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TXN (thioredoxin)

Identity

Other namesADF
DKFZp686B1993
MGC61975
SASP
TRDX
TRX
TRX1
Trx
HGNC (Hugo) TXN
LocusID (NCBI) 7295
Location 9q31.3
Location_base_pair Starts at 113006092 and ends at 113018920 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order 9q telomere-3'TXN 5'-centromere.
 
  Chromosome : 9, Location : 9q31.
(Please visit http://www.ncbi.nlm.nih.gov for more details).

DNA/RNA

 
  5 exons of thioredoxin.
(Please visit http://www.ncbi.nlm.nih.gov for more details).
Description 5 exons, 5' part of exon 1 and 3' part of exon 5 are non-coding.
Transcription 508 bps mRNA, transcribed in a telomere to centromere direction. Alternative splicing of human thioredoxin (lacking exon 2 and 3) was reported in cancer cells.
Thioredoxin (TRX/TXN/ADF) expression is induced by a variety of physiochemical stresses, including virus infection, mitogens, UV-irradiation, hydrogen peroxide, ischemia reperfusion and so on. Natural substances including hemin, estrogen, prostaglandins, sulforaphane, and cAMP can also induce the expression and secretion of TRX. Geranylgeranylacetone (GGA), an acyclic polyisoprenoid as anti-ulcer drug, or tert-butylhydroquinone (tBHQ), a xenobiotics, can also induce TRX expression.
The 5' flanking sequence of TRX gene contains a series of stress-responsive elements, antioxidant responsive element (ARE), cAMP responsive element (CRE), xenobiotics responsive element (XRE) and Sp1.

Protein

Note Thioredoxin is a 12 Kda ubiquitous protein that has disulfide-reducing activity. The structural fold of thioredoxin, including redox-active site, is called "TRX-family domain", which is shared by other TRX superfamily proteins.
 
  Active site and conserved domain of thioredoxin.
(Please see http://www.ncbi.nlm.nih.gov for more details).
Description In 1964, thioredoxin, named by one swedish group, was first identified from extracts of Escherichia coli B as hydrogen donor from NADPH to ribonucleotide reductase. Human thioredoxin was originally cloned by a Japanese group as an IL-2Ralpha (CD25) induced factor in HTLV-1 infected T-cell lines and designated as Adult T cell leukemia derived factor (ADF). It was also cloned independently by a French group as an IL-1 like growth factor produced by Epstein-Barr virus-transformed cells.
Thioredoxin is a 12 Kda multifunctional protein with a redox-active site (Cys-Gly-Pro-Cys), which is involved in dithiol/disulfide exchange reaction. Reduced TRX can reduce protein disulfide bonds and oxidized TRX is reduced by NADPH and thioredoxin reductase.
Expression Thioredoxin is ubiquitously expressed in normal tissues or cells. Plasma levels of TRX in normal individuals vary between 10 and 80 ng/mL. The plasma TRX level is elevated in certain human diseases including HIV infection and cancer. As mentioned above, thioredoxin can also be induced by various physiochemical stress and some natural agents or drugs.
Localisation Thioredoxin is mainly localized in the cytoplasm. Under environmental stress, such as UVB irradiation, PMA, H2O2, hypoxia, the cancer drug cisplatin, hemin and so on, it can translocate to the nucleus, possibly participating to the regulation of nuclear transcription factors, such as Ref-1. Thioredoxin can also be secreted in response to oxidative stress and function as a cytokine to alleviate inflammation. The secretion mechanism of thioredoxin remains unclear. Thioredoxin accumulation in the membrane fraction has long been implied by Holmgren's group in 1989. Later it is found to be expressed on the surface of HUVECs (human umbilical vein endothelial cells), including lipid raft which may be involved in redox signalling.
Function Thioredoxin plays an important role in scavenging reactive oxygen intermediates (ROIs) produced in various oxidative stress. Redox-associated signal transduction inside the cell may be attributed to enhanced DNA binding ability of several transcription factors, such as Ref-1, AP-1, NF-kappaB, which have been proved to be modulated directly or indirectly by thioredoxin. Acting as an intracellular reductase, thioredoxin promotes cellular proliferation to alleviate oxidative stress. Besides reducing activity, thioredoxin inhibit apoptosis through direct binding to apoptosis signal regulating kinase-1 (ASK-1). Thioredoxin is essential for early differentiation and morphogenesis of mouse embryo. Thioredoxin-transgenic (TRX-TG) mice are more resistant to oxidative stress and survive longer than normal mice.
Extracellular thioredoxin shows cytokine or chemokine-like effects. It was reported to show mitogenic effects on leukemia cells, which is also dependent on the presence of reducing agents like 2-ME, and the intact active di-thiol site. It was also reported to show cytoprotective effects through suppressing the production of some inflammatory cytokines. Chemotactic effects of thioredoxin was also observed which may be immune cell type specific and dose dependent since TRX in higher concentration (>1 microg/ml) in circulation shows anti-chemotactic effects. How extracellular thioredoxin interacts with potential target proteins at the plasma membrane may be a key for clarifying the complicated mechanisms.
Several TRX-binding proteins have been identified so far. Reduced TRX in cytosol can bind ASK-1, which activate c-Jun N-terminal kinase (JNK) and p38 MAPK kinase pathway and is required for TNF-a-induced apoptosis. TRX also regulates transcription factor by interaction with redox factor 1 (Ref-1), which has a reducing activity and apurine/apyrimidine endonuclease repair activity. TRX was also reported to bind conserved DNA binding domain of glucocorticoid receptor under oxidative conditions to regulate nuclear receptor-mediated signal transduction. More well-known binding partner of TRX is thioredoxin binding protein-2 (TBP-2/TXNIP/VDUP-1). TBP-2 can downregulate the expression and the reducing activity of TRX. TBP-2 shows potent growth suppressive effect and until recently it was reported to be a metabolic mediator of lipid and glucose metabolisms. All these findings suggest that TRX/TBP-2 binding may regulate redox and metabolic responses in vivo.
Homology Thioredoxin is ubiquitously expressed in different organisms. Chicken, mouse, rat and bovine TRXs have also been cloned. Human and other mammalian TRXs contain, in addition to the two cysteins in Trp-Cys32-Gly-Pro-Cys35-Lys, three other Cys redidues, Cys62, Cys69, and Cys73 (numbers are based on human TRX), which are not found in TRX of bacterial origins. The C-terminal Cys73 residue of mammalian TRX is shown to be involved in dimmer formation.
Proteins sharing the similar active sites Cys-Xxx-Yyy-Cys, are called as members of TRX superfamily. TRX-2 is one homologous protein of TRX, which also contains Cys-Gly-Pro-Cys active site. However, TRX-2 is located in mitochondrial with extra N-terminal mitochondrial translocation signal peptide. TRX2 may play an important role in the mitochondria-mediated apotosis. Other TRX superfamilly proteins consist of MIF (macrophage migration inhibitory factor), PDI (protein disulfide isomerase), TMX, glutaredoxin, nucleoredoxin, etc... These proteins have different redox-relative functions in respective cellular compartment.

Implicated in

Entity Various cancers
Note Elevated expression of thioredoxin was reported in various human cancers, including hepatocellular carcinoma, pancreatic, lung, cervical, gastric, colorectal cancer, Adult T cell Leukemia, myeloma, non-Hodgkin lymphoma, and acute lymphocytic leukemia. The overexpression of TRX in cancer cells seems to be associated with the growth promotion of cancer cells, a worse prognosis for patients, and the development of resistance to anti-cancer agents.
However, there is no evidence showing that exogenously administered rhTRX promotes the growth of cancer, although exogenous rhTRX may alleviate local or systemic inflammatory disorders in these cancer patients.
Prognosis In non-small cell lung carcinomas, intracellular TRX expression is indicative of a more aggressive tumor phenotype and worse prognosis.
Oncogenesis Unknown
  
Entity Adult T cell leukemia (ATL), acquired immunodeficiency syndrome (AIDS), hepatitis C virus (HCV), originated from virus infection
Note As mentioned above, human thioredoxin was first cloned as a secreted adult T cell leukemia (ATL) derived factor. Its expression is markedly enhanced in HTLV-I-infected T cells.
The elevated level of plasma thioredoxin was reported in AIDS patients with worse prognosis and inversely correlated with intracellular glutathion level.
In hepatitis C virus infection, serum levels of TRX is also elevated. The serum TRX levels of patients with HCV infection increased with their serum ferritin levels and the progression of liver fibrosis. Furthermore, serum thioredoxin and ferritin are good markers for the efficacy of interferon therapy.
Prognosis As above, the plasma or serum level of thioredoxin is a good marker for oxidative stress associated with virus infection, so as to be possibily used in clinics.
Oncogenesis Unknown.
  

External links

Nomenclature
HGNC (Hugo)TXN   12435
Entrez_Gene (NCBI)TXN  7295  thioredoxin
Cards
AtlasTXNID44354ch9q31
GeneCards (Weizmann)TXN
Ensembl (Hinxton)ENSG00000136810 [Gene_View]  chr9:113006092-113018920 [Contig_View]  TXN [Vega]
AceView (NCBI)TXN
Genatlas (Paris)TXN
SOURCE (Stanford)NM_001244938 NM_003329
Genomic and cartography
GoldenPath (UCSC)TXN  -  9q31.3   chr9:113006092-113018920 -  9q31   [Description]    (hg19-Feb_2009)
EnsemblTXN - 9q31 [CytoView]
Mapping of homologs : NCBITXN [Mapview]
OMIM187700   
Gene and transcription
Genbank (Entrez)AF065241 AF085844 AF276919 AF313911 AK289508
RefSeq transcript (SRS)NM_001244938 NM_003329
RefSeq transcript (Entrez)NM_001244938 NM_003329
RefSeq genomic (SRS)AC_000141 NC_000009 NC_018920 NT_008470 NW_001839236 NW_004078058
RefSeq genomic (Entrez)AC_000141 NC_000009 NC_018920 NT_008470 NW_001839236 NW_004078058
Consensus coding sequences : CCDS (NCBI)TXN
Cluster EST : UnigeneHs.435136 [ SRS ] Hs.435136 [ NCBI ]
CGAP (NCI)Hs.435136
Alternative Splicing : Fast-db (Paris)GSHG0031060
Alternative Splicing GalleryENSG00000136810
Gene ExpressionTXN [ NCBI-GEO ]   TXN [ EBI - ARRAY_EXPRESS ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP10599 (SRS) P10599 (Uniprot)
NextProtP10599
With graphics : InterProP10599
Splice isoforms : SwissVarP10599(Swissvar)
Domaine pattern : Prosite (SRS)THIOREDOXIN_1 (PS00194)    THIOREDOXIN_2 (PS51352)   
Domaine pattern : Prosite (Expaxy)THIOREDOXIN_1 (PS00194)    THIOREDOXIN_2 (PS51352)   
Domains : Interpro (SRS)Thioredoxin    Thioredoxin-like_fold    Thioredoxin_CS    Thioredoxin_domain   
Domains : Interpro (EBI)Thioredoxin    Thioredoxin-like_fold    Thioredoxin_CS    Thioredoxin_domain   
Related proteins : CluSTrP10599
Domain families : Pfam (SRS)Thioredoxin (PF00085)   
Domain families : Pfam (Sanger)Thioredoxin (PF00085)   
Domain families : Pfam (NCBI)pfam00085   
DMDM7295
Blocks (Seattle)P10599
PDB (SRS)1AIU    1AUC    1CQG    1CQH    1ERT    1ERU    1ERV    1ERW    1M7T    1MDI    1MDJ    1MDK    1TRS    1TRU    1TRV    1TRW    1W1C    1W1E    2HSH    2HXK    2IFQ    2IIY    3E3E    3KD0    3M9J    3M9K    3QFA    3QFB    3TRX    4TRX   
PDB (PDBSum)1AIU    1AUC    1CQG    1CQH    1ERT    1ERU    1ERV    1ERW    1M7T    1MDI    1MDJ    1MDK    1TRS    1TRU    1TRV    1TRW    1W1C    1W1E    2HSH    2HXK    2IFQ    2IIY    3E3E    3KD0    3M9J    3M9K    3QFA    3QFB    3TRX    4TRX   
PDB (IMB)1AIU    1AUC    1CQG    1CQH    1ERT    1ERU    1ERV    1ERW    1M7T    1MDI    1MDJ    1MDK    1TRS    1TRU    1TRV    1TRW    1W1C    1W1E    2HSH    2HXK    2IFQ    2IIY    3E3E    3KD0    3M9J    3M9K    3QFA    3QFB    3TRX    4TRX   
PDB (RSDB)1AIU    1AUC    1CQG    1CQH    1ERT    1ERU    1ERV    1ERW    1M7T    1MDI    1MDJ    1MDK    1TRS    1TRU    1TRV    1TRW    1W1C    1W1E    2HSH    2HXK    2IFQ    2IIY    3E3E    3KD0    3M9J    3M9K    3QFA    3QFB    3TRX    4TRX   
Human Protein AtlasENSG00000136810
HPRD01761
IPIIPI00216298   IPI00552768   
Protein Interaction databases
DIP (DOE-UCLA)P10599
IntAct (EBI)P10599
FunCoupENSG00000136810
REACTOMETXN
Protein Interaction Database7295
BioGRIDTXN
InParanoidP10599
Interologous Interaction database P10599
IntegromeDBTXN
Polymorphism : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)TXN
SNP (GeneSNP Utah)TXN
SNP : HGBaseTXN
Genetic variants : HAPMAPTXN
Somatic Mutations in Cancer : COSMICTXN 
CONAN: Copy Number AnalysisTXN 
Mutations and Diseases : HGMDTXN
OMIM187700   
GENETests187700   
Disease Genetic AssociationTXN
Huge Navigator TXN [HugePedia]  TXN [HugeCancerGEM]
Genomic VariantsTXN  TXN [DGVbeta]
snp3D : Map Gene to Disease7295
General knowledge
Homologs : HomoloGeneTXN
Homology/Alignments : Family Browser (UCSC)TXN
Phylogenetic Trees/Animal Genes : TreeFamTXN
Chemical/Protein Interactions : CTD7295
Chemical/Pharm GKB GenePA37091
Clinical trialTXN
Cancer Resource (Charite)ENSG00000136810
Ontology : AmiGOnegative regulation of transcription from RNA polymerase II promoter  protein binding  extracellular region  nucleoplasm  mitochondrion  cytosol  transcription, DNA-dependent  glycerol ether metabolic process  cellular component movement  signal transduction  cell-cell signaling  cell proliferation  electron carrier activity  response to radiation  protein disulfide oxidoreductase activity  peptide disulfide oxidoreductase activity  nucleobase-containing small molecule interconversion  electron transport chain  regulation of protein import into nucleus, translocation  nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway  positive regulation of DNA binding  small molecule metabolic process  innate immune response  cell redox homeostasis  negative regulation of protein export from nucleus  nucleobase-containing small molecule metabolic process  oxidation-reduction process  
Ontology : EGO-EBInegative regulation of transcription from RNA polymerase II promoter  protein binding  extracellular region  nucleoplasm  mitochondrion  cytosol  transcription, DNA-dependent  glycerol ether metabolic process  cellular component movement  signal transduction  cell-cell signaling  cell proliferation  electron carrier activity  response to radiation  protein disulfide oxidoreductase activity  peptide disulfide oxidoreductase activity  nucleobase-containing small molecule interconversion  electron transport chain  regulation of protein import into nucleus, translocation  nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway  positive regulation of DNA binding  small molecule metabolic process  innate immune response  cell redox homeostasis  negative regulation of protein export from nucleus  nucleobase-containing small molecule metabolic process  oxidation-reduction process  
Other databases
Probes
Litterature
PubMed198 Pubmed reference(s) in Entrez
PubGeneTXN
iHOPTXN

Bibliography

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PMID 17697931
 
TXNIP regulates peripheral glucose metabolism in humans.
Parikh H, Carlsson E, Chutkow WA, Johansson LE, Storgaard H, Poulsen P, Saxena R, Ladd C, Schulze PC, Mazzini MJ, Jensen CB, Krook A, Bjornholm M, Tornqvist H, Zierath JR, Ridderstrale M, Altshuler D, Lee RT, Vaag A, Groop LC, Mootha VK.
PLoS Med. 2007 May;4(5):e158.
PMID 17472435
 
Thioredoxin and thioredoxin binding protein 2 in the liver.
Okuyama H, Son A, Ahsan MK, Masutani H, Nakamura H, Yodoi J.
IUBMB Life. 2008 Oct;60(10):656-60. (REVIEW)
PMID 18636507
 
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Contributor(s)

Written10-2009Zhe Chen, Eiji Yoshihara, Hajime Nakamura, Hiroshi Masutani, Junji Yodoi
Department of Biological Responses, Institute for Virus Research, Kyoto University, Shogoin, Kawahara-cho, Sakyo-ku, Kyoto, Japan

Citation

This paper should be referenced as such :
Chen Z, Yoshihara E, Nakamura H, Masutani H, Yodoi J . TXN (thioredoxin). Atlas Genet Cytogenet Oncol Haematol. October 2009 .
URL : http://AtlasGeneticsOncology.org/Genes/TXNID44354ch9q31.html

This paper is referenced by INIST as such :
http://documents.irevues.inist.fr/bitstream/2042/44832/1/10-2009-TXNID44354ch9q31.pdf   [ Bibliographic record ]

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