DOI: 10.1046/j.1432-1327.2000.01701.x. Physiological functions of thioredoxin and thioredoxin reductase

Physiological functions of thioredoxin and thioredoxin reductase

10.1046/j.1432-1327.2000.01701.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

Thioredoxin, thioredoxin reductase and NADPH, the thioredoxin system, is ubiquitous from Archea to man. Thioredoxins, with a dithiol/disulfide active site (CGPC) are the major cellular protein disulfide reductases; they therefore also serve as electron donors for enzymes such as ribonucleotide reductases, thioredoxin peroxidases (peroxiredoxins) and methionine sulfoxide reductases. Glutaredoxins catalyze glutathione‐disulfide oxidoreductions overlapping the functions of thioredoxins and using electrons from NADPH via glutathione reductase. Thioredoxin isoforms are present in most organisms and mitochondria have a separate thioredoxin system. Plants have chloroplast thioredoxins, which via ferredoxin–thioredoxin reductase regulates photosynthetic enzymes by light. Thioredoxins are critical for redox regulation of protein function and signaling via thiol redox control. A growing number of transcription factors including NF‐κB or the Ref‐1‐dependent AP1 require thioredoxin reduction for DNA binding. The cytosolic mammalian thioredoxin, lack of which is embryonically lethal, has numerous functions in defense against oxidative stress, control of growth and apoptosis, but is also secreted and has co‐cytokine and chemokine activities. Thioredoxin reductase is a specific dimeric 70‐kDa flavoprotein in bacteria, fungi and plants with a redox active site disulfide/dithiol. In contrast, thioredoxin reductases of higher eukaryotes are larger (112–130 kDa), selenium‐dependent dimeric flavoproteins with a broad substrate specificity that also reduce nondisulfide substrates such as hydroperoxides, vitamin C or selenite. All mammalian thioredoxin reductase isozymes are homologous to glutathione reductase and contain a conserved C‐terminal elongation with a cysteine–selenocysteine sequence forming a redox‐active selenenylsulfide/selenolthiol active site and are inhibited by goldthioglucose (aurothioglucose) and other clinically used drugs.

Bibliography

ArnÃ©r, E. S. J., & Holmgren, A. (2000). Physiological functions of thioredoxin and thioredoxin reductase. European Journal of Biochemistry, 267(20), 6102â6109. Portico.

Authors 2

Elias S. J. Arnér (first)
Arne Holmgren (additional)

References 85 Referenced 2,022

10.1002/9780470123096.ch2
10.1146/annurev.bi.54.070185.001321
{'key': 'e_1_2_7_4_2', 'first-page': '121', 'volume-title': 'Chemistry and Biochemistry of Flavoenzymes', 'author': 'Williams C.H. Jr', 'year': '1992'} / Chemistry and Biochemistry of Flavoenzymes by Williams C.H. Jr (1992)
10.1016/S0021-9258(18)71625-6
10.1016/S0969-2126(01)00153-8
10.1016/S0076-6879(99)00129-9
10.1016/s0968-0004(98)01335-8
10.1016/S0021-9258(18)47719-8 / J. Biol. Chem. / Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates by Huber H.E. (1987)
10.1016/S0021-9258(18)66819-X / J. Biol. Chem. / The role of thioredoxin in filamentous phage assembly. Construction, isolation and characterization of mutant thioredoxins by Russel M. (1986)
10.1093/emboj/17.9.2596
10.1126/science.287.5453.655
10.3109/10715769209079515
{'key': 'e_1_2_7_14_2', 'first-page': '229', 'volume-title': 'Oxidative Stress, Cancer, AIDS and Neurodegenerative Diseases', 'author': 'Holmgren A.', 'year': '1998'} / Oxidative Stress, Cancer, AIDS and Neurodegenerative Diseases by Holmgren A. (1998)
10.1073/pnas.91.5.1672
10.1073/pnas.94.8.3633
10.1096/fasebj.10.7.8635688
10.1074/jbc.274.39.27891
10.1006/meth.1996.0424
10.1146/annurev.pharmtox.39.1.67
10.1006/viro.1999.9736
10.1146/annurev.immunol.15.1.351
10.1074/jbc.273.11.6297
10.1074/jbc.272.49.30615
10.1016/S0021-9258(18)35742-9
10.1073/pnas.87.21.8282
10.1016/0167-4781(94)90180-5
{'key': 'e_1_2_7_28_2', 'first-page': '675', 'article-title': 'High rates of thioredoxin secretion correlate with growth arrest in hepatoma cells', 'volume': '55', 'author': 'Rubartelli A.', 'year': '1995', 'journal-title': 'Cancer Res.'} / Cancer Res. / High rates of thioredoxin secretion correlate with growth arrest in hepatoma cells by Rubartelli A. (1995)
10.1016/s0891-5849(97)00429-2
10.4049/jimmunol.163.1.351 / J. Immunol. / Involvement of thioredoxin in rheumatoid arthritis: its costimulatory roles in the TNF‐alpha‐induced production of IL‐6 and IL‐8 from cultured synovial fibroblasts by Yoshida S. (1999)
10.1093/intimm/8.4.603 / Int. Immunol. / Elevation of plasma thioredoxin levels in HIV‐infected individuals by Nakamura H. (1996)
10.4049/jimmunol.156.2.765 / J. Immunol. / Thioredoxin as a potent costimulus of cytokine expression by Schenk H. (1996)
10.1084/jem.189.11.1783
10.1006/excr.1997.3699
10.1016/S0021-9258(18)52988-4 / J. Biol. Chem. / Human eosinophil cytotoxicity‐enhancing factor. Eosinophil‐stimulating and dithiol reductase activities of biosynthetic (recombinant) species with COOH‐terminal deletions by Silberstein D.S. (1993)
10.1016/0008-8749(85)90257-6
10.1002/prot.340110103
10.1016/S0969-2126(96)00079-2
10.1016/S0969-2126(94)00086-7
10.1021/bi00088a023
10.1016/S0969-2126(01)00154-X
10.1042/0264-6021:3390001
10.1074/jbc.275.3.1902
10.1006/bbrc.1997.8003
10.1074/jbc.273.30.19160
10.1006/geno.1996.4493
10.1002/biof.5520100220
10.1074/jbc.272.5.2936
10.1073/pnas.93.3.1006
10.1073/pnas.93.12.6146
10.1111/j.1432-1033.1992.tb17068.x
10.1016/S0021-9258(18)42403-9
10.1016/S0021-9258(18)43889-6
10.1074/jbc.270.20.11761
10.1006/dbio.1996.0208
10.1073/pnas.94.11.5531
10.1074/jbc.m000690200
10.1074/jbc.273.15.8581
10.1073/pnas.100114897
10.1073/pnas.94.8.3621
10.1073/pnas.050579797
10.1074/jbc.274.35.24522
10.1046/j.1432-1327.1999.00286.x
10.1016/s0891-5849(97)00216-5
10.1046/j.1432-1327.1999.00578.x
10.1006/jmbi.1999.3085
{'key': 'e_1_2_7_67_2', 'first-page': '2281', 'article-title': 'Thioredoxin reductase, a redox‐active selenoprotein, is secreted by normal and neoplastic cells: presence in human plasma', 'volume': '60', 'author': 'Söderberg A.', 'year': '2000', 'journal-title': 'Cancer Res.'} / Cancer Res. / Thioredoxin reductase, a redox‐active selenoprotein, is secreted by normal and neoplastic cells: presence in human plasma by Söderberg A. (2000)
10.1042/0264-6021:3470661
10.1016/S0021-9258(18)97742-2
10.1111/j.1432-1033.1968.tb00470.x
10.1016/0076-6879(84)07019-1
10.1093/emboj/17.19.5543
10.1016/S0076-6879(99)00128-7
10.1073/pnas.96.3.887
{'key': 'e_1_2_7_75_2', 'first-page': '91', 'article-title': 'Biochemistry of methionine sulfoxide residues in proteins', 'volume': '3', 'author': 'Brot N.', 'year': '1991', 'journal-title': 'Biofactors'} / Biofactors / Biochemistry of methionine sulfoxide residues in proteins by Brot N. (1991)
10.1046/j.1365-2958.1999.01636.x
10.1074/jbc.274.12.7695
10.1007/BF00408300
10.1016/0003-9861(91)90157-E
10.1016/0891-5849(92)90165-D
10.1093/molehr/4.4.369
10.1152/ajplung.1999.276.3.L530
10.1016/0006-8993(94)90241-0
10.1074/jbc.272.29.18044
10.1016/0888-7543(95)80223-9
10.1016/S0021-9258(19)37617-3

Dates

Type	When
Created	22 years, 5 months ago (March 11, 2003, 12:56 p.m.)
Deposited	1 year, 10 months ago (Oct. 31, 2023, 1:23 a.m.)
Indexed	1 day, 9 hours ago (Sept. 4, 2025, 9:52 a.m.)
Issued	24 years, 11 months ago (Oct. 1, 2000)
Published	24 years, 11 months ago (Oct. 1, 2000)
Published Online	23 years, 8 months ago (Dec. 25, 2001)
Published Print	24 years, 11 months ago (Oct. 1, 2000)

Funders 0

None

BibTeX

@article{Arn_r_2000, title={Physiological functions of thioredoxin and thioredoxin reductase}, volume={267}, ISSN={1432-1033}, url={http://dx.doi.org/10.1046/j.1432-1327.2000.01701.x}, DOI={10.1046/j.1432-1327.2000.01701.x}, number={20}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={Arnér, Elias S. J. and Holmgren, Arne}, year={2000}, month=oct, pages={6102–6109} }

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