperonesmentioning
confidence: 99%