Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide

Nakamura, Hajime; Matsuda, Mitsuhiro; Furuke, Keizo; Kitaoka, Yuki; Iwata, S.; Toda, Ken‐ichi; Inamoto, Takashi; Yamaoka, Yoshio; Ozawa, Kazue; Yodoi, Junji

doi:10.1016/0165-2478(94)90038-8

Cited by 229 publications

(90 citation statements)

References 21 publications

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“…Another interesting function of eukaryotic thioredoxin is its stimulation of interleukin 2 receptor expression in human T-cell leukemic virus (HTLV)-1 transformed T cells, an activity originally described as adult T-cell leukemia-derived factor (ADF) (38,39). Recently, recombinant ADF prevented the cytotoxicity caused by H 2 O 2 (40). These results suggest that high cysteine content, as well as the conserved sequences in human Fc␥BP molecules, serves as an anti-oxidant in mucus.…”

Section: Discussionmentioning

confidence: 99%

Human IgGFc Binding Protein (FcγBP) in Colonic Epithelial Cells Exhibits Mucin-like Structure

Harada¹,

Iijima²,

Kobayashi³

et al. 1997

Journal of Biological Chemistry

104

127

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Section: Discussionmentioning

confidence: 99%

Human IgGFc Binding Protein (FcγBP) in Colonic Epithelial Cells Exhibits Mucin-like Structure

Harada¹,

Iijima²,

Kobayashi³

et al. 1997

Journal of Biological Chemistry

104

127

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“…Thioredoxin can regenerate oxidatively damaged proteins in lens epithelial cells (12) and in porcine endothelial cells (13). Further, thioredoxin is resistant to H 2 O 2 -mediated oxidation as compared with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in porcine endothelial cells (14). Thioredoxin overexpression was found to prevent nitric oxide-induced diminution of NO synthase activity in lung endothelial cells (15).…”

mentioning

confidence: 97%

Redox systems of the cell: Possible links and implications

Das

White

2002

Proc. Natl. Acad. Sci. U.S.A.

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“…In addition to its regulatory activity, thioredoxin is suspected to be involved in defence against oxidative stress by its ability to reduce hydrogen peroxide (Spector et al, 1988;Mitsui et al, 1992;Tomimoto et a/., 1993;Nakamura et al, 1994) and by its thiol redox control in repair of oxidatively inactivated proteins (Fernando et al, 1992;Natsuyama et al, 1992). Thioredoxin has also been reported to act as the physiological hydrogen donor for the antioxidant activity of yeast peroxidase (Chae et al, 1994).…”

Section: P a S T E R N A K A N D O T H E R Smentioning

confidence: 99%

Thioredoxin is Essential for Rhodobacter Sphaeroides Growth by Aerobic and Anaerobic Respiration

et al. 1997

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To investigate the biological role of thioredoxin in the facultative photosynthetic bacterium Rhodobacfer sphaeroides, attempts were made to construct a thioredoxin-def icient mutant by site-specif ic mutagenesis, using the Tn903 kanamycin resistance gene for selection. In situ and Southern hybridization analyses have demonstrated that the TmA-mutation is lethal for R. sphaeroides growth under anaerobic conditions with DMSO as terminal electron acceptor and under aerobic conditions. In addition, the DNA region upstream of the trxA initiation codon is essential for aerobic growth of R.sphaeroides. An ORF of unknown function was identified in this region and is suggested to encode a product essential for aerobic metabolism of R. sphaeroides. The mechanism of thioredoxin action was also analysed by using the procedure for gene replacement to introduce a Cys33 to Ser mutation into the trxA chromosomal copy. The strain carrying this mutation produced a thioredoxin impaired in its protein-disulfide reductase activity and was also not viable. These data suggest that the physiological function of R. sphaeroides thioredoxin is redox-dependent. Thioredoxin purified from R. sphaeroides was shown to have a glutathione-disulf ide oxidoreductase activity typical of glutaredoxins. This unexpected finding suggests that R. sphaeroides thioredoxin, in contrast to Escherichia coli thioredoxin, has the potential to act in GSH-dependent processes. Thus, the fundamental role of R. sphaeroides thioredoxin in cell growth probably originates from the multiple functions it can serve in wivo.

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Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide

Cited by 229 publications

References 21 publications

Human IgGFc Binding Protein (FcγBP) in Colonic Epithelial Cells Exhibits Mucin-like Structure

Human IgGFc Binding Protein (FcγBP) in Colonic Epithelial Cells Exhibits Mucin-like Structure

Redox systems of the cell: Possible links and implications

Thioredoxin is Essential for Rhodobacter Sphaeroides Growth by Aerobic and Anaerobic Respiration

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